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Collagen and its derivatives: From structure and properties to their applications in food industry
Abstract
Collagen is the most abundant extracellular matrix protein in food-producing animals. Gelatin is partially degraded collagen. Collagen peptides refer to the peptides with specific properties identified from collagen hydrolysate who produced by hydrolysis of collagen/gelatin. Due to the specific structural and bio- and physical-chemical properties, collagen and its derivatives are used in the field of food industry. In this review, the structure of the collagen molecule and its biosynthetic process in vivo are introduced, and the production methods and structures of gelatin and collagen peptides described. Then the inherent self-assembly property of collagen, the mechanical properties of collagen and gelatin gels, functional properties of collagen and gelatin, and bioactive properties of collagen peptides are reviewed. Finally, the applications of collagen and its derivatives that are correlated with their properties in food industry are summarized. The mechanisms and advantages of the applications of collagen and its derivatives in food industry are raised, and the limitations and challenges of these applications are also discussed. And possible studies to address the challenges of the applications in different areas are indicated.
... Collagen is a complex protein primarily composed of three polypeptide strands, known as α-chains, which together form a triple helix structure (Fig. 2) [35]. This triple helix is characterized by a repetitive Glycine-X-Y (Gly-X-Y) motif, where X is primarily proline (Pro) and Y is primarily hydroxyproline (Hyp) [36,37]. The Gly-X-Y motif ensures that glycine, the smallest amino acid, occupies every third position, allowing it to fit centrally within the helix. ...
... The Gly-X-Y motif ensures that glycine, the smallest amino acid, occupies every third position, allowing it to fit centrally within the helix. The abundance of Pro and Hyp residues facilitates the preorganization of the α-chain into a polyproline II conformation, thus reducing the entropic cost associated with collagen folding [37]. Each α-chain is a single left-handed helix, and the three chains are coiled into a right-handed triple helix [38]. ...
... Each α-chain is a single left-handed helix, and the three chains are coiled into a right-handed triple helix [38]. The stability of this structure is maintained by hydrogen bonds formed [35,37] between the NH 2 group in glycine and the C=O group on the Pro residue of adjacent chains [39,40]. Additionally, the consist of a spiral region and a non-spiral terminal peptide, further contributing to the unique configuration of collagen [41,42]. ...
Collagen, an abundant extracellular matrix protein in food-producing animals, is widely integrated into food systems for its unique physicochemical properties. Oral collagen-based supplements have received increasing attention for their potential to enhance overall well-being. This review aims to provide valuable insights into the application of oral collagen supplements in food systems, promoting their broader use in food processing, preservation, and the development of functional foods. Specifically, the applications of oral collagen-based supplements in functional foods, focusing on their biological activities, health benefits, and functional properties are summarized. Importantly, their molecular mechanisms of biological activities are critically discussed, including antioxidant, angiotensin-converting enzyme inhibitory, and dipeptidyl peptidase IV inhibitory activities. The health benefits of oral collagen-based supplements, particularly in improving skin, immune, and gastrointestinal health are also explored. Additionally, various functional properties of collagen-based supplements are evaluated, including their stability, bioavailability, taste masking, and sensory attributes.
Graphical abstract
... The extraction of marine collagen often requires preparation and pretreatment steps to remove impurities and non-collagenous materials, which are crucial for ensuring the purity and quality of the final products [63]. The preparation of the raw materials varies depending on their nature and involves critical processes such as cleaning, the isolation of collagen-containing components, and size reduction. ...
... Marine gelatin's typical amino acid composition is -Ala-Gly-Pro-Arg-Gly-Glu-Hyp-Gly-Pro-, which may vary depending on the collagen source and processing techniques [1]. Interestingly, partially hydrolyzed collagens or gelatins show gelling, foaming, emulsifying, stabilizing, and film-forming properties, which make them suitable for several food applications [63,106]. For example, Duan et al. [107] reported adding channel catfish skin gelatin into ice cream, resulting in a thicker and smoother texture than ice cream made with bovine gelatin. ...
... Collagen peptides show higher solubility, digestibility, and bioavailability than native collagen and gelatin. However, collagen peptides do not have thickening or gelling properties [63]. Complete hydrolysis (via enzymatic or chemical means) produces collagen peptides. ...
Collagen is a structural protein found in the connective tissues of terrestrial and marine animals. Its diverse functional attributes span its applications in several industries, including food, supplements, cosmetics, and pharmaceuticals. Typically derived from mammalian sources, collagen and its derivatives, including gelatin and collagen peptides, are essential for the food and supplement industries. Recently, marine collagen has emerged as a viable mammalian collagen alternative due to its unique functionality and sustainability. Marine vertebrates and invertebrates are reliable sources of marine collagen. Some marine organisms are promising sustainable sources of collagen for nutritional applications. Recent research highlights significant advances in marine collagen extraction, processing, and novel applications. Hence, recent interest has propelled research in identifying novel collagen sources and advancing technologies to produce marine collagen-based products. Considering the recent scientific interest in marine collagen, this review provides an overview of recent progress in marine collagen production, including novel sources, innovative processing technologies, nutritional and functional properties, safety and quality control, current challenges, and future research directions. The review highlights certain challenges, including unpleasant odor, flavor, color, insufficient supply, and inconsistent quality of marine collagen. Future research should focus on increasing the collagen extraction yield, improving the smell and flavor, and developing novel delivery systems to increase bioavailability and functionality.
... Type II collagen is utilized for its targetability, specifically for cartilage-targeted delivery, since it can also be found at high concentrations in human cartilage. Type III is worth mentioning; however, it is usually combined with Type I collagen for skin regeneration and wound healing [29][30][31]. ...
... Type II collagen is utilized for its targetability, specifically for cartilage-targeted delivery, since it can also be found at high concentrations in human cartilage. Type III is worth mentioning; however, it is usually combined with Type I collagen for skin regeneration and wound healing [29][30][31]. Collagen has numerous advantages for utilization as a drug delivery system. Since it is a natural protein found abundantly in the human body, it is well-tolerated by the immune system, and is thus biocompatible and biodegradable. ...
... The formed matrix can encapsulate drugs, and, at the gel-forming concentrations, a sustained release can usually be achieved, which can be influenced by crosslinking with polymers. Numerous sites can be found in the collagen's structure to offer chemical modification, which is most auspicious for attachment of ligands to achieve targeted drug delivery [29,32]. Despite all these advantages, some disadvantages are also found in the case of collagen. ...
Regenerative medicine is a challenging field in current research and development, whilst translating the findings of novel tissue regenerative agents into clinical application. Protein-based hydrogels are derived from various sources, with animal-derived products being primarily utilized to deliver cells and promote cell genesis and proliferation, thereby aiding in numerous indications, including bone tissue regeneration, cartilage regeneration, spinal cord injury, and wound healing. As biocompatible and biodegradable systems, they are tolerated by the human body, allowing them to exert their beneficial effects in many indications. In this review article, multiple types of animal-derived proteins (e.g., collagen, gelatin, serum albumin, fibrin) were described, and a selection of the recent literature was collected to support the claims behind these innovative systems. During the literature review, special indications were found when applying these hydrogels, including the therapeutic option to treat post-myocardial infarct sites, glaucoma, and others. Maintaining their structure and mechanical integrity is still challenging. It is usually solved by adding (semi)synthetic polymers or small molecules to strengthen or loosen the mechanical stress in the hydrogel’s structure. All in all, this review points out the potential application of value-added delivery systems in regenerative medicine.
... Our study suggests that significant potential for the development of diverse plant milk varieties, such as nut milk, potato milk, rice milk, and bean milk, to meet diverse consumer demands. Additionally, gender-specific preferences observed in our study align with previous research indicating that female consumers prioritize beauty and skincare benefits, while male consumers focus on muscle building and fitness [25,26]. These insights provide valuable guidance for targeted product development and marketing strategies. ...
... We have observed that female consumers showed the greatest interest in plant milk with high dietary fiber, enriched collagen, and probiotics. Collagen supplements have gained significant popularity in the Asian market, particularly among females [25]. Collagen is a protein that plays a crucial role in maintaining skin firmness, elasticity, and hydration, which helps to decrease the wrinkles and sagging skin. ...
... Collagen is a protein that plays a crucial role in maintaining skin firmness, elasticity, and hydration, which helps to decrease the wrinkles and sagging skin. The Asian female consumers who prioritize skincare chasing for collagen supplements appealing for maintaining youthful skin [25]. In addition, probiotics has been reported to benefit the balance of microflora in the digestive tracts, which prevent multiple diseases to the host. ...
Plant milks are considered to be nutritious, sustainable, and vegetarian food products, and they have been the fastest growing beverages in the past decade in China. However, few studies have investigated consumers’ demands and purchase behaviors with respect to plant milks. Through an online questionnaire (n = 1052 valid responses), this study identified the factors that influenced individuals’ purchase intentions, purchase behaviors, attitudes, and demands with respect to current and future plant milk products. Through descriptive analysis and PCA, this study revealed that nutritional value (63.6%), taste (56.3%), and calories (42.8%) were the top three factors that Chinese consumers most cared about regarding plant milks. In the current Chinese market, coconut milk is the most popular plant milk with the highest purchase rate (61.2%), followed by soymilk (53.9%). Male consumers preferred plant milk with higher protein content and fortified with antioxidants, while female consumers preferred plant milk low in calories and enriched with collagen, dietary fiber, and probiotics. Chinese consumers are willing to pay higher prices for plant milks with enhanced nutritional value, improved product quality, and strengthened safety assurances. Innovative forms of plant milk, such as bean milk, rice milk, and quinoa milk, may be developed to satisfy the diversified needs of consumers.
... Structurally, collagen is characterized by three polypeptide chains linked together to form a righthanded triple helix and a motif, (Glycine-X-Y)n, common to all twenty-nine types of collagen, repeated along the chains. The X and Y positions are often occupied by the amino acids proline and hydroxyproline [1][2][3]. ...
... Although the main source of this protein is animal by-products such as beef, pork and poultry, which account for approximately 30% of its protein content, some recent studies have shown other sources of collagen, such as the recycling of industrial, food and fish waste [1,3,10,11]. In this context, the collagen contained in the hides left over from leather processing has aroused interest in various sectors [12,13]. ...
The aim of the study was to extract and characterize collagen from solid untanned skin waste from the processing of leather in a Capra aegagrus tannery. Using pepsin (SPC), 37 g of collagen were obtained from 100 g of dry weight skin. Characterization took place using SDS-PAGE, FTIR and UV absorption techniques, identifying it as type I collagen. The ultraviolet (UV) absorption spectrum showed a peak at 238 nm. In the thermogram, the maximum transition temperature was 56º C. Using the electrophoresis technique, it was observed that SPC consists of band patterns formed by a γ chain, a β chain and two distinct α chains (α1 and α2). In the FTIR analysis, the collagen showed the absorption peaks for the amides, showing that the SPC extraction process maintained the integrity of the molecule. To observe the effect of NaCl concentration on the solubility of SPC, the collagen showed high solubility, up to a concentration of 2% NaCl. The solubility peak was observed at pH 4.0, with a sharp drop until pH 7.0, reaching its minimum point at pH 10. Scanning microscopy showed some irregular surfaces, cavities and fibrous structures, which may favor the application of collagen as a biomaterial. The zeta potential found the isoelectric point of collagen at pH = 6.61. These results indicate that the collagen obtained has a high level of structural integrity and can be applied as an alternative source, as well as adding value to a waste product that is often discarded in the environment.
... These fibril proteins resemble classical collagen, as observed under electron microscopy and are further characterized by a repeating banding pattern. The collagen protein is classified into different types, such as type 1 collagen, which is significantly present in the vasculature, lungs, bone, tendon, cornea, and the skin; type II collagen, widely occurring in cartilage and more specific tissues; type III collagen, mostly present in the elastic tissues such as lungs, skin, embryonic, and blood vessels; type V collagen, very minor collagen mostly associated with collagen type 1 particularly present in high in the cornea of an eye; type XI collagen, quantitatively minor in amount mostly associated with type II collagen [23,24]. ...
... The triplehelical regions of collagen molecules have presented many interruptions, accounting for about half the length of fibrils. Collagen molecule VII, with both α1 (VIII) and α2 (VIII) chains, exists in heterodimer form, while type X collagen is an α1 (X) homotrimer [23,24,26]. ...
Collagen, the primary fibrillar protein found in marine organisms has gained significant attention due to its nutritional and functional properties. It plays a crucial role in food quality and textural attributes, making it a valuable ingredient in various food applications. This study focuses on the interactions of marine-derived collagen and its gelatin derivatives with small bioactive molecules, including phenolic compounds, poly-saccharides, and others, which are briefly discussed. These interactions are governed by mechanisms such as hydrogen bonding, electrostatic forces, hydrophobic interactions, and van der Waals contacts, resulting in the formation of bio-composites with enhanced stability, bioavailability, and functionality. This article also highlights recent advancements in extraction methods, physicochemical characterization, and the role of collagen-based composites in food applications, such as emulsification, stabilization, and microencapsulation. Furthermore , this review also summarizes the challenges related to the lower thermal stability of marine collagen compared to mammalian sources, along with potential solutions through innovative processing techniques. Finally, the article briefly discusses how marine collagen-based bio-composites offer promising prospects for developing functional and sustainable food products.
... Furthermore, it is important to recognize that ECMbased migration represents a classic model of substratedependent cell movement. As a major component of the ECM, collagen offers several inherent advantages, including excellent biocompatibility, low immunogenicity, widespread availability, and ease of modification [36][37][38], [39][40][41] (Scheme 2). Moreover, collagen differs significantly from other materials used to regulate cell migration. ...
Cell migration is a fundamental biological process that plays a crucial role in both physiological and pathological conditions, and is largely influenced by the complex microenvironment, particularly the extracellular matrix (ECM), a macromolecular network that governs various cellular interactions. Extensive research has established that ECM-cell interactions are critical in multiple biological processes, with some directly regulating cell migration. Among ECM components, collagens stand out as key regulators of cell movement. However, existing reviews have provided only limited perspectives on the role of collagen-based biomaterials in directing migration across different cell populations. This gap in knowledge hinders a comprehensive understanding of collagen’s full potential. Drawing from systematic literature and our ongoing research, this review aims to summarize advancements over the past five years in the application of collagen-based biomaterials for modulating cell migration. The discussion primarily focuses on three pivotal cell types: stem cells, immune cells, and cancer cells. By shedding light on the functions, mechanisms, and therapeutic potential of collagen in cell migration, this review will contribute to the development of innovative collagen-based biomaterials with applications in wound healing and tissue regeneration.
Graphical abstract
... Likewise, gelatin and hydrolysates were produced from Collagen and proteinrich fish skin and utilized in biomedical and nutritional applications. Knowing how important fish size was for producing useful biochemical components could assist in maximizing resource usage and improving processing methods, especially in light of the growing demand for sustainable bioresources worldwide (Tang et al., 2022). The relationship between fish size and its biochemical composition, specifically the amounts of collagen and protein, had not been well studied, despite the rising interest in the biochemistry of fish skin (Muralidharan et al., 2024). ...
Fish skins, particularly those of snakehead fish (Channa striata), mrigal carp (Cirrhinus mrigala), and salmon (Salmo salar), are of great value as by-products in the fisheries industry, because of their high organic matter content and further biochemical processing. It examines into the impact of body weight on the biochemical composition and collagen content of the skins of these three fish species. Both sexes of fresh fish were classified into small, medium, and large bodyweight categories. Biochemical composition, amino acid profiling, hydroxyproline content determination, and Energy Dispersive Spectroscopy (EDS) for each species were used to examine the skin composition for biochemical parameters, amino acid profile, collagen content, microstructure, and mineral composition. Moisture and ash contents decrease, whereas lipid content increases with body weight. There were no significant trends in protein composition concerning body heaviness for any species. Glycine and proline were found to be major amino acids for all species, and with the analysis for hydroxyproline, all three species presented collagen in the skin. EDS analysis of minerals in the different species' skins was also distinguished. No significance in collagen proteins was observed at any of the body weight classes for any species. It highlights the biochemical composition, mineral content, and amino acid profile of fish skin to ascertain its potential economic value and further utilization as a by-product.
... Despite its similar composition gelatin is characterized by shorter and randomly arranged polypeptide chains ( Fig. 3f) [80]. Gelatin is primarily sourced from animal skins and bones, particularly pigs and cows, via acid or alkaline processing, whereas a minor fraction is derived from fish [81]. Gelatin-based films have certain limitations, such as their ability to absorb moisture in humid conditions. ...
Terahertz (THz) devices, owing to their distinctive optical properties, have achieved myriad applications in diverse domains including wireless communication, medical imaging therapy, hazardous substance detection, and environmental governance. Concurrently, to mitigate the environmental impact of electronic waste generated by traditional materials, sustainable materials-based THz functional devices are being explored for further research by taking advantages of their eco-friendliness, cost-effective, enhanced safety, robust biodegradability and biocompatibility. This review focuses on the origins and distinctive biological structures of sustainable materials as well as succinctly elucidates the latest applications in THz functional device fabrication, including wireless communication devices, macromolecule detection sensors, environment monitoring sensors, and biomedical therapeutic devices. We further highlight recent applications of sustainable materials-based THz functional devices in hazardous substance detection, protein-based macromolecule detection, and environmental monitoring. Besides, this review explores the developmental prospects of integrating sustainable materials with THz functional devices, presenting their potential applications in the future.
... Fish biomass presents a valuable source of collagen, the most abundant structural protein in the extracellular matrix of connective tissues, including skin, bones, ligaments, tendons, and cartilage [14,15]. Collagen has extensive applications in biomedical fields due to its versatility as a biopolymer, making it particularly useful in cosmetics and tissue engineering for human health applications [16][17][18]. ...
The global food industry's exponential growth has made it crucial to assess food waste. In this study, collagen extraction from waste fish bones was carried out in the presence of 0.5 M acetic acid. The physicochemical properties of the successfully obtained collagen were determined by Ultraviolet and Visible Spectroscopy (UV-Vis), Fourier Transform Infrared Spectroscopy (FTIR), X-ray diffraction (XRD), and Differential Scanning Calorimetry (DSC). The results of UV-Vis Spectra of collagen showed maximum absorption at 238 nm. The extracted collagen was found to have a triple helix structure by UV-Vis and FTIR analysis. It was determined that it was semi-crystalline with the XRD diffraction pattern. The thermal denaturation temperature was between 129 ºC and 141 ºC with a flow rate of -4.881 mW (141 ºC) and the enthalpy change (ΔH) was 39.2 mJ/mg. The study has shown that sufficient collagen can be isolated from fish waste simply and inexpensively. Moreover, the present study found that collagen obtained from fish processing waste can be used as a high-value-added material in many areas for various industrial purposes, such as the cosmetics and pharmaceutical industries. Most importantly, processing waste can be utilized, and environmental pollution can be prevented.
... All three types of gelatin exhibited broad diffraction peaks, reflecting primarily an amorphous structure with some degree of crystallinity. Gelatin, a denatured form of collagen, generally lacks a highly ordered structure but retains minor crystalline regions due to residual sequences from the native triple helix [57]. The XRD pattern of A gelatin (acid-extracted) shows a broad, low-intensity peak centered around 21 • (2θ), suggesting significant disruption of the collagen structure by acid treatment. ...
Yanbian cattle, a high-quality indigenous breed in China, were selected due to their unique biological characteristics, underutilized bone byproducts, and potential as a halal-compliant gelatin source, addressing the growing demand for alternatives to conventional mammalian gelatin in Muslim-majority regions. This study investigates the physicochemical and functional properties of gelatin extracted from Yanbian cattle bones using three different methods: acid, alkaline, and papain enzymatic hydrolysis. The extraction yields and quality of gelatin were evaluated based on hydroxyproline content, gel strength, viscosity, amino acid composition, molecular weight distribution, and structural integrity. Specifically, A gelatin, prepared using 0.075 mol/L hydrochloric acid, achieved the highest yield (18.64%) among the acid-extraction methods. B gelatin, extracted with 0.1 mol/L sodium hydroxide, achieved the highest yield (21.06%) among the alkaline-extraction methods. E gelatin, obtained through papain hydrolysis, exhibited the highest yield (25.25%) among the enzymatic methods. Gelatin extracted via papain enzymatic hydrolysis not only retained better protein structure but also exhibited higher hydroxyproline content (19.13 g/100 g), gel strength (259 g), viscosity (521.67 cP), and superior thermal stability. Structural analyses conducted using SDS-PAGE, GPC, FTIR, XRD, and CD spectroscopy confirmed that papain extraction more effectively preserved the natural structure of collagen. Furthermore, amino acid composition analysis revealed that gelatin extracted via papain hydrolysis contained higher levels of essential residues, such as glycine, proline, and hydroxyproline, emphasizing the mild and efficient nature of enzymatic treatment. These findings suggest that, compared with acid and alkaline extraction methods, enzymatic hydrolysis has potential advantages in gelatin production. Yanbian cattle bone gelatin shows promise as an alternative source for halal gelatin production. This study also provides insights into optimizing gelatin production to enhance its functionality and sustainability.
... As safe nutraceuticals, collagen supplements come from different sources (e.g., porcine, bovine, marine) and in diverse types (e.g., peptides, hydrolysate, gelatin) [6]. Several studies have reported taking collagen hydrolysate or small peptides as oral supplements for pressure ulcers, xerosis, skin aging, anti-aging, and wound healing [7][8][9]. ...
Background: Osteoporosis has become an inevitable health issue with global aging, and the current drug treatments often have adverse side effects, highlighting the need for safer and more effective therapies. Collagen-derived peptides are promising alternatives due to their favorable safety profile and biological activity. This study aimed to investigate the osteogenic and anti-apoptotic properties of collagen peptide UU1 (GASGPMGPR) in addition to its antioxidant activity. Methods: The effects of UU1 were evaluated in MC3T3-E1 cells by assessing osteogenic markers, including alkaline phosphatase (ALP), Cyclin D1, runt-related transcription factor 2 (Runx2), and Akt/β-catenin signaling. Western blot analysis quantified collagen I, osteocalcin, and phosphorylated Akt levels. Anti-apoptotic effects were measured via p-Akt levels and the Bax/Bcl-2 ratio. Computational molecular docking was performed to explore the molecular mechanism of UU1 via its interaction with epidermal growth factor receptor (EGFR) and collagen-binding integrin. Results: UU1 treatment promoted cell differentiation, with elevated ALP, Cyclin D1, Runx2, and Akt/β-catenin signaling. Notably, at 0.025 mg/mL, UU1 upregulated the levels of collagen I, osteocalcin, and phosphorylated Akt by 2.14, 3.37, and 1.95 times, respectively, compared to the control. Additionally, UU1 exhibited anti-apoptotic effects, indicated by increased p-Akt levels and a reduced Bax/Bcl-2 ratio. Molecular docking analysis suggested that UU1 could assist the dimerization of EGFR, facilitating downstream signaling transductions and activating collagen-binding integrin. Conclusions: These findings highlight UU1 as a multifunctional peptide with antioxidant, osteogenic, and anti-apoptotic properties, positioning it as a promising candidate for anti-osteoporosis applications in the food and pharmaceutical industries.
... The gel provides a viscous medium that maintains the shape of the extruded bioink, preventing collapse without the need for additional structural support. After printing, the scaffold is incubated at 37 • C for 30 min, during which pH neutralization induced by the hydrogel bath stabilizes the collagen structure [32]. The ethanol present in the bath facilitates collagen crosslinking, leading to dehydration and densification of the collagen network, which is essential for enhancing the scaffold's mechanical strength by tightly packing the collagen fibers. ...
To meet the increasing demand for bone scaffolds, advancements in 3D printing have significantly impacted bone tissue engineering. However, the materials used must closely mimic the biological components and structural characteristics of natural bone tissue. Additionally, constructing complex, oblique structures presents considerable challenges. To address these issues, we explored 3D bioceramic printing using a sanitizer-based hydrogel. Collagen, a primary component of the bone extracellular matrix (ECM), was combined with alpha-tricalcium phosphate (α-TCP) to create the bioceramic ink. The sanitizer-based hydrogel was chosen as the gel bath due to its carbopol content, which provides hydrogel-like support, and ethanol, which coagulates collagen and maintains the integrity of the 3D-printed structure. The α-TCP/collagen bioceramic ink was printed within the sanitizer-based hydrogel, then collected, immersed in ethanol, and finally submerged in phosphate-buffer saline to initiate a self-setting reaction that converted α-TCP into calcium-deficient hydroxyapatite. The results demonstrated that complex ceramic/ECM structures could be successfully printed in the sanitizer bath, exhibiting excellent mechanical characteristics. Additionally, scaffolds printed in the sanitizer bath showed higher levels of cell growth and osteogenic activity compared to those produced with only α-TCP in an open-air environment. This bioceramic printing approach has a strong potential for constructing complex scaffolds with enhanced osteogenic potential for bone regeneration.
... Hydrogels based on collagen have emerged as promising biomaterials for regenerative medicine applications. Collagen hydrogels possess excellent biocompatibility, water-holding capacity, and structural resemblance to the extracellular matrix (Tang et al., 2022). These hydrogels can be easily synthesized and modified to incorporate bioactive molecules, growth factors, and cells, enhancing their regenerative potential. ...
Gellan gum and collagen are two biomaterials that have been extensively studied for their potential use in wound healing and tissue engineering applications. Gellan gum is a biologically inert natural polymer that is increasingly favored as a biomaterial to form hydrogels. Collagen, on the other hand, is a major component of the extracellular matrix and is widely used in tissue engineering applications due to its biocompatibility and ability to promote cell adhesion and proliferation. In this review, the recent research will be discussed related to gellan gum and collagen, their properties, and their potential applications in wound healing and tissue engineering.
... As collagen scaffolds aspirate to recapitulate the complex native tissue, collagen-based products are highly variable, including tissue grafts, hydrogels, sponges, fibers, films, hollow spheres, and tissue-engineered living substitutes 3 . Specifically, collagen and its derivative gelatin are extensively used in the cultivated meat and food industry 8,9 , supporting the growth of 3D tissue culture in an ECM-mimicking environment 10 . ...
Collagen, the most abundant protein in the extracellular matrix of mammalian cells, is extensively needed in various biotechnological and therapeutic applications, such as tissue engineering and regeneration, cosmetics, and cultivated meat. Despite the increasing demand for natural collagen from non-animal sources, it is mainly produced from animal connective tissues. Recent research has highlighted that under hypoxia, the activation of the hypoxia-inducible factor (HIF) leads to enhanced collagen type I biosynthesis. However, under normal oxygen conditions, HIF activity is downregulated by the HIF-prolyl hydroxylase (PHD) enzyme. We, therefore, hypothesized that inhibiting PHD could elevate HIF transcriptional activity and enhance collagen biosynthesis under normoxia. Our study demonstrates that inhibiting PHD using exogenous small molecules boosts HIF activity and upregulates the key enzymes, collagen prolyl 4-hydroxylases and lysyl hydroxylases, resulting in up to 29-fold increase in collagen type I in embryonic mouse fibroblast NIH/3T3 cells. These findings suggest that targeting PHD can effectively enhance collagen production in mammalian cells. Therefore, modulating key protein signaling pathways presents a promising strategy for enhancing the production of high-yield natural collagen.
Collagen is a vital structural protein found in the extracellular matrix of mammalian skin, bones, muscles, and various other tissues. It is extensively utilized in the food industry due to its distinct biochemical, structural, and physicochemical properties. These attributes enhance the elasticity, texture, and stability of a wide range of food products while also improving their nutritional and health benefits. This review examines the sources, structures, extraction techniques, and physicochemical characteristics of collagen molecules. Furthermore, it investigates methods for producing collagen-based composites, films, coatings, and electrospun fibers. The review also highlights the potential applications of collagen in active and intelligent packaging, as well as its use in the formulation of food additives and materials for food preservation. The objective is to provide a comprehensive overview of collagen and its derivatives in relation to food safety while addressing the challenges and opportunities for developing sustainable, active materials within the food industry.
This study presents a novel strategy for utilizing chrome-tanned leather shaving dust (CSD), a hazardous industrial byproduct, by converting it into electrospun nanofibrous mats for wound healing applications. Collagen, extracted from CSD through protease-assisted enzymatic hydrolysis with a 99.98 % dechroming efficiency (reducing chromium from 7700 ppm to 4.71 ppm) and a 31 % yield, was combined with poly(vinyl alcohol) (PVA) and chitosan. Nanomats were fabricated by electrospinning and characterized using FT-IR, XRD, DSC, TGA, and SEM. The S-3 formulation (collagen/PVA ratio of 1:3 with 20 % chitosan) demonstrated optimal properties, including a nanofiber diameter of 277 nm, tensile strength of 3.7 MPa, and 90 % elongation at break, indicating suitability for skin tissue engineering. Thermal analysis revealed enhanced thermal stability, and swelling studies revealed controlled water uptake (150 % in water, 118 % in PBS). S-3 exhibited controlled biodegradation, with 57 % weight loss over three weeks in simulated body fluid. Comparative properties and wound healing performance analysis showed superior antibacterial activity against Bacillus subtilis (30 mm inhibition zone) and Escherichia coli (23 mm inhibition zone), exceeding that of existing collagen-based nanomats and commercial scaffolds. In vivo studies confirmed accelerated wound closure (12 days) compared to other collagen-based nanomats and commercial dressings (16-21 days), along with enhanced collagen deposition, and fibroblast proliferation. These findings demonstrate that CSD-derived collagen/PVA/chitosan nanomats offer a sustainable and high-performance alternative to existing wound dressings.
A robust biodegradable packaging material was developed having superior barrier resistance to water, air, oil, grease, and microorganisms, which consisted of paper handsheets made from recycled old-corrugated container (OCC) wastes and collagen hydrolysate by upcycling leather wastes to reduce dependence on conventional packaging materials. The dechroming process of leather waste using 10% NaOH exhibited remarkable efficiency, achieving a 99.98% reduction in chromium content (< 44 ppb) within the World Health Organization’s recommended range. A coating recipe was formulated using collagen hydrolysate, chitosan, and glycerin (20%C-Ch-Gly) and applied on the OCC handsheets, demonstrating excellent barrier properties against hot oil, grease, and organic solvents (Kit rate 12). The developed packaging materials’ water vapor and air permeability decreased significantly by 150- and 10-fold, while tensile and burst strength increased by 140.84% and 77.73% compared to uncoated handsheets. The contact angle for water and organic solvents increased by 49.14% and 47.2%, ensuring excellent solvent repellency while maintaining a smooth and even morphological structure due to reduced average roughness by 76.67%. The optimized packaging material exhibited no cytotoxicity, displayed excellent antimicrobial properties, and was completely biodegraded in 11 weeks. This study demonstrated the potential of bio-based packaging as a viable alternative to hazardous, non-biodegradable plastics commonly used globally through upcycling leather and paper waste.
Graphical Abstract
A huge number of byproducts and wastes are derived from the processing of fishery resources, which, in the case of teleost fish, can represent up to 70% of the initial biomass. In industry, fishery wastes are destined to produce oil and fishmeal used to elaborate animal feeds. Nevertheless, biomass from fish wastes has an excellent potential to be an important source of bioproducts with high added- and commercial values, such as protein, peptides, gelatins, collagen, sulfated polysaccharides, and polyunsaturated fatty acids. Some of these biomolecules are used as food supplements due to their high nutritional value. Still, additionally, they can show one or several biological activities, the most notable being antioxidant, antihypertensive, anticarcinogenic, and antimicrobial, among others. Then, these bioactive molecules may further be used as food additives as well as to formulate nutraceutical and therapeutic products. Thus, aspects such as chemical composition, structural biochemistry of molecules with biological activities, and conventional and innovative biotechnological processes (e.g., enzyme and microbial processing) used to recover or produce such biomolecules from fish waste will be discussed in greater detail in this chapter.
Utilization of mackerel fish waste from the fish processing industry into collagen can increase the value of by-products. The aim this study was to investigate the effect of acetic acid concentration on physicochemical characteristics of collagen from mackerel fish waste ( Euthynnus affinis ). Different concentration of acetic acid (0.1, 0.5, 0.9, 1.5 M) was carried out to extract collagen. The water content was ranging from 1.06 to 1.42%, ash content was ranging from 5.27 to 5.86%, protein content was ranging from 75.22 to 80.87%, white degree was ranging from 73.60 to 81.08%. Amino acids contents were alanine, glutamic acid, glycine, leucine, lysine, methionine, proline, valine, tyrosine, aspartate acid. The best treatment was found on 1.5 M of acetic acid.
As demand for sustainable and eco-friendly packaging grows, industries are studying biopolymers for food packaging. From the stage of conceptualization to the stage of consumer applications in the real world, this review paper focuses on novel combinations of collagen and a variety of natural biopolymers. It offers an in-depth analysis of the process. The review begins with collagen's biopolymer properties and then explores many natural biopolymers suitable for collagen fusion. By examining synergistic effects, the paper shows how each biopolymer improves blend performance. In this study, the influence of processing parameters on the formation of films as well as the mechanical, barrier, and thermal properties of collagen-natural biopolymer films is investigated systematically. The in-depth study includes food industry case studies and consumer perception and sensory attributes of collagen-natural biopolymer packaging. To understand this field's challenges and opportunities, regulatory and compliance issues are examined. To promote sustainable packaging, collagen-natural biopolymer films are evaluated for environmental impact and biodegradability. Cellulose is a promising natural biopolymer for food packaging applications due to its biodegradability, renewability, and excellent barrier properties. When combined with collagen, cellulose can enhance the mechanical strength and stability of the packaging material. Collagen-natural biopolymer films are compared to conventional packaging materials for performance, cost, and environmental impact. This review concludes with current research, challenges, and future directions in collagen fusion with natural biopolymers for food packaging. This review aims to inform researchers, industry professionals, and policymakers about sustainable food packaging.
Studies have been conducted on the effect of natural vegetable and fruit juices (pumpkin, tomato, apple) and their mixtures containing weak organic acids and used as a liquid medium for hydration of pre-treated walleye fish skin (Sander lucioperca) on the degree of its softening, which occurs as a result of hydration of collagen molecules of fish raw materials in the mixture with natural juices, accompanied by an increase in its mass and thickness). It was determined that the initial fish skin with a thickness of 0.18-1.00 mm at the end of the hydrolysis process had a thickness of 2.6-6.3 mm (apple juice), 2.12-4.01 mm (dried) and 0.69-2.08 mm (tomato), and the skin weight increased by 400, 257.5 and 230%, respectively. It was noted that, despite significant swelling (increase in volume), the skin retained its shape during the entire hydrolysis process (up to 30 days in tomato juice), which indicates a weak degree of hydrolysis of raw materials and preservation of the natural shape of the fish collagen molecule. It is shown that the hydrolyzed mixture is easily homogenized to obtain a homogeneous mass, which is a juice-containing hydrate of fish collagen (food additive). The dynamics of pH changes in various juices and their mixtures is presented depending on the duration of the hydrolysis process with fish skin, which depends on the type of juice used and has a general tendency to deoxidation of the resulting final product compared with the juice used. The values of peak loads for needle puncture and rupture of fish skin were determined, which showed a significant decrease in their hydrolysis process, compared with raw skin.
This study investigates the development of a novel soft cottage cheese product enriched with collagen concentrate from poultry processing by-products and antioxidant-rich plant extracts for the adaptive nutrition of athletes. Collagen concentrate was obtained from chicken skin, bone tissue, and feet through enzymatic hydrolysis and freeze-drying. Antioxidant-rich extracts were prepared from sea buckthorn and cinnamon rosehip using ethanol extraction. The plant extract demonstrated high antioxidant potential, containing 1.98% phenolic compounds, 29.8 mg/100g vitamin A, 48.9 mg/100g vitamin E, and 756.4 mg/100g vitamin C. The antioxidant extract demonstrated significant immune-boosting effects in experimental rats by enhancing lymphocyte and T-cell counts. Various ratios of collagen concentrate and plant extract were tested in the cottage cheese product. Optimal water-holding capacity and effective viscosity were achieved with a 6:4 or 8:4 collagen-to-extract ratio, balancing collagen’s gelation properties with the antioxidant benefits. The addition of 8% dry collagen concentrate and 4% sea buckthorn and rosehip extract resulted in an enhanced nutritional profile, particularly through increased polyunsaturated fatty acids (Omega-3 and Omega-6), vitamins A, C, E, and essential minerals like calcium, phosphorus, and magnesium. Storage stability studies indicated optimal preservation of product structure at 0-2°C for up to 96 hours, maintaining a viscosity loss coefficient between 15.0-15.8%. This enhanced soft cottage cheese product demonstrates improved nutritional profiles and antioxidant properties while maintaining structural stability, making it a promising functional food for athletes and health-conscious consumers.
The aim of the study was to extract and characterize collagen from solid untanned skin waste from the processing of leather in a Capra aegagrus tannery. Using pepsin (SPC), 37 grams of collagen were obtained from 100 grams of dry weight skin. Characterization took place using SDS-PAGE, FTIR and UV absorption techniques, identifying it as type I collagen. The ultraviolet (UV) absorption spectrum showed a peak at 238 nm. In the thermogram, the maximum transition temperature was 56º C. Using the electrophoresis technique, it was observed that SPC consists of band patterns formed by a γ chain, a β chain and two distinct α chains (α1 and α2). In the FTIR analysis, the collagen showed the absorption peaks for the amides, showing that the SPC extraction process maintained the integrity of the molecule. To observe the effect of NaCl concentration on the solubility of SPC, the collagen showed high solubility, up to a concentration of 2% NaCl. The solubility peak was observed at pH 4.0, with a sharp drop until pH 7.0, reaching its minimum point at pH 10. Scanning microscopy showed some irregular surfaces, cavities and fibrous structures, which may favor the application of collagen as a biomaterial. The zeta potential found the isoelectric point of collagen at pH = 6.61. These results indicate that the collagen obtained has a high level of structural integrity and can be applied as an alternative source, as well as adding value to a waste product that is often discarded in the environment.
Objectives
This study aimed to investigate the physical properties of Indonesian local sheep skin collagen extracted by acid and enzymatic methods.
Materials and Methods
Collagen was isolated from Pure Breed Garut Sheep (Ovis aries sp.) skin, 1.5 years old. The skins were obtained from a local slaughterhouse in Cirebon, Indonesia. The solvents used were CH3COOH and three different enzymes: neutrase, alcalase, and bromelain.
Results
The highest yields of extracted collagen were bromelain-soluble collagen (BSC), which reached 37.07%. The range of Ph values for all samples started from 4.01 to 4.76. The viscosity values (cP) of acid-soluble collagen (ASC), neutrase-soluble collagen (NSC), alcalase-soluble collagen (LSC), and BSC were 3.42, 3.90, 3.45, and 3.12, respectively. Regarding SDS-PAGE analyses, Garut sheepskin collagen is categorized as collagen type I, which has a molecular weight of about 140.99 to 148.74 kDa for α1 and around 110 to 111.86 kDa for α2. The results of FTIR and DSC analyses for all samples show the same motif with commercial collagen motifs based on the literature.
Conclusion
Garut sheep skin has the potential to be an alternative raw material source for producing collagen. Collagen extracted using a combination of CH3COOH and bromelain enzyme showed the most desirable results in almost every characteristic.
This article describes the compositional, mechanical, and structural differences between collagen gels fabricated from different sources and processing methods. Despite extensive use of collagen in the manufacturing of biomaterials and implants, there is little information as to the variation in properties based on collagen source or processing methods. As such, differences in purity and composition may affect gel structure and mechanical performance. Using mass spectrometry, we assessed protein composition of collagen from seven different sources. The mechanics and gelation kinetics of each gel were assessed through oscillatory shear rheology. Scanning electron microscopy enabled visualization of distinct differences in fiber morphology. Mechanics and gelation kinetics differed with source and processing method and were found to correlate with differences in composition. Gels fabricated from telopeptide‐containing collagens had higher storage modulus (144 vs. 54 Pa) and faster gelation (251 vs. 734 s) compared to atelocollagens, despite having lower purity (93.4 vs. 99.8%). For telopeptide‐containing collagens, as collagen purity increased, storage modulus increased and fiber diameter decreased. As α1/α2 chain ratio increased, fiber diameter increased and gelation slowed. As such, this study provides an examination of the effects of collagen processing on key quality attributes for use of collagen gels in biomedical contexts.
In 2020, the world’s food crisis and health industry ushered into a real outbreak. On one side, there were natural disasters such as the novel coronavirus (2019-nCoV), desert locusts, floods, and droughts exacerbating the world food crisis, while on the other side, the social development and changes in lifestyles prompted the health industry to gradually shift from a traditional medical model to a new pattern of prevention, treatment, and nourishment. Therefore, this article reviews animal by-products collagen and derived peptide, as important components of innovative sustainable food systems. The review also considered the preparation, identification, and characterization of animal by-product collagen and collagen peptides as well as their impacts on the food system (including food processing, packaging, preservation, and functional foods). Finally, the application and research progress of animal by-product collagen and peptide in the food system along with the future development trend were discussed. This knowledge would be of great significance for a comprehensive understanding of animal by-product collagen and collagen peptides and would encourage the use of collagen in food processing, preservation, and functional foods.
Fish gelatin and its hydrolysates exhibit a variety of biological characteristics, which include antihypertensive and antioxidant properties. In this study, fish gelatins were extracted from extrusion-pretreated tilapia scales, and then subjected to analyses to determine the physicochemical properties and antioxidant activity of the extracted gelatins. Our findings indicate that TSG2 (preconditioned with 1.26% citric acid) possessed the greatest extraction yield, as well as higher antioxidant activities compared with the other extracted gelatins. Hence, TSG2 was subjected to further hydrolyzation using different proteases and ultrafiltration conditions, which yielded four gelatin hydrolysates: TSGH1, TSGH2, TSGH3, and TSGH4. The results showed that TSGH4 (Pepsin + Pancreatin and ultrafiltration < 3000 Da) had a higher yield and greater antioxidant activity in comparison with the other gelatin hydrolysates. As such, TSGH4 was subjected to further fractionation using a Superdex peptide column and two-stage reverse-phase column HPLC chromatography, yielding a subfraction TSGH4-6-2-b, which possessed the highest 2,2-diphenyl-1-picrylhydrazyl (DPPH) scavenging activity compared with the other fractions. Further LC-ESI/MS/MS analysis of TSGH4-6-2-b suggested two novel peptides (GYDEY and EPGKSGEQGAPGEAGAP), which could have potential as naturally-occurring peptides with antioxidant properties. These promising results suggest that these antioxidant peptides could have applications in food products, nutraceuticals, and cosmetics.
This study was conducted to decipher the mechanism of emulsion-based food stabilization by fish-derived collagen hydrolysate. Collagen type I was isolated from seven fish processing by-products with yields ranging from 9.15 to 92.38%. The isolated samples had a mass of 110–120kDa and eluted at 30.44% NaCl in ion-exchange chromatography. The collagen samples were enzymatically digested to obtain collagen hydrolysate (CH) with mass <6kDa. The seven CH samples were subsequently screened for surface activity. CH obtained from Pacu skin and Tilapia bones exhibited more than 80% solubility over a wide pH range, zeta potential greater than +50mV, moisture retention up to 92–96%, emulsification activity of 53–70 m²g⁻¹, and emulsion stability of 62–85min, and successfully increased the emulsion stability of a drug by 14 times. Both CH samples were able to retain the emulsion properties of butter and chocolate sauce for 25 weeks and did not show any cytotoxic effect on leukocytes and Vero cells. Structural studies revealed that the CH peptides existed in polyproline-II conformation that assembled to form a vast quasifibrillar network. Sequence analysis through tandem mass spectroscopy revealed that the peptides could be classified into multiple groups depending on the distribution of hydrophilic/lipophilic residues (H/L). The surface activity of the CH was found to be dependent on (1) small size and a wide array of H/L ratio, (2) abundance of hydroxyproline, and (3) assembly of the peptides in the emulsion interface to form a mimic-helix–based quasifibrillar network which ensured optimal orientation and subsequent interaction with multiple phases.
The utilization of bigeye tuna skin as a source of collagen has been increasing the value of these skins. In this study, the quality of the skin was studied first. The skin after 14 h freeze-drying showed a high protein level (65.42% ± 0.06%, db), no histamine and a lack of heavy metals. The collagens were extracted through acid and acid-enzymatic methods. The enzymes used were bromelain, papain, pepsin, and trypsin. The two highest-yield collagens were pepsin-soluble collagen (PSC) and bromelain-soluble collagen (BSC). Both were type I collagen, based on SDS-PAGE and FTIR analysis. They dissolved very well in dimethyl sulfoxide and distilled water. The pH ranges were 4.60–4.70 and 4.30–4.40 for PSC and BSC, respectively. PSC and BSC were free from As, Cd, Co, Cr, Cu, and Pb. They showed antioxidant activities, as determined by the DPPH method and the reducing power method. In conclusion, bigeye tuna skin shows good potential as an alternative source of mammalian collagen. Although further work is still required, PSC and BSC showed the potential to be further used as antioxidant compounds in food applications. Other biological tests of these collagens might also lead to other health applications.
In the present study, antioxidant activities and functional properties of cowhide collagen antioxidant peptides (CCAPs) with different molecular weight (MW) were investigated. The optimum preparation conditions of CCAPs were hydrolysis time of 1.53 hr, temperature of 54.9 °C, pH 7.38, and neutral enzyme to trypsin ratio of 0.048 g: 0.016 g according to single factor test and response surface methodology (RSM). Three fractions (CCAP‐I, CCAP‐II, and CCAP‐III) were obtained by ultrafiltration and lyophilization. Antioxidant activities revealed that CCAP‐III had high reducing power activity (0.323 ± 0.035) and scavenging effect on 2,2‐diphenyl‐1‐picrylhydrazyl (DPPH) radicals (64.30 ± 5.99%), 2,2‐azino‐bis‐(3‐ethylbenzothiazoline)‐6‐sulfonic acid (ABTS) radicals (75.25 ± 3.14%), and hydroxyl radicals (68.26 ± 6.74%) compared to the other fractions. In addition, LC‐MS/MS analysis showed that Ala‐Gly‐Glu‐Arg, Gly‐Ile‐Ala‐Gly‐Glu‐Arg, Gly‐Pro‐Ala‐Gly‐Pro‐Ala‐Gly‐Pro‐Arg, Gly‐Val‐Val‐Gly‐Pro‐Glu‐Gly‐Ala‐Arg and Gly‐Phe‐Ser‐Gly‐Leu‐Asp‐Gly‐Ala‐Lys were the major peptides of CCAP‐III. CCAP‐III showed good hygroscopicity (HYG), water holding capacity (WHC), and oil holding capacity (OHC) when compared with CCAP‐I and CCAP‐II. However, CCAP‐II has great emulsifying properties, and CCAP‐I has excellent foaming properties. Therefore, CCAPs can be used as a promising source of functional peptides with antioxidant properties.
Practical Application
This study demonstrated the peptides of cowhide collagen has superior antioxidant and functional properties. This study provided a scientific basis for the preparation of antioxidant peptides from cowhide collagen.
Collagen hydrolysate has various beneficial effects, such as bone strengthening, joint/skin protection and lipid metabolism regulation. In this study, the anti-obesity activity of ginger protease-degraded collagen hydrolysate (GDCH) was evaluated in BALB/c mice fed diets containing 14% casein (control group) or 10% casein + 4% GDCH (GDCH group) for 10 weeks. In the GDCH group, triglyceride (TG) and cholesterol (CHO) levels in blood and adipocyte size in white adipose tissue were significantly decreased compared with those of the control group. Further, gene expression related to fatty acid synthesis, such as acetyl-CoA carboxylase, fatty acid synthase and stearoyl-CoA desaturase, was decreased in the liver and white adipose tissue of GDCH-fed mice. On the other hand, single oral administration of GDCH did not result in decrease in blood TG and CHO compared with vehicle and casein in ICR mice pre-administered soybean oil. These results suggest that the GDCH-induced decreases in tissue and blood lipids occur through long-term alterations in lipid metabolism, not transient inhibition of lipid absorption. The lipid-lowering effects exhibited by partial substitution of casein with GDCH imply the possibility that daily supplementation of GDCH contributes to prevention/attenuation of obesity and hyperlipidemia.
Collagen peptides are collagen derived products by enzymatic proteolysis, which is widely distributed in mammalian connective tissues. They have exhibited various bioactivities, including antioxidant activity, antihypertensive activity, improvement of joint pain, etc. However, the immunomodulatory effects of collagen peptides in the condition of immune suppression have not been elucidated. The objective of this study was to investigate the effects of collagen peptides on immune function in immunosuppressed mice. The immunosuppression was induced by intraperitoneal injection of dexamethasone for three days and at same time, collagen peptides (0, 300, 600, 900 mg/kg body weight) were given by gavage for seven days. On the day 8, the mice were sacrificed by decapitation. The body weight and the weights of thymus and spleen were recorded. Thymus and spleen indexes were calculated. The proliferation and interleukin-2 production of splenic T lymphocytes and ratio of CD4+/CD8+T lymphocytes in the peripheral blood were examined. Compared with the control mice, the body weight, thymus and spleen indexes, the proliferations and interleukin-2 production in T lymphocytes and the ratios of CD4+/CD8+T cells were significantly decreased in dexamethasone induced immunosuppressed mice. However, in collagen peptides treated mice, the thymus indexes, proliferation index, secretion of interleukin-2 and the ratio of CD4+/CD8+ were significantly increased compared with the mice in experimental model group. These results indicate that collagen peptides could play a protect role in glucocorticoid-induced immunosuppression.
Inhibition of dipeptidyl peptidase IV (DPP‐IV) was considered to be a crucial target for type 2 diabetes, and food‐derived peptides were superior source of DPP‐IV inhibitory peptides. The purpose of this investigation was to identify inhibitory peptides from salmon skin collagen using simulated digestion combined with Caco‐2 cell monolayer membrane model. The analysis in silico showed that TKLPAVF and YLNF were potential inhibitory peptides. Determination of the inhibition activity showed that the IC50 values of TKLPVAF and YLNF were 242.10 ± 3.40 and 146.90 ± 4.40 µm, respectively. Molecular docking results showed that seven hydrogen bonds were formed between YLNF and key residues of DPP‐IV. YLNF may be considered a novel DPP‐IV inhibitory peptide. In addition, YLNF could be transported by Caco‐2 cell monolayer membrane in intact, and the apparent permeability coefficient value was (3.54 ± 0.34) × 10‐6 cm s⁻¹ at 5 mm.
Background & Aims
Nutritional composition is key for skeletal muscle maintenance into older age. Yet the acute effects of collagen protein blended with other protein sources, in relation to skeletal muscle anabolism, are ill-defined. We investigated human muscle protein synthesis (MPS) responses to a 20g blend of collagen protein hydrolysate + milk protein (CP+MP, 125ml) oral nutritional supplement (ONS) vs. 20g non-blended milk protein source (MP, 200ml) ONS, in older adults.
Methods
Healthy older men (N=8, 71±1y, BMI: 27±1kg·m⁻²) underwent a randomized trial of 20g protein, from either a CP+MP blend (Fresubin®3.2kcal DRINK), or a kcal-matched (higher in essential amino acids (EAA) ONS of MP alone. Vastus lateralis (VL) MPS and plasma AA were determined using stable isotope-tracer mass spectrometry; anabolic signaling was quantified via immuno-blotting in VL biopsies taken at baseline and 2/4 h after ONS feeding. Plasma insulin was measured via enzyme-linked immunosorbent assay (ELISA). Measures were taken at rest, after the feed (FED) and after the feed + exercise (FED-EX) conditions (unilateral leg exercise, 6×8, 75% 1-RM).
Results
MP resulted in a greater increase in plasma leucine (MP mean: 152 ± 6 μM, CP+MP mean: 113 ± 4 μM (Feed P<0.001) and EAA (MP mean: 917 ± 25 μM, CP+MP mean: 786 ± 15 μM (Feed P<0.01) than CP+MP. CP + MP increased plasma glycine (peak 385 ± 57 μM (P<0.05)), proline (peak 323 ± 29 μM (P<0.01)) and non-essential amino acids (NEAA) (peak 1621 ± 107 μM (P<0.01)) with MP showing no increase. Plasma insulin increased in both trials (CP+MP: 58±10 mU/mL (P<0.01), MP: 42±6 mU/mL (P<0.01), with peak insulin greater with CP+MP vs. MP (P<0.01). MPS demonstrated equivalent increases in response to CP+MP and MP under both FED (MP: 0.039±0.005%/h to 0.081±0.014%/h (P<0.05), CP+MP: 0.042±0.004%/h to 0.085±0.007%/h (P<0.05)) and FED-EX (MP: 0.039±0.005%/h to 0.093±0.013%/h (P<0.01), CP+MP: 0.042±0.004%/h to 0.105±0.015%/h, (P<0.01)) conditions. FED muscle p-mTOR fold-change from baseline increased to a greater extent with CP+MP vs. MP (P<0.05), whilst FED-EX muscle p-eEF2 fold-change from baseline decreased to a greater extent with CP+MP vs. MP (P<0.05); otherwise anabolic signaling responses were indistinguishable.
Conclusion
Fresubin®3.2kcal DRINK, which contains a 20g mixed blend of CP+MP, resulted in equivalent MPS responses to MP alone. Fresubin® 3.2 Kcal DRINK may provide a suitable alternative to MP for use in older adults and a convenient way to supplement calories and protein to improve patient adherence and mitigate muscle mass loss.
High-speed atomic force microscopy (AFM) enabled the imaging of protein interactions with millisecond time resolutions (10 fps). However, the acquisition of nanomechanical maps of proteins is about 100 times slower. Here, we developed a high-speed bimodal AFM that provided high-spatial resolution maps of the elastic modulus, the loss tangent, and the topography at imaging rates of 5 fps. The microscope was applied to identify the initial stages of the self-assembly of the collagen structures. By following the changes in the physical properties, we identified four stages, nucleation and growth of collagen precursors, formation of tropocollagen molecules, assembly of tropocollagens into microfibrils, and alignment of microfibrils to generate microribbons. Some emerging collagen structures never matured, and after an existence of several seconds, they disappeared into the solution. The elastic modulus of a microfibril (∼4 MPa) implied very small stiffness (∼3 × 10–6 N/m). Those values amplified the amplitude of the collagen thermal fluctuations on the mica plane, which facilitated microribbon build-up.
The purpose was to examine the effects of concurrent training (CT) combined with specific collagen peptides (SCP) intake on cardiometabolic parameters and performance indices in women. In a double-blind, placebo-controlled, randomized trial recreationally active women (n = 59) completed a 12-week CT training (3 day/week) and ingested 15 g of SCP (treatment group [TG]) or placebo (control group [CG]) on a daily basis. Running distance as a marker of endurance performance (time trial), velocity and heart rate at the lactate and anaerobic threshold (incremental running test) and body composition (bioelectrical impedance analysis [BIA]) were measured. BIA measurements included determination of fat mass (FM) and fat free mass (FFM). Additionally, muscular strength (one-repetition-maximum [1RM]) and muscular endurance (60% of 1RM) were assessed. After 12-weeks, TG had a higher increase in running distance (1,034 ± 643 m) compared to the CG (703 ± 356 m) indicated by a significant interaction effect (p < 0.05). Velocity at lactate and anaerobic threshold improved in both groups over time (p < 0.001), with no significant differences between groups. Similarly, heart rate at lactate threshold decreased over time (p < 0.001), with no time × group interaction. TG declined more in heart rate at anaerobic threshold (−8 ± 14 bpm) than the CG (−1 ± 7 bpm), which resulted in a significant interaction effect (p < 0.01). FM decreased over time in TG and CG (p < 0.001), with no group differences. On contrary, TG had a higher increase in FFM (0.8 ± 0.9 kg) compared to the CG (0.3 ± 1.0 kg) (time × group interaction: p < 0.05). Both, 1RM and muscular endurance improved over time (p < 0.001), with no significant group differences. In conclusion, supplementation of SCP in combination with CT resulted in a significant increase in endurance performance compared to the control group. This might potentially be a consequence of improved structural and cardiometabolic adaptations.
Growth of ice crystals can cause serious problems, such as frozen products deterioration, road damage, energy losses, and safety risks of human beings. Antifreeze peptides (AFPs), a healthy and effective cryoprotectant, have great potential as ice crystal growth inhibitors for a variety of frozen products. In this review, methods and technologies for the production, purification, evaluation, and characterization of AFPs are comprehensively summarized. First, this review describes the preparation of AFPs, including the methods of enzymatic hydrolysis, chemical synthesis, and microbial fermentation. Next, this review introduces the major methods by which to evaluate AFPs’ antifreeze activity, including nanoliter osmometer, differential scanning calorimetry, splat‐cooling, the biovaluation model, and novel technology. Moreover, this review presents an overview of the molecular characteristics, structure–function relationships, and action mechanisms of AFPs. Furthermore, advances in the application of AFPs to frozen food, including frozen dough, meat products, fruits, vegetable products, and dairy, are summarized and holistically analyzed. Finally, challenges of AFPs and future perspectives on their use are also discussed. An understanding of the production, structure–function relationships, mechanisms and applications of AFPs provides inspiration for further research into the use of AFPs in food science and food nutrition applications.
Background
Studies indicate a 30% increase in demand for all types of food and non-food grade gelatins in the world. The largest volume of gelatin production comes from mammal sources (cows and pigs). Nowadays, health, cultural, and religious concerns have arisen due to consumption of mammalian gelatin. This has prompted scientists to look for non-mammal sources that closely resembles the desirable physicochemical, functional, and sensory characteristics of mammalian gelatins. Non-mammalian gelatin from poultry and fish by-products are also gaining importance in food industry. Over the past decade, poultry production has increased by about 37.34%. Poultry by-products have good potential for replacing mammalian sources for gelatin extraction.
Scope and approach
This paper reviews in detail the fundamental properties of poultry gelatins (PG), including rheological, functional and physicochemical properties. This study provides a perspective on their potential food, pharmaceutical, medical and industrial applications.
Key findings and conclusions
The highest quality PG was extracted through acid treatments. PG extracted in this way exhibited favorable rheological, fat replacement, film formation, foaming, emulsifying and sensory properties, and nutritional quality. PG films showed better barrier properties than mammal-origin gelatin, making them ideal for food and medical applications. The amino acids composition of PG, especially the imino acid and hydrophobic amino acids, which determine the physicochemical and functional properties of gelatin, are higher than gelatin obtained from mammals and fish that classifies them in the upper Bloom category.
The aim of this study was to assess the possibility of using collagen protein hydrolysate in the production of milk fermented by Bifidobacterium animalis ssp. lactis Bb-12 and Lactobacillusrhamnosus. Physicochemical and organoleptic properties were studied and microbiological analysis of fermented milk was performed on days 1 and 21 of storage. Milk with the addition of 3% collagen protein hydrolysate was pasteurized (85 °C/30 min), divided into two groups, cooled to 37 °C and inoculated: the first group with Bifidobacteriumanimalis ssp. lactis Bb-12, second with Lactobacillus rhamnosus. Incubation was carried out at 37 °C/10 h. After 21 days of refrigerated storage, the pH value decreased in all analyzed milk samples. Collagen protein hydrolysate was a good milk additive to increase gel hardness and reduce syneresis. Moreover, its addition did not change the taste and odour of milk fermented with the use of Bifidobacterium Bb-12 and Lactobacillus rhamnosus. Collagen protein hydrolysate favourably stimulated the survival of Bifidobacterium Bb-12 during 21 days of storage. After 21 days of cold storage in milk with collagen, the number of Lactobacillus rhamnosus cells was reduced by 0.11 log cfu g−1.
Background
Chronic wounds continue to be a burden to healthcare systems with ageing linked to increased prevalence of chronic wound development. Nutraceutical collagen peptides have been shown to reduce signs of skin ageing, but there therapeutic potential for cutaneous wound healing remains undefined
Aims
To determine the potential for nutraceutical collagen peptides to promote cutaneous wound healing in vitro in the context of age.
Methods
The potential for bovine or porcine‐derived nutraceutical collagen peptides to promote wound healing of primary cutaneous fibroblasts and keratinocytes derived from young and aged individuals in vitro was assessed by 2D scratch and cell viability assays and immunofluorescence for cell proliferation marker, Ki67. The achievement of peptide concentrations in vivo , equivalent to those exerting a beneficial effect on wound healing in vitro was confirmed by pharmacokinetic studies of hydroxyproline, a biomarker for collagen peptide absorption, following peptide ingestion by healthy varying aged individuals.
Results
Results demonstrated significant nutraceutical collagen peptide‐induced wound closure of both young and aged fibroblasts and keratinocytes, mediated by enhanced cellular proliferation and migration. Analysis of blood levels of hydroxyproline in young and aged individuals following porcine collagen peptide ingestion revealed peak serum/plasma levels after 2 hours at similar concentrations to those exerting a beneficial effects on wound healing in vitro.
Conclusions
These data demonstrate the capacity for nutraceutical collagen peptides to promote cutaneous wound closure in vitro, at pharmacologically achievable concentrations in vivo, thereby offering a potential novel therapeutic strategy for the management of cutaneous wounds in young and aged individuals.
Dynamic quantitative descriptive analysis and temporal dominance of sensations were used to analyze the data of sensory evaluation and characterize the taste profiles of chicken soup. The results showed that umami and saltiness were the dominant taste of the chicken soup and chicken soup with ginger. Nine taste peptides were identified by Nano-LC-Q-TOF-MS/MS and evaluated by sensory evaluation and electronic tongue. Among the identified peptides, AGPSIVH, IKDPHVD and TPPKID were characterized by umami. Besides, IKDPHVD, FAGDDAPR and NALNDITSL showed umami-enhancing effects. The results of molecular docking suggested that the key binding sites were crucial to the docking, such as His71, Ser107 and Glu301 of taste receptor type 1 member 1 and Asp216, Ser104, His145 and Ala302 of taste receptor type 1 member 3. Considering the ranking of sensory analysis, the interaction with taste receptor type 1 member 3 was more likely to relate to the umami intensity of peptides.
Two novel collagen peptides derived from Yak bones, UU1 (GASGPMGPR) and K7 (GLPGPM) were demonstrated to be antioxidative in vitro and in Caenorhabditis elegans. In vitro, UU1 and K7 shown decent scavenging activities on free radicals of DPPH, ABTS, ·OH and ·O–2. Their effects on worms, including the lifespans, locomotory behavior, and reproduction were further evaluated. Whether under normal or thermal conditions, UU1 and K7 extended the survival time accordingly, and promoted the reproduction. Additionally, UU1 and K7 remarkably attenuated the accumulations of reactive oxygen species (ROS) and malondialdehyde (MDA) and enhanced the activities of superoxide dismutase (SOD) and catalase (CAT) in worms. Furthermore, both UU1 and K7 impressively upregulated the expressions of daf-16, sod-3 and skn-1, but their effects on the hsf-1 and the sir-2.1 were distinct. Thus, UU1 and K7 two highly active antioxidant peptides were revealed and could be applied in antioxidant productions.
New forms of composite gels were generated from date seed soluble dietary fiber and gelatin. Gelatin-SDF gels' mechanical and functional characteristics were investigated. These gels were used to make low-fat hamburgers. In comparison to control groups (10% and 20% fats), the impact of the SDF-gelatin composite gels on chemical composition, technical parameters, and textural and sensory characteristics was assessed. The results of textural analysis, swelling ratio, water-holding capacity, and freeze-thaw stability revealed that composite gels had the potential to provide unique functional gels, which is beneficial for formula product development. The addition of composited gels raised the moisture, ash, protein, Na, and Ca content of the burger. Furthermore, the composited gels had a significant influence on the L*(brightness), a*(redness), and b*(yellowness) parameters of the hamburger. The composited gels softened and chewed the burger while increasing its springiness. IPN gels made of SDF and gelatin were effectively used as a fat substitution in meat manufacturing with greater health advantages.
The properties of gelatin film fabricated by ethanol precipitation effect dehydration, Hofmeister effect dehydration and hot air drying dehydration were investigated. The results revealed that the mechanical properties were significantly improved by ethanol precipitation and Hofmeister effect. The tensile strength and elongation at break of the film prepared by ethanol precipitation were increased by 83.28% (20% gelatin concentration) and 122.42% (5% gelatin concentration) respectively compared with that of hot air-dried gelatin film. The water contact angle was increased and water solubility was reduced by ethanol precipitation, which could attribute to the formation of compact structure, more triple helix content, and non-covalent interactions. However, the water contact angle of Hofmeister effect fabricated films was decreased compared with that of hot air drying owing to the adhesion of ammonium sulfate. Moreover, ethanol precipitation effect improved the color difference and opacity due to the ethanol decolorization effect.
This study was aimed to manufacture a functional yogurt fortified with three fish collagen-derived bioactive peptides including GPLGAAGP (P1), GRDGEP (P2), and MTGTQGEAGR (P3) at different concentrations (0.2 to 1.0 mg.mL-1). Bioactive peptides did not significantly alter the pH, titratable acidity (TA), moisture, ash, and fat contents as well as sensory properties (flavor, texture, and appearance) of samples at all concentrations. The protein content, water holding capacity (WHC), and viscosity showed direct relationships with the peptides concentration. The highest DPPH-radical scavenging (86.17% for P1), ferrous chelating (77.00% for P1), reducing power (0.46 for P2), angiotensin-converting enzyme (ACE) inhibitory (77.50% for P2), and dipeptidyl peptidase-IV (DPP-IV) inhibitory (55.30% for P1) activities were at 1mg.mL-1. The gastrointestinal digestion only reduced all biological activities of samples containing P3 at all concentrations significantly. This study demonstrated that the fish collagen-derived bioactive peptides could be promisingly used to manufacture functional yogurt with health promoting properties.
The potential health risks and high cost of current cryoprotectants have emphasised the need to develop antifreezes with high safety and low expense. Gelatine is a promising alternative to these cryoprotectants due to its inherent structural attributes and high availability. In this study, the feasibility of three types of gelatines (gelatine A, B and P) as cryoprotectants in terms of the secondary structure and gel properties related to antifreeze performance was comprehensively investigated. Sodium dodecyl sulphate–polyacrylamide gel electrophoresis analysis patterns suggested that gelatine A had the lowest structural stability upon freeze–thaw (F–T) treatments, which was confirmed by the presence of low-molecular-weight fragments. The two-dimensional correlation infrared spectroscopy indicated that gelatine P had the greatest stability and highest sensitivity to F–T treatments according to changes in the polyproline type II helix structure. Gelatine B showed the lowest gel strength and viscosity compared with the two other gelatines when subjected to the same F–T cycles, which may be ascribed to the loose and inhomogeneous microstructure of gelatine B due to its impaired molecular structure. Gelatine P may be the promising antifreeze used for cryoprotection of the frozen food via the further modifications. This work may provide some valuable guidelines for the development of novel cryoprotectants from the perspective of bottom-up strategies.
With the emergence of social aging problem, people's demand for active ingredients for skin health protection and therapeutic efficacy increases. Bioactive peptides are the optimal substances for skin anti-aging with its great diversity of biological activities and high security, such as antioxidation, anti-aging, anti-diabetes, anti-hypertension, and antibacterial. In recent years, natural and synthetic anti-aging peptides have been extensively studied in vitro, in vivo and clinically. Anti-aging peptides, such as collagen peptides, can affect various physiological pathways of skin, and have significant skin protection effect when applied locally and eaten. These characteristics show that bioactive peptides can improve skin health by providing specific physiological functions. In this review, we summarized the research of anti-aging peptides and the finishing of anti-aging peptides on improving skin health which is mainly based on the collagen peptides and the related synthetic peptides.
Chirality is a basic property of nature and plays an important role in several biological activities of living organisms. However, the function of chirality in the self-assembly of natural collagen is still unclear. Herein, we investigated the effect of chirality on the self-assembly of bovine Achilles tendon collagen (BATC) usingd/l-glutamic acid (GA) as model molecules. Kinetic studies indicated that the rate of self-assembly ofd-GA/BATC was faster than that ofl-GA/BATC. Results from scanning electron microscopy showed that collagen fibrils assembled in the presence ofl-GA had a larger diameter than those assembled in the presence ofd-GA. Differential scanning calorimetry and viscoelasticity analyses confirmed thatl-GA/BATC gel had better thermal stability and mobility than the correspondingd-GA/BATC gel. Collectively, these results indicated that molecular chirality can be used as a novel strategy to regulate the performance of collagen self-assembly products. © The Royal Society of Chemistry and the Centre National de la Recherche Scientifique 2021.
The characteristics and self-assembly properties of acid soluble collagen (ASC) from tilapia skin in simulated body fluid (SBF) with different NaCl concentrations were investigated. When the concentration of NaCl was 65 mM, the lag time in the turbidity of collagen fibril formation was 2 min, which increased with the NaCl concentration. However, the collagen fibril forming degree decreased with the increasing NaCl concentration. Gel strength decreased when NaCl concentration increased from 135 mM to 160 mM. Rheological and differential scanning calorimetric analyses showed that the elasticity, melting temperature (Tm), and enthalpy (ΔH) of collagen fibril gel were promoted by the increasing NaCl concentration. Self-assembly could affect the conformation but did not affect denaturation of collagen. The dense fibril network structure of collagen gels was formed at SBF with high NaCl concentration. No obvious change was found in the d-periodicities of assembled fibrils. The amide I, II, and III bands in the Fourier transform infrared spectra of collagen gel moved from 1633, 1538, and 1236 cm⁻¹, respectively, to 1628, 1532, and 1229 cm⁻¹, respectively with the increasing NaCl concentration. These results exhibit that the ASC can self-assemble to form different collagen fibril gels in the SBF by adjusting the NaCl concentration.
Tilapia skin collagen was hydrolyzed by five proteases (trypsin, pepsin, neutral protease, alkaline protease and protamex). The results showed that the tilapia skin collagen hydrolysate (TSCH) obtained by 2 h hydrolysis with trypsin exhibited the highest iron chelating rate. The TSCH was then separated by immobilized metal affinity chromatography (IMAC-Fe²⁺) and obtained the tilapia skin collagen iron-chelating peptides (TSCICP). The iron chelating sites of TSCICP were corresponding to carboxylic groups of Asp/Glu and guanidine nitrogen of Arg/Lys. After chelated with iron ions, TSCICP was folded and aggregated to form spherical particles with increased particle size. The TSCICP-iron complexes could maintain high iron solubility at various pH and in simulated gastrointestinal digestion. The iron bio-accessibility of TSCICP-iron complexes was high than that of ferrous glycinate and ferrous sulfate. Finally, TSCICP was purified by RP-HPLC and identified by LC-MS/MS. Four iron-chelating peptides were identified as GPAGPAGEK (782.39 Da), DGPSGPKGDR (984.46 Da), GLPGPSGEEGKR (1198.59 Da) and DGPSGPKGDRGETGL (1441.68 Da). These results indicating that the iron-chelating peptides derived from tilapia skin collagen could be used as potential dietary iron supplement.
The inhibitory mechanism and transepithelial transport of angiotensin I-converting enzyme (ACE)-inhibitory peptides (VGPV and GPRGF) derived from Alcalase®-and papain-hydrolyzed bovine collagen were investigated. The inhibitory mechanism of VGPV and GPRGF was experimentally determined to be non-competitive and the results were supported by molecular docking data. In silico and in vitro gastrointestinal digestion indicated that VGPV remained resistant to digestive enzymes, while GPRGF was degraded into smaller ACE-inhibitory peptides (GPR and GF). VGPV and GPRGF were transported across monolayers of human intestinal epithelial Caco-2 cells through paracellular pathway and retained their ACE-inhibitory activities. The present study suggests that VGPV and GPRGF may possibly be absorbed and exert antihypertensive effects in vivo.
Low molecular weight (LMW) collagen peptides show skin and bone health benefits for human. However, the production of LMW collagen peptides from land vertebrate sources remains challenging due to the presence of advanced glycation end products (AGEs) cross-links. In this study, the effect of α-amylase pre-treatment on proteolytic production of LMW collagen peptides by papain was investigated; spent hen, bovine, porcine, and tilapia skin collagens (HSC, BSC, PSC, and TSC, respectively) were chosen. Results showed that pre-treatment with α-amylase considerably improved the production of LMW peptides (< 2 kDa) from HSC (33.79 to 67.66%), PSC (86.03 to 90.85%), BSC (6.60 to 28.78%), and TSC (89.92 to 90.27%). The HSC presented the highest carbohydrate content and was increased the most in LMW peptides after amylase pretreatment. These results suggested that α-amylase could cleave glycosidic bonds of AGEs between collagen and thus enhance the production of LMW collagen peptides.
Nowadays, attention has been dedicated towards the development of foodstuffs whose constituents are from natural sources. In this study, grape, mulberry, and carob molasses containing natural sugars were evaluated in order to replace the use of sugar syrup and artificial additives in the production of gummy candy which was prepared by varied gelatin ratios. The molasses which have similar °Brix values (78-79) presented different types and amounts of sugar components. High invert sugar with low sucrose was observed in grape and mulberry but high sucrose with low fructose and glucose appeared in carob molasses. Unlike grape and mulberry, carob based jellies had a whitish appearance possibly as a result of the crystallization due to its high sucrose/invert sugar ratio. For all parameters of TPA, carob candy with 5 g/100 g gelatin and grape candy with 10 g/100g gelatin had the lowest and highest values, respectively. Gelatin concentration dependency trend of hardness, gumminess, chewiness and resilience was determined as grape > mulberry > carob. No significant effect (p > 0.05) on gelling temperatures (21-29 °C) but significant effect (p < 0.05) on melting points (33-39 °C) of molasses types were observed for candies. The properties of grape based candy having higher thermal stability and lower temperature sensitivity were attributed to its higher total sugar contents than other samples. The sensorial acceptability score for molasses gummy candies obtained more than 3.0 on a 5-point hedonic scale. These results illustrate the potential for the use of molasses in a healthier confectionery product development instead of commonly used sugars.
Millions of tons of collagen-rich bovine bone are produced as byproducts of the consumption of beef. Hydrolyzing bovine bone collagen (BBC) is an effective measure for both increasing its added value and protecting the environment. In this study, a kind of recombinant bacterial collagenase mining from Bacillus cereus was successfully performed and applied to hydrolyze BBC to collagen-soluble peptides (CPP). Response surface methodology (RSM) was applied to optimize the processing conditions of antioxidant CPP, attaining a distinguished ABTS free radical scavenging activity of 99.21 ± 0.35% while keeping DPPH free radical scavenging activity and reducing power at high levels under the optimal condition. Furthermore, we identified five new antioxidant peptides by LC-MS/MS with typical collagen repeated Gly-Xaa-Yaa sequence units within the CPP. These results suggest that our recombinant collagenase is a powerful tool for degrading collagen and the CPP are promising candidates for antioxidant and related functional food applications.
Biodegradable polymers obtained from renewable resources, such as chitosan and collagen, are sustainable alternatives to develop environmentally friendly materials. Due to their abundance, biocompatibility and antimicrobial properties, chitosan and collagen could become a suitable source for food and biomedical applications. In particular, chitosan formulations are used for food packaging purposes to develop intelligent packaging with the aim of providing information about the quality of the packaged product or to prepare active packaging and extend food shelf life. In this regard, chitosan nanoparticles can be used to provide a sustained release of active substances. Regarding collagen, denatured collagen or gelatin is prevalently used in food industry as a food additive, microencapsulating agent or biodegradable packaging material due to its rheological properties and physical versatility. In turn, collagen-derived peptides have revealed antioxidant and antihypertensive activity, among other health beneficial effects for cosmetic and nutraceutical applications. Additionally, collagen is widely used in tissue engineering, also combined with chitosan, to achieve the functional properties required for specific applications in the biomedical field. In this sense, collagen/chitosan scaffolds have been used for bone, cartilage and skin regeneration. This research in the design and processing of materials based on proteins and polysaccharides is leading to great advances in food and biomedical fields.
The emphasis on mechanism of collagen self-assembly shows great significance for development of collagen-based materials with targeted attributes. Here, combination of isothermal titration calorimetry (ITC) dilution experiments, circular dichroism (CD) and FTIR measurements were employed to investigate the thermodynamic differences and corresponding mechanisms associated with self-assembly of acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC). Firstly, the microrheology measurements of ASC and PSC under the different temperatures (20 °C, 25 °C, 30 °C and 37 °C) had confirmed the temperature induced collagen aggregation. The several thermodynamic parameters (Gibbs free energy change, enthalpy change and entropy change) and the critical mass concentration (CMC) of ASC and PSC, obtained by ITC dilution experiments, decreased with the rising temperatures. The magnitudes of negative Gibbs free energy changes were always higher for ASC than that of PSC, indicating former was more energetically favorable. Besides, the self-assembly of both two collagens were driven by hydrophobic interactions, as evidenced by a negative heat capacity value (ΔCp,mic<0). Specifically, the hydrophobic effects improved due to the transformation of PPII into β-sheet conformations upon collagen self-assembly, as supported by differential CD spectra and FT-IR measurements. Overall, ASC had a higher PPII population than PSC at most temperatures, which may elaborate the thermodynamic differences of two collagens in terms of secondary structure.
Gelatin is a commonly used gelling agent in many confectionery gel (CG) products such as gummy candies. The rheological behaviors of gelatin in gummy products are still poorly understood. The objective of this study was to investigate how gummy formulation affects rheological behaviors of the gelatin network in both linear and nonlinear viscoelastic regions. The effects of °Brix, acids, hydrocolloids, and nutrients on gelatin gelation in gummies were investigated using both small amplitude oscillatory shear (SAOS) tests and large amplitude oscillatory shear (LAOS) tests. °Brix appeared not to impact the gelling temperature of the gelatin gummy until it reached 80 or higher when the gelling temperature decreased probably due to the extrusion of sugar from the gelatin network. Both citric acid and malic acid weakened the gelatin gummy network due to their restrictive effect on the formation of hydrogen bonds. Incorporating hydrocolloids, such as pectin and agar-agar, into the gelatin gummy showed synergistic effect on the gel network due to the nature of hydrocolloids and the ratio to gelatin in the formulation. Incorporating inulin into gelatin gummy enhanced the gel network through hydrogen bonding between inulin and gelatin. As indicated by the frequency sweep tests, incorporating whey protein isolate caused a whey protein dominated bi-continuous gel network which was enhanced by the presence of gelatin. Large deformation rheological tests showed that the gelatin gummy with 81 °Brix had greater nonlinear behaviors under large shear strains, whereas gelatin gummy with 78 °Brix was more resistant to the large deformation. These gelation and stability differences of gelatin gummy network can contribute to the differences in texture and stability of gummies during processing and storage.
Diabetes mellitus, particularly type 2 diabetes, is a major global health issue, the prevalence of which seems to be on the rise worldwide. Interventions such as healthy diet, physical activity, maintaining a healthy weight, and medication (for those with a diagnosis of diabetes) are among the most effective strategies to prevent and control diabetes. Three-quarters of patients diagnosed with diabetes are in countries with poor financial infrastructure, nutritional awareness and health care systems. Concomitantly, the cost involved in managing diabetes through the intake of anti-diabetic drugs makes it prohibitive for majority of patients. Food protein-derived bioactive pepti-des have the potential of being formulated as nutraceuticals and drugs in combating the pathogenesis and pathophysiology of metabolic disorders with little or "no known" complications in humans. Coupled with lifestyle modifications, the potential of bioactive peptides to maintain normoglycemic range is actualized by influencing the activities of incretins, DPP-IV, a-amylase, and a-glucosidase enzymes. This article discusses the biofunctionality and clinical implications of anti-diabetic bioactive peptides in controlling the global burden of diabetes.
Mostly, collagen is obtained from mammalian sources, but its use is limited because of high cost and various allergic reactions. In this review, different alternative sources of collagen were explored and methods for isolation and peptide generations are summarized. Bioactive peptides are short sequences of 2–20 amino acid residues with positive effect on human health. This review summarizes various biological activities of sea food derived peptides/hydrolysates includes antioxidant, inflammatory, antifreeze, angiotension-I converting enzyme (ACE-I) inhibition, antimicrobial, antiaging, wound healing and anticoagulant activities. Moreover, this review also highlights the therapeutic potential and importance of sea-food derived peptides in various pharmaceutical, biomedical, food and cosmetic industries. This review also proposes biological solution for utilization of seafood derived waste in the development of collagen-based food ingredients that is otherwise cause environmental pollution.
Tilapia (Oreochromis nilotica L.) skin collagen is a meritorious commercial resource to be exploited. The purpose of this study was to obtain, evaluate, and characterize tilapia skin collagen-derived antioxidant hydrolysates (TSCP). AAPH-induced erythrocyte hemolysis assay and antifatigue test in mice were implemented. It was indicated that TSCP treatment at 1 mg mL⁻¹ could effectively attenuate AAPH-induced erythrocyte hemolysis rate from 56.35 ± 2.46% to 18.78 ± 2.48% (p < 0.01). A 2.5 mg/(10 g d) dose of TSCP intragastric administration could observably prolong the exhaustive swimming time of the loaded mice and its mechanism was multiple, including the decrease in the levels of serum lactic acid, serum urea nitrogen, and creatine kinase activity, thus improving the contents of liver and muscle glycogen and endogenous SOD activity. Five oligopeptides from the antioxidant fraction were identified as Gly-Hyp, Glu-Asp, Asp-Hyp-Gly, Glu-Pro-Pro-Phe, and Lys-Pro-Phe-Gly-Ser-Gly-Ala-Thr and then synthesized. Among them, the octapeptide exhibited the strongest antioxidant capacity. Therefore, tilapia skin-derived collagen is a meritorious edible resource for producing commercial functional foods, thus helping to scavenge radicals, protecting erythrocytes, and further resisting fatigue.
As a heparin analogue, sulfonated chitosan (SCS) has been confirmed to have similar structure and properties to heparin which is shown to be a linker molecule having specific binding sites with collagen fibrils. In this study, the effects of a varying concentration of SCS on the self-assembly process of type I collagen were investigated. The study on intermolecular interaction between collagen and SCS was carried out via using ultraviolet-visible (UV–vis) spectrophotometry and circular dichroism (CD) spectroscopy. The addition of SCS did not disrupt the triple helix conformation of collagen. However, the decreased value of Rpn showed that the SCS, to some extent, influenced the percentage of triple helix conformation. The turbidity measurements revealed that the self-assembly rate was increased in the presence of a low concentration of SCS whereas decreased with further increasing the SCS concentration. The observation of microstructure via scanning electron microscopy (SEM) and atomic force microscopy (AFM) exhibited the characteristic D-periodicity, indicating that the presence of SCS did not disrupt the self-assembly nature of collagen. Moreover, the addition of SCS facilitated the lateral aggregation of fibrils, leading to the formation of larger fibrils. The rheological analysis showed that the gelation time of collagen was prolonged with increasing the concentration of SCS, in support of a longer lag-phase duration detected in turbidimetric measurements. We expect that valuable data would be provided in this study for further developing of ECM analogues, and propitious performances could be endowed to these biomimetic materials after SCS incorporation.
The structure–activity relationship (SAR) and release behavior of angiotensin I-converting enzyme inhibitory (ACEi) peptides obtained from enzymolysis of collagen influence the large-scale production of ACEi peptides. However, researchers have paid insufficient attention to these areas. In this study, we extracted collagen from tilapia skin, and hydrolyzed it using three proteases. A total of 270 peptides were released from the collagen parent protein. The SAR of these larger collagen ACEi peptides indicated that the presence of proline at position C2 of three C-terminal sequences has a greater effect on increasing the ACEi activity of the peptide than at position C1. The release behavior of these collagen peptides showed that bromelain and alcalase preferentially cleave the N-terminal region of the collagen α1 subunit and then the C-terminal region. These enzymes evenly cleave regions of the collagen α2 subunit. Collagenase preferentially cleaves the C-terminal region of the collagen subunit, followed by the N-terminal region, and then the middle region. The pattern of peptide release from different proteases and the SAR of larger collagen peptides can help guide food production processes to ensure food safety, and to produce high-quality active peptide products.
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Background
Gelatins are important natural amphiphilic macromolecules and can act as emulsifiers in oil-in-water emulsions due to their surface-active properties. However, they are generally weaker emulsifiers than other surface-active substances. In the past two decades, many studies have worked to understand the relationships of gelatins structures with their function properties and to explore the possible molecular modification methods to improve their emulsion stabilization abilities.
Scope and approach
It is well known that protein structure determines function in natural sciences. Based on this axiom, this review summarizes and discusses the extraction, chemical composition, molecular structure, and molecular modification of gelatins for oil-in-water emulsion development. Finally, the review provides a brief summary and outlook of gelatins as emulsifiers.
Key findings and conclusions
Gelatin sources/organs and extraction methods/parameter have obvious effects on the chemical composition, molecular structure, and emulsifying properties of gelatin. Many molecular modification methods have shown efficient improvements in the interfacial layer molecular structures and emulsion stabilization abilities of gelatins such as physical, chemical, enzymatic, and complex modifications. However, further studies are still required to better understand the relationships of gelatin sources-extraction methods-chemical compositions-molecular structures-molecular modifications-interfacial layer structures-emulsion stabilization abilities. This work can provide basic information on the structure-function relationships of gelatins and can guide the research and development of gelatins as emulsifiers in the future.
Chemical pretreatment of collagen raw materials is time-consuming and environmentally hazardous. Collagen extraction after fermentation pretreatment has not been reported. We extracted and characterized acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) from Nile tilapia (Oreochromis niloticus) skin following fermentation and chemical treatments and comparatively evaluated the feasibility of fermentation. Fermentation-ASC (FASC) and fermentation-PSC (FPSC) yields (4.76 and 8.14 wt%, respectively) were slightly but not significantly higher than chemical-ASC (CASC) and chemical-PSC (CPSC) yields (4.27 and 7.60 wt%, respectively). All extracts were identified as type I collagens by SDS-PAGE and retained their triple helical structure well, as confirmed through Fourier transform infrared spectroscopy. All collagen microstructures under scanning electron microscopy were multi-layered aggregates. These collagens also had similar biochemical properties (i.e. denatured between 36.5 and 37.1 °C, high soluble at pH 1–4 and at <3% [w/v] NaCl). Therefore, fermentation method is a viable alternative for pretreating collagen extraction materials.
Gelatin-based traditional Chinese medicines have long been used to treat anemia. Here, rats on the gelatin-based AIN-93G diet showed higher hemoglobin regeneration efficiencies and liver iron concentrations than those fed the diets based on several other animal proteins from muscle sarcoplasm and fibrils, egg white, whey and casein. However, among these animal proteins, gelatin had the lowest digestibility under simulated gastric-proximal intestinal digestion, and its hydrolysate showed the lowest capacity to aid iron absorption in Caco-2 monolayers via templating ferric oxyhydroxide nanoparticles. In another rat hemoglobin regeneration assay, dietary supplementations with gelatin and its two major degradation products, glycine and prolyl-hydroxyproline, revealed that gelatin boosted iron absorption not through glycine, but rather via prolyl-hydroxyproline, which had inhibitory and stimulatory effects on the plasma levels of hepcidin and erythropoietin, respectively. Dietary gelatin thus seems to enhance non-heme iron absorption via regulating systemic iron homeostasis rather than via solubilizing luminal ferric iron.
Effect of pigskin gelatin and its hydrolysates on overall changes that frozen dough underwent during storage was investigated. The results showed that gelatin from pigskin could fortified the frozen dough bread quality, embodying in larger bread volume, softer and more uniform bread crumb. Impact of pigskin gelatin on changes in the structure of gluten network in frozen dough was evaluated by different techniques. SDS-polyacrylamide gel electrophoresis (SDS-PAGE) showed gelatin may inhibit the crosslinking of HMW macromolecules and entangle with SDS-soluble LMW proteins. The increased SDS-soluble proteins suggested a lower aggregation extent of glutenin macropolymer (GMP) caused by pigskin gelatin. However, the significant reduction in GMP depolymerization degree and thiol groups (-SH) content after 60-day frozen storage in presence of gelatin indicated the formation of a more resistant gluten structure against the distortion of ice crystals. There were no significant differences in the alteration of secondary structure and high-temperature stability between gelatin-depleted and gelatin-fortified groups. Nevertheless, the effect of pigskin gelatin on qualities of frozen dough was independent on its hydrolysis degree.
The diverse application of collagen has created a need to discover renewable and economical sources with prevailing/improved physico-chemical properties. To address this scenario, the present study has extracted collagen from Human Amniotic Membrane (AM) and Umbilical cord, which are treated as medical waste and compared its physico-chemical properties. Collagen was extracted by pepsin solubilization using various salt concentrations (1 M, 2 M and 4 M). Umbilical Cord Collagen (UC) yield was 10% higher than Amniotic Membrane Collagen (AC). UC reported 58% higher sulphated glycosaminoglycan content than AC. Electrophoretic pattern of AC and UC in both disulphide bond reducing and non-reducing conditions showed bands corresponding to collagen type I, III, IV, V and XV. Collagen morphology was examined using SEM and the amino acid content was quantified by HPLC and LC-MS/MS. Triple helicity was confirmed by CD and FTIR spectra. Thermal transition temperature of AC and UC was found equivalent to animal collagen. Self-assembly, fibril morphology and spatial alignment was studied using AFM and DLS. Biocompatibility was analyzed using 3T3 fibroblast cells. In conclusion, UC with higher yield, presented with better physico-chemical, structural and biological properties than AC could serve as an efficient alternative to the existing animal collagen for diverse applications.
The purpose of this work was to characterize the dynamic texture perception and study the mechanisms occurring in bolus from chewing to swallowing during white bread oral processing. Results indicated that the microstructural and chemical composition properties determined the oral processing behaviors. At the initial stage of oral processing, the roughness, hardness, and dryness perception were the dominant attributes. At the end of oral processing the adhesiveness and softness perception were dominant, which correlated to the higher bolus water content and adhesive properties. The softness and adhesiveness perception were the key factors that trigger swallowing. In vitro artificial mastication experiments confirmed that mucin rapidly increased the adhesive force of bolus at the initial stage of oral processing, whereas α-amylase gradually increased the adhesive force. These results can help to better understand the dynamic texture perception and its change mechanisms during oral processing.
Collagen and elastin are the most abundant structural proteins in animals and play an integral biological and structural role in the extracellular matrix. The biosynthesis and maturation of collagen and elastin occurs via multi-step intracellular and extracellular processes including the formation of several covalent crosslinks to stabilise their structure, confer thermal stability and provide biochemical properties to tissues. There are two major groups of crosslinks based on their formation pathways, enzymatic and non-enzymatic. The biosynthesis of enzymatic crosslinks starts with the enzymatic oxidation of lysine or hydroxylysine residues into aldehydes. These aldehdyes undergo a series of spontaneous condensation reactions with lysine, hydroxylysine or other aldehdye residues to form immature covalent crosslinks which are further matured via poorly understood mechanisms into multivalent crosslinks. While enzymatic crosslinks make up the majority of protein-protein crosslinks, the non-enzymatic unselective glycation of lysine residues via the Maillard reaction results in the formation of Advanced Glycation Endproducts (AGEs). These latter biosynthesis pathways are not fully understood as they are produced by a series of oxidative reactions between carbohydrates and collagen via Amadori rearrangements. Both covalent crosslinks and AGEs appear to correlate with several diseases such as skin and bone disorders, cancer metastasis, diabetes, Alzheimer's and cardiovascular diseases. Although several crosslinks are isolated, purified and described in collagen and elastin, only a few of them are chemically synthesized. Chemical synthesis plays an essential and important role in research providing pure crosslinks as reference materials and enabling the discovery of compounds to understand the biosynthesis of crosslinks and their properties. Synthetic crosslinks are crucial to verify the structures of collagen and elastin crosslinks where only a handful of structures have been determined by NMR spectroscopy and many other structures have only been predicted using mass spectrometry. This makes crosslinks and AGEs an interesting target for organic synthesis to produce sufficient quantities of material to enable studies on their biological significance and determine their absolute stereochemistry. The biological and chemical synthesis of both enzy-matic and non-enzymatic crosslinks are extensively described in this review. Collagen Collagen is integral for the structure of the extracellular matrix (ECM) and therefore vital for living organisms like mammals. 1 Collagen is expressed throughout all organs and tissues making it the main component of connective tissues in the body. 2 In vertebrates, up to 28 different types of collagen are known, most of them interact with other ECM proteins to form supramolecular network architecture which play a vital part in cell adhesion, migration and proliferation as well as providing strength. 3 The most common type is the fibrillar type I collagen (Col-I) contributing about 90% of total collagen content in the body. Col-I has an average size of 3000 amino acid residues and is involved in the formation of the structural network of tissues including skin, tendons, bones, cornea and the vascular system. 4 There are significant differences between the amino acid number and sequence, structure, and the role of different col-lagen types, however all share a common feature of at least one triple helical domain. 5 This domain is formed by three helical polyproline type II (PP-II) chains tightly packed into a right-handed triple helix which consists of a characteristic repeating amino acid motif (X AA-Y AA-Gly)n. Glycine occupies every third position in the sequence which fit into the centre of the triple helix, therefore larger residues are not tolerated. Even minor
We investigate the sol-gel transition of aqueous pig-skin gelatin solutions at different concentrations and temperatures. In particular, we characterize the isothermal gelation kinetics close to the critical melting temperature, previously evaluated with dynamic temperature ramp tests. The time evolution of the moduli is analyzed at a specific fixed frequency and at various temperatures and concentrations. The isothermal study allows to evaluate the gel time and to determine its dependence on concentration and temperature.
The study of the gelation kinetics over a wide range of concentrations allows to link the behavior in solution to the gelation phenomenon, confirming a different temperature dependence of the sol-gel transition according to the concentration regime.
Although some models are available to describe this dependence, they, however, do not simultaneously account for the effect of both parameters (i.e. temperature and concentration). Here, we propose a full empirical model that accommodates the dependence upon both temperature and concentration.
The optimal formulation of gluten-free functional noodles (GFN) based on rice (70%) and cassava (30%) flour enriched with gelatin hydrolysates was studied. The effect of pregelatinized flour (rice: cassava, 70:30) (X1, 10–30%), fish gelatin hydrolysates (X2, 1–5%) and transglutaminase (X3, 0.1–1.0%) on physiochemical, functional and sensory properties of GFN were evaluated by using a response surface methodology (RSM) with Box and Behnken design. The results showed that a quadratic equation was appropriate for all models with high R² value (0.90–0.98). Optimum conditions for X1, X2 and X3 were 20.5, 5.0 and 0.25%, respectively. The optimized GFN had a 1.16 mm thickness, 24% cooking loss, 279% cooking weigth, 179% water absorption, and 0.19 N tensile strength. Antioxidative activities of GFN (IC50) were 0.57 g/mL for DPPH scavenging activity, 0.87 g/mL for ABTS scavenging activity and 0.01 mmol FeSO4/g for FRAP assay. Addition of fish gelatin hydrolysates resulted in GFN noodles with slightly rougher surface. Sensory properties lay in the range of like slightly to like moderately (6–7).