Article

Functional and bioactive properties of collagen and gelatin from alternative sources: A review

Authors:
To read the full-text of this research, you can request a copy directly from the authors.

Abstract

The rising interest in the valorisation of industrial by-products is one of the main reasons why exploring different species and optimizing the extracting conditions of collagen and gelatin has attracted the attention of researchers in the last decade. The most abundant sources of gelatin are pig skin, bovine hide and, pork and cattle bones, however, the industrial use of collagen or gelatin obtained from non-mammalian species is growing in importance. The classical food, photographic, cosmetic and pharmaceutical application of gelatin is based mainly on its gel-forming properties. Recently, and especially in the food industry, an increasing number of new applications have been found for gelatin in products such as emulsifiers, foaming agents, colloid stabilizers, biodegradable film-forming materials and micro-encapsulating agents, in line with the growing trend to replace synthetic agents with more natural ones. In the last decade, a large number of studies have dealt with the enzymatic hydrolysis of collagen or gelatin for the production of bioactive peptides. Besides exploring diverse types of bioactivities, of an antimicrobial, antioxidant or antihypertensive nature, studies have also focused on the effect of oral intake in both animal and human models, revealing the excellent absorption and metabolism of Hyp-containing peptides. The present work is a compilation of recent information on collagen and gelatin extraction from new sources, as well as new processing conditions and potential novel or improved applications, many of which are largely based on induced cross-linking, blending with other biopolymers or enzymatic hydrolysis.

No full-text available

Request Full-text Paper PDF

To read the full-text of this research,
you can request a copy directly from the authors.

... The amino acid composition of gelatin is specific for each species and tissue type from which it is extracted, as well as the molecular weight distribution, resulting mainly from processing conditions (Abedinia et al., 2020;Gómez-Guillén et al., 2011). The physicochemical properties and functionalities of gelatin are mainly related to the composition of amino acids, which have glycine-proline-proline or glycine-prolinehydroxyproline repeating chains, and the N-and C-terminal regions are generally composed of residues of lysine and hydroxylysine (Hyl) and aldehyde derivatives (Gómez-Guillén et al., 2011;Karim & Bhat, 2009). ...
... The amino acid composition of gelatin is specific for each species and tissue type from which it is extracted, as well as the molecular weight distribution, resulting mainly from processing conditions (Abedinia et al., 2020;Gómez-Guillén et al., 2011). The physicochemical properties and functionalities of gelatin are mainly related to the composition of amino acids, which have glycine-proline-proline or glycine-prolinehydroxyproline repeating chains, and the N-and C-terminal regions are generally composed of residues of lysine and hydroxylysine (Hyl) and aldehyde derivatives (Gómez-Guillén et al., 2011;Karim & Bhat, 2009). Table 1 presents the main sources of extracted and commercialized gelatins, as well as their physicochemical characteristics. ...
... Regarding the extraction method, type A gelatin is obtained by acid extraction, resulting in gelatin with an isoelectric point between 7 and 9, which is the most commonly used method for covalently bound collagens with a lower degree of crosslinking Gómez-Guillén et al., 2011). Type B gelatin is the result of alkaline denaturation and has an isoelectric point ranging from 4 to 5, a method generally applied to more complex collagens, compared to type A gelatin, causing type B gelatin nanoparticles to have a higher degree of higher crosslinking and degrade more slowly (Ahmad et al., 2017;Gómez-Guillén et al., 2011). ...
Article
Gelatin is the product resulting from collagen denaturation, which, in addition to conventional sources of extraction, can be recovered from wastes and byproducts rich in collagen widely generated by the industrial activities of poultry and cattle slaughterhouses and the fishing industry. Given the properties of good film-forming ability, nontoxicity, and biocompatibility for the addition of other compounds to obtain composite materials, gelatin is a potential polymer for the production of biodegradable films and, if extracted from waste sources, can contribute to the reduction of environmental pollution and positively impact several of the Sustainable Development Goals from the United Nations Organization. The gelatins extracted from porcine, poultry, and fish skins and untanned bovine hide wastes, or by-products can be used for the production of packaging films or edible coatings, while chromium-tanned leather wastes can be applied with mulching films in agriculture aiming at greater crop yield for food production. Also, the crosslinking of gelatin protein chains and the addition of plasticizers and other additives have shown promising results in improving gelatin films' mechanical, barrier, and solubility properties. In this sense, this paper reviewed gelatin-based films from wastes, covering the main characteristics of gelatin, techniques for film production and characterization, and applications of obtained films for the food field, in addition to considerations about social, environmental, and economic aspects.
... The increase in the number of food, pharmaceutical, and cosmetic products has led to an increase in the use of gelatin to some 450 kilotons in 2018 for gelling, stabilizing, emulsifying, and water-binding [1][2][3]. At the commercial scale, the gelatin production sources have been produced from by-products of mammalian animals, including pigs and cows, by partial hydrolysis of skin, cartilage, and bones [4]. With a great concern for food safety, questions regarding bovine spongiform and foot and mouth diseases associated with bovine gelatin, as well as strict religious issues of porcine gelatin [1][2][3][4][5], have driven the use of by-products of fish from marine sources as an alternative commercial gelatin. ...
... At the commercial scale, the gelatin production sources have been produced from by-products of mammalian animals, including pigs and cows, by partial hydrolysis of skin, cartilage, and bones [4]. With a great concern for food safety, questions regarding bovine spongiform and foot and mouth diseases associated with bovine gelatin, as well as strict religious issues of porcine gelatin [1][2][3][4][5], have driven the use of by-products of fish from marine sources as an alternative commercial gelatin. Fish gelatin has also been potentially certified in accordance with kosher and halal regulations [6,7]. ...
... Gelatin gel is a thermo-reversible gel where the denatured coils of collagen form a network structure maintained by hydrogen bonds within junction zones [22]. Reviews of factors affecting gelatin quality are the source of marine raw material; chemicals used for pretreatment; pH; and extraction conditions of temperature and time [1][2][3][4][5]. Among one of the marine animals, jellyfish has been researched concerning gelatin. ...
Article
Full-text available
The use of by-products of salted jellyfish for gelatin production offers valuable gelatin products rather than animal feed. Several washes or washing machines have reported removing salt in salted jellyfish. However, the green ultrasound technique has never been reported for the desalination of salted jellyfish. The objectives were to determine how effectively the raw material's salt removal was done by combining the traditional wash and then subjected to the ultrasonic waves in a sonication bath for 20-100 min. For gelatin production, the ultrasonicated jellyfish by-products were pretreated with sodium hydroxide and hydrochloric acid, washed, and extracted with hot water for 4, 6, and 8 h. Results showed that the increased duration of ultrasound time increased the desalination rate. The highest desalination rate of 100% was achieved using 100 min ultrasonic time operated at a fixed frequency (40 kHz) and power (220 W). The jellyfish gelatin extracted for 4, 6, and 8 h showed gel strengths in 121-447, 120-278, and 91-248 g. The 80 min ultrasonicated sample and hot water extraction for 8 h (JFG80-8) showed the highest gel yield of 32.69%, with a gel strength of 114.92 g. Still, the 40 min ultrasonicated sample with 4 h of extraction delivered the highest gel strength of 447.01 g (JFG40-4) and the lower yield of 10.60%. The melting and gelling temperatures of jellyfish gelatin from ultrasonicated samples ranged from 15-25°C and 5-12°C, which are lower than bovine gelatin (BG) and fish gelatin (FG). Monitored by FITR, the synergistic effect of extended sonication time (from 20-100 min) with 4 h extraction time at 80 °C caused amide I, II, and III changes. Based on the proteomic results, the peptide similarity of JFG40-4, having the highest gel strength, was 17, 23, or 20 peptides compared to either BG, FG, or JFG100-8 having the lowest gel strength. The 14 peptides were similarly found in all JFG40-4, BG, and FG samples. In conclusion, for the first time in this report, the improved jellyfish gel can be achieved when combined with traditional wash and 40 min ultrasonication of desalted jellyfish and extraction time of 4 h at 80 °C.
... Important areas of research are the stabilization of various foods environments, including the study of the properties of colloids [1][2][3][4][5], structuring of food systems with the disclosure of biopolymer potential (proteins, polysaccharides, etc.), technology development in various industries, including food recipes based on natural raw materials. The main tasks of work are to compare the features of structuring the biopolymers of different groups and their influence on the technological and consumer properties of culinary products on a meat basis. ...
... A generalization of the research results made it possible to confirm the concept of the formation of structures based on natural biopolymers, some salts, etc., to give a fairly complete and detailed histological picture of fibrous protein systems and food products, positively assess the physicochemical changes, including architectonics (relative homogeneity of system, cohesion, etc.), therefore, the texture and other organoleptic properties of food products. The performed developments correspond to the modern level of research on biopolymers, their functional and technological features and applications [5,6], including the production of meat semi-finished products and products, such as hamburgers, cutlets, etc. [7]. ...
Article
Full-text available
The features of the structure and properties of raw materials, which are a source of biopolymers of natural origin are presented. The main focus of the theoretical part is paid to the study of the process of structuring of biopolymers (proteins and polysaccharides). Practical approbation was carried out on the example of meat-containing meat and meat chopped products and semi-finished products.
... While in the production of processed meat like head cheese, chicken rolls and jellied meat, gelatin is used to absorb meat juices and give strength to the products. Gelatin turns out to be irreplaceable supporting materials in food industry for its ultimate physical properties, great purity content and various uses [2]. ...
... They can reversibly turn into liquid from gelling from when heated at certain temperature. Some plant hydrocolloids such as carrageenan and agar can perform thermally reversible gels too, however the melting points are slightly higher than that gelatin gels [2]. ...
Article
Gelatin is a common ingredient used in various industrial sectors including food and beverage, cosmetic, pharmaceutical as well as biomedical. Due to inexpensive processing cost and shorter processing time, porcine becomes the main source of gelatin. Thus, the application of this ingredient creates several problems especially issues related to its halal status among Muslim community. The present study aims at reviewing the development of gelatin from halal sources and their potential as alternatives to substitute the sources of non-halal gelatins. The applications of gelatin in food industry and the current issues on halal gelatin have been discussed in detail. The halal source of gelatin required intense study due to prominent demand of it not only in food industry but also in pharmaceutical industry. The development of halal gelatin provides Muslim alternatives and choices to consume gelatin as food and pharmaceutical products and yet complying with Islamic obligations.
... Besides, its surface showed features related to an emulsion, foam formation, and the capability to penetrate a lipid-free interface 9 . The collagen structure with its exceptional amino acid configuration gives it the properties of antioxidative and antihypertensive, antimicrobial activity, and immunomodulatory activity 10 . Therefore, its importance is derived from having a biocompatible, biodegradable, and weak antigenicity and immunogenicity in comparison with other types of biopolymers, for instance, gelatin and albumin 11,12 . ...
... Therefore, its importance is derived from having a biocompatible, biodegradable, and weak antigenicity and immunogenicity in comparison with other types of biopolymers, for instance, gelatin and albumin 11,12 . Therefore, understanding the physiological structure and mechanical integrity of native collagen helps us in further enhancing the extraction procedure and artificial collagenous synthesis for biomedical and pharmaceutical applications, food manufacturing, as well as for cosmetics 10,13 . ...
Article
Full-text available
Background: In the recent years, the focus on taking out biologically active molecules from animals' byproducts, especially from marine organisms have been increased. These sources play a major role in extracting collagen to be used as a biomaterial for medical applications and in the food industry. However, collagen-producing firms can be found all around the world, but not all of them kind 100% pure collagen; instead, they make gelatin hydrolyzed collagen. These businesses lack additional collagen development. Therefore, extracting collagen from fish scales as a potential raw material and using it to study high-value applications might potentially produce an economic potential for anti-inflammatory protein.
... The regression equation for the ash content of the first gelatin fraction was as follows: ℎ (%) = −0.448 + 4.37 + 0.0095 − 0.0193 x (17) According to the p-factor, the significance level for factor A was 0.001, for factor B 0.067, and for factors A and B 0.792. With 95% probability, we can say that factor A, the amount of enzyme added, has a significant effect on the ash content of the first gelatin fraction. ...
... However, the study did not indicate the content of ash in the gelatins. If the ash content is less than 2.0% within the study, high-quality gelatin can be applied to the production of hard gelatin capsules or to the production of collagen films that can be applied to burns [17]. The 182-360 Bloom gelatins were extracted from HCl conditioned chicken paws collagen [22]. ...
Article
Full-text available
With the increasing consumption of poultry meat around the world, the use of chicken stomachs as a source of collagen is being offered. The objective of this study was to extract gelatin from the stomachs of broiler chickens and to estimate their gel strength, ash content, viscosity, gelling point, melting point, clarity and digestibility. An innovative biotechnological method based on the conditioning of collagen with a microbial endoproteinase (Protamex®) and hot-water extraction was used to control the chemical and thermal denaturation process of collagen to prepare gelatin. The experiments were planned using a Taguchi design, 2 factors at 3 levels; factor A for the amount of proteolytic enzyme (0.10, 0.15 and 0.20%) and factor B for the extraction temperature (55.0, 62.5 and 70.0 °C). Data were statistically processed and analyzed at a significance level of 95%. The gelatin yield averaged 65 ± 8%; the gel strength ranged from 25 ± 1 to 439 ± 6 Bloom, the viscosity from 1.0 ± 0.4 to 3.40 ± 0.03 mPa·s, gelling point from 14.0 ± 2.0 to 22.0 ± 2.0 °C, melting point from 28.0 ± 1.0 to 37.0 ± 1.0 °C. The digestibility of gelatin was 100.0% in all samples; the ash content was very low (0.44 ± 0.02–0.81 ± 0.02%). The optimal conditions for the enzymatic treatment of collagen from chicken stomachs were achieved at a higher temperature (70.0 °C) and a lower amount of enzyme (0.10–0.15%). Conditioning chicken collagen with a microbial endoproteinase is an economically and environmentally friendly processing method, an alternative to the usual acid- or alkaline-based treatment that is used industrially. The extracted products can be used for food and pharmaceutical applications.
... Another significant factor affecting the mechanical properties of gels is the hydrogels' tendency to swell. 55,56 From the SEM images ( Figure 2D), the component lyophilized hydrogel scaffolds contained interconnected pores, which demonstrated good swelling capabilities. As shown in Figure 3G, the mean swelling rates of Alg, Gel, GA, and GA-nCeO 2 hydrogel scaffolds were, respectively, 72.68 ± 2.31%, 45.39 ± 3.18%, 65.86 ± 3.78%, and 70.00 ± 4.58%. ...
... The structure of Alg exhibited increased stiffness and Gel provided a matrix with a precise shape for cell adhesion and value addition. 56,62 Mechanical strength was substantially impacted by the hydrogel scaffold's porosity and degree of cross-linking. 63,64 In addition to preventing the irreversible hydrolysis of Gel, using cationic crosslinked Gel gives it more mechanical strength than the simple Gel fraction. ...
Article
Full-text available
Background: Clinicians frequently face difficulties when trying to fix bone abnormalities. Gelatin-Alginate (GA) is frequently employed as a carrier because it is non-toxic, biodegradable, and has a three-dimensional network structure. Meanwhile, cerium oxide nanoparticles (nCeO2) demonstrated high antioxidant enzyme simulation activity. Therefore, in order to develop a porous hydrogel scaffold for the application of bone tissue engineering, an appropriate-type GA-nCeO2 hydrogel scaffold was developed and evaluated. Methods: GA-nCeO2 hydrogel scaffold was prepared by the lyophilized method and characterized. The surface morphology and cell adhesion of the scaffold were observed by the scanning electron microscope. CCK8 and live-dead staining methods were used to evaluate its biological safety and cell proliferation. Then the osteogenic differentiation in early and late stages was discussed. The expression of osteogenic genes was also detected by RT-PCR. Finally, a bone defect model was made in SD rats, and bone formation in vivo was detected. Results: The results showed that GA-nCeO2 hydrogel scaffold exhibited a typical three-dimensional porous structure with a mean pore ratio of 70.61 ± 1.94%. The GA-nCeO2 hydrogel was successfully endowed with simulated enzyme activity including superoxide dismutase (SOD) and catalase (CAT) after the addition of nCeO2. Osteoblasts demonstrated superior cell proliferation and adhesion on composite scaffolds, and both mineralization test and gene expression demonstrated the strong osteogenic potential of GA-nCeO2 hydrogel. The outcomes of hematoxylin and eosin (H&E) staining and Masson trichrome staining in the femoral defect model of SD rats further supported the scaffold's favorable biocompatibility and bone-promoting capacity. Conclusion: Due to its favorable safety, degradability, and bone formation property, GA-nCeO2 hydrogel was anticipated to be used as a potential bone defect healing material.
... Structurally, the proposed three chains together form a 3-phases wound healing platform by generating a hydrogen bond among the side chain of glycine to -NH peptide of hydroxyproline and =CH of proline. Since glycine, proline, and hydroxyproline/hydroxylysine are abundant in collagen, so the structure of collagen is largely centered on intra-and inter-chain hydrogen bonding, with GLY-X-Y standing for as previously depicted in Fig. 2. Approximately 4-8 collagen molecules are attached with covalent bonds forming collagen fibrils [66], where X indicates proline and also Y indicates hydroxyproline. Sometimes modifications of a certain amount of lysine and proline residues are hydroxylated through enzyme dominating bio-synthesis. ...
... M.C. Gomez-Guillen added that audited antioxidative and medication properties have presumptively been combined with this single organic compound composition [66]. The biological activities of the super molecule hydrolysates are concerning the amino acid composition, sequence, size, and configuration of peptides [91]. ...
Article
Full-text available
Essentially cell forming and vigorous conjunctive tissues such as skin, joints, ligaments, and bones are expressed as fibril forming the most abundant protein collagen in the human body substantially about one-quarter by weight. Additionally, amongst the biopolymers, the collagen macromolecule is serving humanity in myriad ways. Although it has been used in cosmetics for a long time, nowadays its biological characteristics like nontoxic, biocompatible, biodegradable, structural integrity, cellular affinity and weak antigenicity have encouraged using of it significantly in biomedical and pharmaceutical applications. Its excellent biodegradability and notable bioactivity by endogenous collagenases enzyme convert exogenous collagen for biomedical use. Triple helix 29 collagen composed of three α-chain characteristic variants, type I is the most suitable extracellular matrix (ECM) macromolecule gradually consumed thickness and strength with time being, can be correlated with skin aging phenomena. This review focuses on the sources, structures, extractions, and properties (e.g., bioactive, mechanical, viscoelastic, tensile, etc.) of collagen proteins for use in biomedical applications. The abundance of collagen protein from a natural source can be effectively used in human tissue scaffolds, cardiac implantation, wound healin g, cornea membranes, dental membrane, dermal filler, cosmetic surgery, etc. as highlighted in this review. The application-based advantages and disadvantages of body-suits collagen are also discussed with prospects.
... Collagen is an important fibrous protein found in almost all living organisms, as it is the main component of structural tissues (Regenstein & Zhou 2007). In marine animals, collagen is also an important contributor to total proteins in the whole body as it is a major constituent in scales, bones, skin, and fins (Gómez-Guillén et al. 2011;Coppola et al. 2020). However, collagen and collagenous tissues are of particular importance in echinoderms, such as sea urchins, starfishes, and sea cucumbers, because they protect their coelom and body shape, while also playing a key role in motion and defense systems by being the major constituent of their skin, podia, and spines (Santos et al. 2005;Wilkie 2005;Senadheera et al. 2020). ...
Article
Due to their unique biochemical composition, sea cucumbers are highly prized marine echinoderm species. One of their most important properties is that they contain a high amount of collagen in their body wall. In this study, the relationship between collagen and pepsin-solubilized collagen yields from Holothuria tubulosa and Holothuria poli and morphometric and biochemical parameters were investigated. Collagen yields were in the range of 10.63–16.04% for H. tubulosa and 7.12–13.10% for H. poli. It was determined that they may be related to length, body wall weight, and biochemical composition at different length frequencies. Moreover, maturity may have a direct effect on the yield, as mature specimens were found to have lower content of collagen, whereas immature small specimens contained a higher percentage of collagen. It was found that with increasing pepsin concentration, the PSC yield increased to 1.83–1.89% in H. tubulosa and H. poli, respectively. It was determined that collagen from smaller individuals, which contained more moisture and ash, was likely more susceptible to pepsin hydrolyzation. This is the first published study demonstrating that collagen yield of sea cucumbers can vary with length, weight, maturity, and biochemical composition, in addition to species-specific differences.
... On another note, one of the naturally occurring polymers utilized often in numerous industries is gelatin, especially in clinical settings and bioengineering applications. Gelatin is a highly compatible, highly soluble, abundant and cheap raw material and, most importantly, biodegradable [6][7][8]. Gelatin is a collagen derivative through different approaches: heating or enzymatic, to produce authentic short peptides. It shows less toxicity occur from accidents or burning that lead to skin wound healing. ...
Article
Full-text available
A skin wound without immediate treatment could delay wound healing and may lead to death after severe infection (sepsis). Any interruption or inappropriate normal wound healing, mainly in these wounds, commonly resulted in prolonged and excessive skin contraction. Contraction is a common mechanism in wound healing phases and contributes 40–80% of the original wound size post-healing. Even though it is essential to accelerate wound healing, it also simultaneously limits movement, mainly in the joint area. In the worst-case scenario, prolonged contraction could lead to disfigurement and loss of tissue function. This study aimed to fabricate and characterise the elastin-fortified gelatin/polyvinyl alcohol (PVA) film layered on top of a collagen sponge as a bilayer hybrid biomatrix. Briefly, the combination of halal-based gelatin (4% (w/v)) and PVA ((4% (w/v)) was used to fabricate composite film, followed by the integration of poultry elastin (0.25 mg/mL) and 0.1% (w/v) genipin crosslinking. Furthermore, further analysis was conducted on the composite bilayer biomatrix’s physicochemical and mechanical strength. The bilayer biomatrix demonstrated a slow biodegradation rate (0.374967 ± 0.031 mg/h), adequate water absorption (1078.734 ± 42.33%), reasonable water vapour transmission rate (WVTR) (724.6467 ± 70.69 g/m2 h) and porous (102.5944 ± 28.21%). The bilayer biomatrix also exhibited an excellent crosslinking degree and was mechanically robust. Besides, the elastin releasing study presented an acceptable rate post-integration with hybrid biomatrix. Therefore, the ready-to-use bilayer biomatrix will benefit therapeutic effects as an alternative treatment for future diabetic skin wound management.
... These collagens are predominantly sourced from discarded porcine and bovine hides, tendons, bones and hooves from commercial abattoirs [13]. However, religious constraints and increasing social concern over the ethics of cultivating animal products have led to a rise in research into alternative collagen sources [14]. ...
Article
Full-text available
Collagen is the most ubiquitous biomacromolecule found in the animal kingdom and is commonly used as a biomaterial in regenerative medicine therapies and biomedical research. The collagens used in these applications are typically derived from mammalian sources which poses sociological issues due to widespread religious constraints, rising ethical concern over animal rights and the continuous risk of zoonotic disease transmission. These issues have led to increasing research into alternative collagen sources, of which marine collagens, in particular from jellyfish, have emerged as a promising resource. This study provides a characterization of the biophysical properties and cell adhesion interactions of collagen derived from the jellyfish Rhizostoma pulmo (JCol). Circular dichroism spectroscopy and atomic force microscopy were used to observe the triple-helical conformation and fibrillar morphology of JCol. Heparin-affinity chromatography was also used to demonstrate the ability of JCol to bind to immobilized heparin. Cell adhesion assays using integrin blocking antibodies and HT-1080 human fibrosarcoma cells revealed that adhesion to JCol is primarily performed via β1 integrins, with the exception of α2β1 integrin. It was also shown that heparan sulfate binding plays a much greater role in fibroblast and mesenchymal stromal cell adhesion to JCol than for type I mammalian collagen (rat tail collagen). Overall, this study highlights the similarities and differences between collagens from mammalian and jellyfish origins, which should be considered when utilizing alternative collagen sources for biomedical research.
... Interestingly, marine collagen is also metabolically compatible, water soluble, lacks religious constraints and is considered free of animal pathogens [12][13][14]. In food sector, collagen is used as a gelatin precursor in the production of emulsions, foams, colloids, and biodegradable films [15] or as source of collagen peptides that can be absorbed into mucosa via a buccal delivery system [16]. ...
Article
Full-text available
The industrial processing of fish for food purposes also generates a considerable number of by-products such as viscera, bones, scales, and skin. From a value-added perspective, fish by-products can act also as raw materials, especially because of their collagen content (particularly in fish skin). Interestingly, the potential of marine collagen for cosmetic applications is enormous and, remarkably, the extraction of this protein from fish skins has been established for different species. Using this approach, we investigated the integration of marine collagen (COLRp_I) extracted from the skin of the Greenland halibut as an active ingredient in a cosmetic hydrogel formulation. In this study, extracts of marine collagen at concentrations up to 10 mg/mL showed a non-cytotoxic effect when cultured with fibroblast cells for 3 days. In addition, marine collagen extract, when incorporated into a cosmetic hydrogel formulation, met criterion A of ISO 11930:2019 regarding the efficacy of the preservative system (challenge test). In addition, the cosmetic formulations based on marine collagen at dosages of 0.1, 0.25 and 0.5% were tested in a clinical study on the skin of the forearms of 23 healthy volunteers, showing a sightly hydration effect, suggesting its potential for beauty applications. Moreover, this work illustrates that the circular economy concept applied to the fish processing industry can represent important benefits, at innovation, environmental and economic levels.
... The positive effects of collagen hydrolysates include antioxidant, anti-aging, anti-tumor, anti-inflammatory, and anti-obesity properties [21]. Collagen hydrolysates from the bones of domestic yaks (Bos grunniens) have been found in a study to have immune-stimulating properties and to have the ability to enhance mice's innate and adaptive immunity [22]. ...
Article
Full-text available
Important dietary components known as nutraceuticals have both therapeutic and nutritional impacts. The active ingredients in these foods, including such carotenoids, collagen hydrolysate, and dietary fibers, are what provide them their health benefits. Nutraceuticals have been shown to have a good impact on immunological and cardiovascular health, as well as play a part in the prevention of infections and cancer. Depending on its nature and manner of action, nutraceuticals can be divided into many types. Various nutraceutical categories and their therapeutic potential effects, including anti-cancer, antioxidant, anti-inflammatory, and anti-lipid activity in disease, will be examined in this study. In addition, the many ways in which these accepted methods and structures, their application, and human safety would be covered, along with recent trends and nutraceuticals’ potential for the development.
... These biologically active peptides are not active when encapsulated in proteins but are activated and released from their precursors only after food processing, exogenous enzyme hydrolysis, or gastrointestinal digestion [8,9]. Owing to their high bioactivity, biocompatibility, and safety [10,11] properties, collagen peptides are increasingly utilized for their anti-hypertension [12], antioxidant [13], and antitumor [14] effects, and in the field of cosmetics [15]. ...
Article
Full-text available
Type I and V collagens are the major components of fibrillogenic proteins in fish skin, and their hydrolysis products possess hyaluronidase inhibitory activity. In this study, for the first time, type I and V collagens were isolated from the skin of shortbill spearfish and striped marlin. Type I (2α1[I]α2[I]) and type V (α1[V]α3[V]α2[V]) collagens composed of distinct α-peptide chains with comparable structures were investigated using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and UV spectrophotometric chromatography. After enzymatic digestion, the collagen peptides were purified by using ultrafiltration (30 KDa) and high-performance liquid chromatography (RP-HPLC) to yield CPI-F3 and CPV-F4 fractions with strong hyaluronidase inhibition rates (42.17% and 30.09%, respectively). Based on the results of simulated gastrointestinal fluid, temperature, and pH stability assays, CPI-F3 and CPV-F4 exhibited stability in gastric fluid and showed no significant changes under the temperature range from 50 to 70 • C (p > 0.05). The results of this first research on the bioactivity of type V collagen peptides provide valuable information for the biomedical industry and show the potential for future bioactivity investigations of type V collagen and its peptides.
... As the main component of bone and cartilage, collagen extracted from chicken bones is an important source of useful bioactive peptides (Saiga et al., 2008). In particular, collagen has a gel-forming property and is widely used in the food and pharmaceutical industries (Gómez-Guillén et al., 2011). To efficiently extract and utilize collagen and gelatin, researchers have studied the quality of gelatin extracted from chicken head bones (Ee et al., 2019) and the functional properties of collagen and gelatin extracted from chicken head bones (Du et al., 2013). ...
Article
Full-text available
This study investigated the effect of brown rice-vinegar-induced changes in pH on the physicochemical properties (ash, moisture, protein, fat, collagen, chondroitin sulfate, sugar, and mineral content, color, salinity, and pH) of chicken bone extract. The following treatments were employed: control (purified water, 62%; chicken bones, 30.47%; chicken feet, 6.88%; garlic, 0.58%; pH 7), T1 (purified water, 62%; chicken bones, 30.47%; chicken feet, 6.88%; garlic, 0.58%; organic brown rice vinegar, 0.01%; pH 6), T2 (purified water, 62%; chicken bones, 30.47%; chicken feet, 6.88%; garlic, 0.58%; organic brown rice vinegar, 0.02%; pH 5), and T3 (purified water, 62%; chicken bones, 30.47%; chicken feet, 6.88%; garlic, 0.58%; organic brown rice vinegar, 0.23%; pH 4). Protein, ash, and chondroitin sulfate contents and the brightness tended to increase, while the yellowness and redness, sugar content, salinity, and pH tended to decrease when the percentage of brown rice vinegar was increased. The collagen content was significantly higher in the control and T3 groups. Further, the Ca content tended to increase, while K, Mg, N, and P contents tended to decrease with increasing percentage of brown rice vinegar. The Ca/P ratio improved as the percentage of brown rice vinegar increased. At a concentration of 0.02%, brown rice vinegar effectively improved the overall quality of chicken bone extract in terms of the investigated physicochemical properties (minerals being the exception). Therefore, use of 0.02% brown rice vinegar during the preparation of chicken bone extract would result in the most ideal physicochemical properties.
... Collagen and its denatured form known as gelatin casing, is considered an important molecule. It offers excellent uniformity of appearance and strength and is usually used to fix the size and shape of processed meat products [84]. Gelatin solution is often injected into cured meats, which solidifies and increases water retention and resistance to cutting. ...
Article
Full-text available
Food adulteration refers to the alteration of food quality that takes place deliberately. It includes the addition of ingredients to modify different properties of food products for economic advantage. Color, appearance, taste, weight, volume, and shelf life are such food properties. Substitution of food or its nutritional content is also accomplished to spark the apparent quality. Substitution with species, protein content, fat content, or plant ingredients are major forms of food substitution. Origin misrepresentation of food is often practiced to increase the market demand of food. Organic and synthetic compounds are added to ensure a rapid effect on the human body. Adulterated food products are responsible for mild to severe health impacts as well as financial damage. Diarrhea, nausea, allergic reaction, diabetes, cardiovascular disease, etc., are frequently observed illnesses upon consumption of adulterated food. Some adulterants have shown carcinogenic, clastogenic, and genotoxic properties. This review article discusses different forms of food adulteration. The health impacts also have been documented in brief.
... In addition, hydroxyproline is an abundant amino acid in animal protein, but is uncommon in plant-source feedstuffs [50,51]. MBM has been characterized by fundamental gelatin properties, including poor solubility in cold water and molecular weight ranging from 15 to 400 kDa, with its properties ultimately depending on the conditions of the manufacturing process [4,52,53]. Therefore, the altered free-HYP content in MSM also might be able to indicate the hydrolysis of MBM after fermentation. In this study, free-HYP increased in all fermented groups, compared to the control group (p < 0.05). ...
Article
Full-text available
In this study, we screen the proteolytic activity of Bacillus species in meat and bone meal (MBM) and investigate the effects of fermented MBM–soybean meal products (FMSMPs) on the growth performance of broilers. In Trial 1, FMSMPs were fermented using four strains—Bacillus siamensis M3 (M3), B. velezensis M5 (M5), B. subtilis M6 (M6), and B. subtilis M20 (M20)—all of which presented more total peptides and higher degrees of hydrolysis (DH) than Bacillus subtilis var. natto N21 (N21). In Trial 2, 280 0-day-old Arbor Acres broilers, with equal numbers of both sexes, were randomly assigned into 5% fish meal (FM), MBM–soybean meal (MSM, as control), and N21, M3, M5, M6, and M20 FMSMP groups. The results demonstrated that the crude protein, total amino acids, alkaline protease, trichloroacetic acid–soluble nitrogen (TCA-SN), TCA-SN/total nitrogen, total peptides, DH, and free-hydroxyproline levels in the M6 group were greater than those in any other group (p < 0.05). Furthermore, the weight gain in the M6 group was superior to that of the FM and MSM groups in 0–21 and 0–35-day-old broilers (p < 0.05). In conclusion, B. subtilis M6 likely efficiently decomposes MSM to improve the protein properties and nutritional value of the product after fermentation. Supplementation with 5% FMSMP may promote weight gain in broilers.
... That is a major essential protein in the connective tissue of animal skin and bone and composes about 30% of the total proteins (Ogawa et al., 2003;Li et al., 2013). It is used as a vehicle for drugs, proteins, and genes, as well as a substitute for human skin, blood vessels and ligaments (Gómez-Guillén et al., 2011). Gelatin is a partially hydrolyzed form of collagen, and mostly it has been used as a potential agent in the food and packaging industry. ...
Book
Full-text available
Dear Colleagues, It was a great honour and pleasure to host the 2th International Symposium on Pufferfish/Lionfish held on 20-22 May 2022 in Turkey, which was organized by - Republic of Turkey Ministry of Agriculture and Forestry General Directorate of Fisheries and Aquaculture, - General Directorate of Agricultural Research and Policies, Mediterranean Fisheries Research, Production and Training Institute, - Iskenderun Technical University Marine Science and Technology Faculty, - Nature and Science Society. The symposium bought together leading scientists in the domain of interest from around the world. Around a hundred participants from 15 different countries presented oral and poster presentations. We would like to thank all participants for their attendance and contribution to the symposium. This book, which has a unique source for researchers, administrative, NGOs, and fishers interested in pufferfish and lionfish, contains abstracts of the presentations (both oral and poster). Many thanks to the scientific and organizing committee, and the others worked voluntarily. Yours sincerely, Cemal Turan Chair of the Symposium
... That is a major essential protein in the connective tissue of animal skin and bone and composes about 30% of the total proteins (Ogawa et al., 2003;Li et al., 2013). It is used as a vehicle for drugs, proteins, and genes, as well as a substitute for human skin, blood vessels and ligaments (Gómez-Guillén et al., 2011). Gelatin is a partially hydrolyzed form of collagen, and mostly it has been used as a potential agent in the food and packaging industry. ...
Conference Paper
Full-text available
Pufferfishes are commonly found in tropical and subtropical marine waters and include 28 genera and approximately 184 species all over the world in marine waters within the Tetraodontidae family. The Tetraodontidae family is famous for the occurrence of the powerful marine paralytic toxins in their body called Tetrodotoxin. For this reason, they have no commercial value except for a few types consumed in Eastern countries. In Turkish marine waters, pufferfish belonging to the Tetraodontidae family represented by 7 species, Lagocephalus lagocephalus, L. sceleratus, L. suezensis, L. guentheri, Sphoeroides pachygaster, Torquigener flavimaculosus and Tylerius spinosissimus. They were reported as invasive alien species in Turkish Marine Waters. Marine species present a rich source of natural source compounds, such as collagen, gelatin, and hydroxyapatite, which are the most abundant valuable products, which can be an alternative source for pharmaceutical and biomedical applications. Alternative management actions are important to mitigate the negative effects stemming from the potential future invasion of pufferfish. Therefore, this review focused on how pufferfish can be brought into the economy.
... Moreover, this protein was also responsible for the anti-adhesive activity against enteropathogenic E. coli 0157: H7 on collagens, reducing the ability to form biofilms by 59.71% compared to the control well [58]. Gelatin is a soluble, degraded form of collagen that is obtained by partial hydrolysis [59]. The comparable results achieved in the present study for these surfaces may be due to their similarities. ...
Article
Full-text available
Lactic acid bacteria (LAB) naturally inhabits the organisms of honeybees and can exhibit adhesive properties that protect these insects against various pathogenic microorganisms. Thus, cell surface (auto-aggregation, co-aggregation, hydrophobicity) and adhesive properties of LAB to two abiotic (polystyrene and glass) and four biotic (collagen, gelatin, mucus, and intestinal Caco-2 cells) surfaces were investigated. Additionally, anti-adhesion activity and the eradication of honeybee pathogen biofilms by LAB metabolites (culture supernatants) were determined. The highest hydro-phobicity was demonstrated by Pediococcus pentosaceus 19/1 (63.16%) and auto-aggregation by Lac-tiplantibacillus plantarum 18/1 (71.91%). All LAB showed a broad spectrum of adhesion to the tested surfaces. The strongest adhesion was noted for glass. The ability to co-aggregate with pathogens was tested for the three most potently adherent LAB strains. All showed various levels of co-aggre-gation depending on the pathogen. The eradication of mature pathogen biofilms by LAB metabo-lites appeared to be weaker than their anti-adhesive properties against pathogens. The most potent anti-adhesion activity was observed for L. plantarum 18/1 (98.80%) against Paenibacillus apiarius DSM 5582, while the strongest biofilm eradication was demonstrated by the same LAB strain against Melissococcus plutonius DSM 29964 (19.87%). The adhesive and anti-adhesive activity demonstrated by LAB can contribute to increasing the viability of honeybee colonies and improving the conditions in apiaries.
... Furthermore, it is a common waste product for industrial food manufacturing processes. 31,32 Gelatin forms chains in a coil conformation. However, during cooling in aqueous solutions, these chains undergo a coil-to-helix transition, thus aligning them within a semi-solid matrix. ...
Article
Full-text available
Manipulation of bacterial cellulose (BC) morphology is important to tune BC properties to meet specific application requirements. In this study, gelatin was added to cultivation media at 0.1–7.5 wt %. After cultivations, gelatin was removed from the BC matrix, and its effects on BC matrix characteristics and fermentation production efficiency were determined. Higher contents of gelatin in cultivation media (up to 5%) resulted in BC that, from scanning electron microscopy observations, had larger pore sizes and formation of a lamina morphology that was highly unidirectional. Crystallinity remained unchanged between 0.1 and 5 wt % gelatin concentrations (92–95%); however, it decreased to 86% at a gelatin concentration of 7.5 wt %. Mechanical properties showed a positive trend as both the specific modulus and specific strength values increased as the gelatin concentration increased to 5 wt %. A breakdown in the ordered structure of the BC matrix occurs at 7.5 wt % gelatin, with corresponding decreases in the specific modulus and specific strength of the BC. The productivity increased by almost 4-fold relative to the control, reaching 1.64 g·L–1h–1 at the 2.5 wt % gelatin content. Also, the water holding capacity increased by 3-fold relative to the control, reaching 306.6 g of water per g BC at the 5.0 wt % gelatin content. The changes observed in these BC metrics can be explained based on literature findings associated with the formation of gelatin aggregates in the cultivation media and an increase in gel stiffness seen at higher media gelatin concentrations. Overall, this work provides a roadmap for manipulating BC properties while creating highly organized lamina morphologies.
... Gelatin is a fibrous protein with a unique sequence of amino acids which is obtained from hydrolyzed collagen [43]. Collagen is the major component of connective tissue such as skin, tendons and bones [44]. According to the treatment method, it is usually divided into acid-treated gelatin and alkali-treated gelatin [45]. ...
Article
Full-text available
Micro-nano hydrogel is a novel functional material that has attracted extensive attention in various fields. Due to the size of micron and nano level, high water content and high specific surface area, the micro-nano hydrogels can achieve minimally invasive repair and are considered as promising agents in tissue repair engineering. In this review, we summarize the design and development of micro-nano hydrogels for biomedical applications, first introduce biopolymers for the synthesis of hydrogels, then introduce the preparation technologies of microgels and nanogels respectively, and systematically summarize the application characteristics and forms of different preparation technologies. Finally, the latest application progresses of microgels in local drug delivery, bone tissue repair, soft tissue repair and immunomodulation are introduced in detail, as well as the latest application progress of nanohydrogels in cartilage repair, antibacterial, antitumor/cancer nerve repair and prevention and diagnosis of diseases, and the key research directions of micro-nano hydrogel preparation technologies in the future are clarified.
... Collagen's commonly used source as a food additive is scale, skin, and bones from cows, pigs, or fish [13,14]. Collagen from fish is known as a halal alternative source [15,16]. ...
Conference Paper
Functional drink is currently an interesting study, especially if they are non-alcoholic based as one of the cornerstones of consumer acceptance in several countries. Roses, which are usually only used as decoration, can actually be processed into functional drink with high antioxidant activity. This study uses the basic ingredients of roses and apples with the addition of fish collagen hydrolysate as a non-alcoholic and halal functional drink. Factorial Randomized Design Group 2 factors were used in this study. The first factor was the Rose-Apple ratio variation consisted of 60:40, 50:50, and 40:60 %v/v. The second factor was Fish Hydrolysate Collagen concentration variation consisted of 0, 0.3, 0.5, and 0.7 %w/v. The data then analyzed with ANOVA at α=5% and Duncan's Multiple Range Test. This study result that rose-apple extract 50 (%v/v) with fish hydrolysate collagen 0.7 (%w/v) is the best formulation. The characteristic of the best formulation is pH 2.88 (match with SNI standard about fruit extract which pH maximal 4), total dissolved solids is 29.75oBrix (suitable with SNI standard which minimal 10.5oBrix), vitamin C is 5.18%, and antioxidant activity is 91.26%. Comparison result with commercial collagen drink appeared that the best formulation (89.9%) has higher antioxidant activity than commercial product (19.53%). This study aims that rose-apple drink with fish hydrolysate collagen is a non-alcoholic functional drink that is good for health.
... Gelatin, the partial thermal-decomposition of collagen with a relatively stable heatresistant structure, is one of the typical proteins to compose bioactive hybrid materials with PGS. [200][201][202] In 2018, Yoon et al. developed a PGS-gelatin by directly blending pre-PGS with gelatin at 120 C, without any solvent added (Fig. 14A). [163] Covalent bonds establish between PGS and gelatin chains at such high temperatures, eliminating the phase separation and further constructing a staggered PGS-gelatin hybrid network. ...
Article
Full-text available
Poly(glycerol sebacate) (PGS) and its derivatives have been developed and used for various biomedical applications over the past two decades. Several publications have reviewed the development of PGS from different perspectives, typically focusing on the biofabrication techniques and intended biomedical applications of PGS. However, a comprehensive review of the progress in the research on PGS and its derivatives over the past two decades, in terms of material design, synthesis, and properties have not been conducted. Herein, we review the design and preparation of PGS using different synthesis processes, ranging from the traditional heat curing method to various novel synthesis approaches, before systematically exploring the development of novel PGS derivatives prepared by functional groups modification or (and) hybridizing with other substances. Moreover, a statistical analysis of related publications is presented to quantify the progress in the research on PGS and its derivatives from different perspectives and identify any trends. We expect that this review and the design principles of PGS-based materials summarized herein will inform and promote the further development and optimization of PGS and its derivatives for biomedical applications.
... At present, synthetic polymers with low toxicity and natural biomass-derived macromolecules are often adopted as raw materials to prepare conductive hydrogels with good biocompatibility. As a hydrolysis product of natural collagen, gelatin has advantageous characteristics, such as a wide range of sources, good biocompatibility, low price, etc. 16,17 It contains a variety of functional groups including amino, hydroxyl, and carboxyl groups and can be easily modified. For example, Van Den Bulcke and coworkers 18 modified gelatin using methacrylamide to increase the viscoelasticity of the resulting hydrogels, but the preparation method for the gelatinbased hydrogels is cumbersome and time-consuming. ...
... 2 of 11 Collagen is the main structural protein of by-products (e.g., connective tissues, bones, skins, and scales). Collagen peptides, the products of collagen hydrolysis, can be used as antimicrobial and antioxidant ingredients in food [15,16]. The aim of this study was to evaluate the effectiveness of a chitosan coating incorporated with cinnamon bark essential oil and collagen peptides in optimizing the dry-ageing process of beef, compared to the traditional dry-ageing and in-bag dry-ageing. ...
Article
Full-text available
The aim of this study was to evaluate the effects of the chitosan/collagen peptides/cinnamon bark essential oil composite coating on dry-aged beef. Chitosan (2%, w/v), collagen peptides (1%, w/v), and cinnamon bark essential oil (1%, v/v) were homogenized to obtain the coating. Beef samples were divided into three groups (traditional dry-ageing, in-bag dry-ageing, and coating and then dry-ageing) and dry-aged for 42 days. Physiochemical, microbial, and sensorial parameters of samples were determined during the dry-ageing process. There were no significant differences (p > 0.05) in pH values, shear force values, cooking loss, color, juiciness, tenderness, and flavor across groups. The total volatile base nitrogen value of the coating group was lower than those of the other two groups. Compared to traditional dry-ageing, in-bag and coating dry-ageing reduced (p < 0.05) many volatile compounds such as alcohols, aldehydes, ketones, and acetate. In-bag and coating dry-ageing had no impact on the fungal community, but changed the bacterial community by inhibiting Pseudomonas. This study demonstrates that the chitosan/collagen peptides/cinnamon bark essential oil coating reduces microbial spoilage during dry-ageing, and has a small influence on product quality.
... Recent reports of antioxidant protein hydrolysates/peptides obtained from edible parts of meat, waste or by-products, and processed meat products are shown in Table 2. Collagen is the most abundant protein among the various by-products obtained from the meat industry such as bone, cartilage, tendon, skin, and connective tissue, especially found in bovine bone, hides, and tendons [98]. A series of amino acid sequences with antioxidant activity have been identified from various collagen sources and validated in different oxidative systems [99,100]. Recently, Wang et al. [46] investigated the chemical and biological antioxidant effects of GASGPMGPR and GLPGPM, novel peptides derived from yak collagen. ...
Article
Full-text available
The antioxidant activity of protein-derived peptides was one of the first to be revealed among the more than 50 known peptide bioactivities to date. The exploitation value associated with food-derived antioxidant peptides is mainly attributed to their natural properties and effectiveness as food preservatives and in disease prevention, management, and treatment. An increasing number of antioxidant active peptides have been identified from a variety of renewable sources, including terrestrial and aquatic organisms and their processing by-products. This has important implications for alleviating population pressure, avoiding environmental problems, and promoting a sustainable shift in consumption. To identify such opportunities, we conducted a systematic literature review of recent research advances in food-derived antioxidant peptides, with particular reference to their biological effects, mechanisms, digestive stability, and bioaccessibility. In this review, 515 potentially relevant papers were identified from a preliminary search of the academic databases PubMed, Google Scholar, and Scopus. After removing non-thematic articles, articles without full text, and other quality-related factors, 52 review articles and 122 full research papers remained for analysis and reference. The findings highlighted chemical and biological evidence for a wide range of edible species as a source of precursor proteins for antioxidant-active peptides. Food-derived antioxidant peptides reduce the production of reactive oxygen species, besides activating endogenous antioxidant defense systems in cellular and animal models. The intestinal absorption and metabolism of such peptides were elucidated by using cellular models. Protein hydrolysates (peptides) are promising ingredients with enhanced nutritional, functional, and organoleptic properties of foods, not only as a natural alternative to synthetic antioxidants.
Article
This study showed that sodium alginates (SA)-based beads reinforced with collagen hydrolysates (CHs) significantly increased an encapsulation rate of tea polyphenols (TP) from 34.54 % to 85.06 % when the mass ratio of SA: CHs increased from1.5:0 to 1.5:0.5. And after the 30-day storage at 37 °C, the retention rate of TP in beads with CHs at the solutions with pH = 4.0 or pH = 7.0 increased from 61.10 % to 80.21 %, or from 67.72 % to 80.47 % after sterilization at 98 °C or 121 °C for 30 min, respectively. Also, the addition of CHs at 0.5 % resulted in a greater retention of the polyphenolic compositions values of TP determined by UPLC-Orbitrap-MS system. Additionally, the DPPH and ABTS+ free-radical scavenging capacities and ferric-reducing antioxidant power of beads with CHs after sterilization at 98 °C or 121 °C for 30 min were significantly higher than which without CHs. Physical phenomena based on ζ-potential, particle size, fluorescence, UV spectroscopy and confocal laser scanning microscope showed that tightly non-covalent complexes of CHs in combination to TP could be uniformly and stably distributed in the network of SA solution for encapsulating TP in SA-based beads. These findings provided suggestions for the co-encapsulation design and development of hydrophilic nutritive compounds based on CHs in SA-based beads.
Article
Algae have shown numerous advantages as biofunctional and bioactive material sources. The development of biosynthetic or synthetic materials has enabled algal-derived macromolecules and their derivatives to be used in biomedical applications. This review examines and analyzes the most recent developments in the production of biomaterials from algal-derived macromolecules and their composites and their potential applications in bone and cardiovascular tissue engineering. Several macromolecules derived from algal polysaccharides, including sulfated polysaccharides, fucoidans, and fucans, have been developed for cartilage, intervertebral disc, bone, and skeletal muscle transplants because of their stable structures. Alginates, fucoidans, chitin, porphyrin, and other algal polysaccharide derivatives have been investigated for engineering blood vessels, heart valves, and even the liver. One advantage of algal-derived macromolecules and composites is their safe immunity properties. This review also highlights cutting-edge developments in applying algal-derived macromolecules with a broader biomedical scope to encourage in-depth research into their potential as biomaterial scaffolds in medical applications.
Article
Full-text available
O uso de fontes de energia alternativas nas atividades agrícolas pode fomentar diversos benefícios para a agricultura camponesa e suas comunidades rurais. Objetivando o incremento e o fortalecimento de aspectos como a segurança alimentar, a sustentabilidade ambiental, a agregação de valor aos produtos, a economia/geração de recursos para a região, a mobilização social e a promoção da saúde, este projeto busca promover a Tecnologia Social do Desidratador Solar de Alimentos com famílias camponesas dos distritos de Ouro Preto e Mariana - MG. Para o seu desenvolvimento está sendo utilizada a Metodologia Social Camponês a Camponês, tendo a Pesquisa-Ação-Participativa como desenho de estudo e atuação. As atividades consistem na articulação e estruturação pré-campo e nos trabalhos de campo com as famílias das comunidades definidas, sendo estes realizados por meio de Oficinas, Encontros e Rodas de Diálogo. Durante esses encontros, é realizada, também, a aplicação de um questionário de mapeamento de conhecimentos e práticas agroecológicas, que tem como objetivo entender os padrões de distribuição dos saberes tradicionais sobre técnicas agroecológicas, visando estruturar ações posteriores de transição agroecológica, de organização camponesa e de promoção da saúde, tendo os recursos e potenciais locais como fundamentos para a construção de processos geradores de autonomia. Como resultados deste projeto são esperados: a implantação de Desidratadores Solares de Alimentos nos distritos selecionados; a utilização regular da tecnologia de forma apropriada e autônoma pelas famílias envolvidas no projeto; o intercâmbio e aproximação das famílias camponesas dos distritos; e o aprofundamento de processos econômicos e organizativos locais.
Article
Full-text available
Jamun (Syzygium cumini L.) is a fruit rich in anthocyanins, an important group of natural pigments, with color ranging from red to blue, soluble in water, highly antioxidant. Despite its great potential for use as a natural dye, its application is a challenge, due to the instability of these compounds in the environmental conditions of processing and storage commonly used by the food industry. Therefore, this study evaluated the microencapsulation of anthocyanin-rich jamun pulp by ionic gelation (IG) and its protein-coating by electrostatic interaction (PC). The effect of the ratio of sodium alginate solids and jamun pulp (1:0.40 to 1:2, w/w) and the concentration of gelatin coating solution (0% to 10%, w/w) on the morphology, water and total protein content and anthocyanins content in the microparticles were evaluated. Visually, the IG particles showed color tones ranging from reddish to purplish, which became less intense and opaque after being submitted to the gelatin coating process. Microscopic images demonstrated that microparticles formed had an irregular and heterogeneous shape with disorganized gel network formation is due to the presence of solid structures of jamun pulp, observed within the microparticles. The greater the concentration of gelatin in the coating solution, the greater the protein adsorption for the formation of the protective layer, ranging from 21.82 ± 0.72% (T1) to 55.87 ± 4.23% (T6). Protein adsorption on the GI resulted in a decrease in moisture content (ranging from 87.04 ± 0.22 to 97.06 ± 0.12%) and anthocyanins contents (ranging from 5.84 ± 0.62 to 0.78 ± 0.14%) in the PC microparticles.
Article
With the rise of a consumer market increasingly concerned with food and healthy lifestyle habits, the search for functional products has increased in the last years. In this context, dairy products are relevant since they are already included in the consumer's diet. Furthermore, hydrolyzed collagen stands out among products with bioactive action, as it promotes the reduction of the incidence of arthritis, osteoporosis, hypertension, obesity, and premature aging and contains healing, antioxidant and antimicrobial properties. In addition to health benefits, the addition of these ingredients to dairy products can influence physical, chemical, rheological, microbiological, and sensory characteristics, such as: decreased syneresis and improved texture of fermented milks; viscosity increase in dairy beverage; increased proteolytic activity in cheeses; and increasing the viability of probiotics, without significantly altering the quality standards of the legislation. Despite the benefits described, more studies are needed to evaluate these effects in different dairy products.
Article
Although metal-organic frameworks (MOFs) with intriguing physiochemical properties have recently stimulated increasing attention of researchers, MOFs have not adequately achieved various applications due to their instability and unsatisfied processability. Hence,...
Conference Paper
Gelatin’s supply chain encompasses multiple actors before arriving at the end destination. However, costs related to distribution and carbon emissions along the supply chain could be high and motivates the exploration of efficient management solutions. This paper presents a mixed-integer linear programming model for a halal gelatin supply chain and multi-echelon problem. The echelons consist of multiple marine fisheries, multi-aquaculture, fish, and aquaculture processing plants, a halal gelatin plant, and customers. The purpose of this research is to maximize the total profit. The model considers carbon emissions resulting from production and transportation processes. A study case in East Java, Indonesia, is demonstrated to verify the proposed model. The results showed that the total profit and carbon emission produced were IDR S96,395,593,934 and 64,015.34 kg.CO 2 -eq, respectively.
Article
Collagen oligopeptides have wide applications in foods, pharmaceuticals, cosmetics, and others due to their high bioactivities and bioavailability. The S8 family is the second-largest family of serine proteases. Several collagenolytic proteases from this family have been reported to have good potential in the preparation of collagen oligopeptides, however, the underlying mechanism remains unknown. A4095 was the most abundant S8 protease secreted by the protease-producing bacterium Anoxybacillus caldiproteolyticus 1A02591. Here, we characterized A4095 as an S8 collagenolytic protease and illustrated its structural basis to produce collagen oligopeptides. Protease A4095 preferentially hydrolyzed the Y-Gly peptide bonds in denatured bovine bone collagen, leading to high production (62.48% <1000 Da) of collagen oligopeptides. Structural and mutational analyses indicated that A4095 has a unique S1' substrate-binding pocket to preferentially bind Gly, which is the structural determinant for the high production of collagen oligopeptides. This study provides mechanistic insight into the advantage of the S8 collagenolytic proteases in preparing collagen oligopeptides.
Article
Around 10% of the global fish catch (>90 million tonnes) is currently discarded, while by-products in fisheries account for up to 70% of the whole fish weight. From these, fish bones and scales represent 14–20% of by-products, which are also discarded. Therefore, there is an unmet need for valorising these by-products by transforming them into functional and nutritious ingredients. Towards this objective, we report herein different culinary processes to extract gelatine from fish scales, as well as fish flours from bones and scales, as innovative methods for waste valorisation in the food services industry. On the one hand, gelatine was extracted from demineralised and non-demineralised scales and their respective gelling and melting properties were analysed and compared in culinary elaborations. Both gelatines showed a lower melting point (23 °C) than pork gelatine (29 °C, used as control), which provided these gelatines with a smooth and creamy texture in mouth. On the other hand, financiers made of fish bone and fish scales flour were compared with those made with regular wheat-flour, resulting in no significant differences regarding their adhesiveness and springiness. These results showcase the potential of upcycling fish by-products into protein-rich value-added ingredients in the food services industry.
Article
Edible biphasic gels with high lipid fractions (>50%) were developed and characterized for their freeze-thaw and lipid oxidation stability. Gels consisted of gelatin in aqueous buffer (hydrogel; HG), and rice bran wax (RBW) in high-oleic soybean oil (oleogel; OG). Freeze-thaw stability was studied by rheology, liquid loss measurement, and microstructural characterization of the gels before and after one freeze-thaw cycle. Biphasic gels were stored for 6 months under accelerated oxidation conditions to assess oxidative stability through peroxide value (PV) analysis. Biphasic gels led to superior systems compared to control OG and HG. The storage modulus (G′) increased with increasing OG. Yield stress (σ*) for biphasic gels were greater than for OG alone, and σ*increased as the proportion of HG increased. Micrographs of biphasic gels showed OG-in-HG matrix for all gels, including those of >50% OG. After one freeze-thaw cycle, biphasic gels had less total liquid loss by approximately 50% compared to the controls and showed an increase in G′. No samples were rancid after the storage period, as demonstrated by the low PV (<3 meq/kg). Changing the ratio of OG:HG for this biphasic gel demonstrates the potential to design semi-solid fat replacers of desired properties with good overall physico-chemical stability.
Article
Bioactive glass-based organic/inorganic hybrids are a family of materials holding great promise in the biomedical field. Developed from bioactive glasses following recent advances in sol-gel and polymer chemistry, they can overcome many limitations of traditional composites typically used in bone repair and orthopedics. Thanks to their unique molecular structure, hybrids are often characterized by synergistic properties that go beyond a mere combination of their two components; it is possible to synthesize materials with a wide variety of mechanical and biological properties. The polymeric component, in particular, can be tailored to prepare tough, load-bearing materials, or rubber-like elastomers. It can also be a key factor in the determination of a wide range of interesting biological properties. In addition, polymers can also be used within hybrids as carriers for therapeutic ions (although this is normally the role of silica). This review offers a brief look into the history of hybrids, from the discovery of bioactive glasses to the latest developments, with a particular emphasis on polymer design and chemistry. First the benefits and limitations of hybrids will be discussed and compared with those of alternative approaches (for instance, nanocomposites). Then, key advances in the field will be presented focusing on the polymeric component: its chemistry, its physicochemical and biological advantages, its drawbacks, and selected applications. Comprehensive tables summarizing all the polymers used to date to fabricate sol-gel hybrids for biomedical applications are also provided, to offer a handbook of all the available candidates for hybrid synthesis. In addition to the current trends, open challenges and possible avenues of future development are proposed.
Article
Methods have been developed for obtaining polyfunctional preparations of various degree of purification from rhopilema jellyfish in the form of collagen and proteoglycane complexes, and their safety for the external application has been assessed. We used HPLC, SDS-PAGE, and IR spectroscopy for our study. The composition (proteins, including collagen, amino acids, and carbohydrates) and the properties of the obtained preparations were determined. The structure of collagen as a part of the isolated complexes was analyzed and the degree of preservation of its tertiary structure was shown. Changes in the molecular weight distribution of protein fractions were established for different methods of isolation of compounds. The safety of external use of the obtained preparations was analyzed in test animals in terms of acute toxicity, as well as skin irritation and sensitizing effects in accordance with the requirements for the toxicological characteristics of ingredients of cosmetics.
Article
Surimi products have unsatisfactory gel properties. Hence, this study evaluates the effect of collagen-adding on surimi gel properties and provides the first observation results regarding collagen type influence. With higher water solubility and more charged amino acids than type II, collagen type I intertwines with surimi myofibrillar proteins better to induce higher exposure of protein functional domains, more sufficient conformational changes of myosin and greater formation of chemical forces among proteins. These enhancements accelerate the gelation rate, leading to a well-stabilized surimi gel. The collagen I-containing surimi gels show more compact structures with uniformly distributed smaller pores than those containing collagen II, thereby providing the final products with higher water holding capacity and better textural profiles. As such, the surimi gel fortification performance of collagen I and the well-elucidated collagen-myofibrillar protein interaction mechanism will guide the further exploitation of collagen as an effective additive in the food industry.
Article
Carp (Cyprinus carpio) has the potential which is not only consumed from flesh as an edible portion but it is also able to be utilized from waste. One of waste is the scales of the carp known potentially contain of collagens. Micro-collagen has been extensively applied in various fields which were health and cosmetics. The problem to find the supply of collagens from non-halal animal sources and prone to infectious diseases is the fundamental consideration of this research to be undertaken in order to discover alternative sources of them. It was aimed at production and characterization of micro-collagen by utilizing carp scales waste. The stages of the proximate test, deproteinization, extraction, analysis, and characterization were series of processes to acquire collagen. The extraction results found that the yield of collagen extracted from carp scales waste was 8.62% with a yellowish-white color. Physical characterization of collagen obtained was pH of 6.59. The maximum of UV absorption at a wave length of 268nm was originated from the structure of collagen fibrils with amide bonds of A, B, I, II, and III. Furthermore, the characterization of micro-collagen showed a particle size distribution from the smallest particles which was 668 – 1581nm with the highest intensity at a particle size of 1146 nm according to PSA analysis and corresponding with the morphology of micro-collagen through visualization using SEM. It indicates that the carp scales waste have the potential to be used as an alternative source to find supply micro-collagen.
Article
Full-text available
Nowadays, edible and eco-friendly packaging applications have been studied as an alternative to conventional/synthetic packaging due to the great interest of consumers in healthy, safe, and natural food, and of researchers in meeting the needs of consumers and producers. Various biopolymers are being extensively explored as potential materials for food packaging. The edible biopolymers utilized so far for packaging applications include proteins, lipids, and polysaccharides. Occasionally, these biopolymers have incorporated different bioactive substances to enhance the composite films’ characteristics. Gelatin and chitosan are two of the most important biopolymers for the production of films. Different biopolymers or bioactive substances have been incorporated into the matrix to enhance the gelatin-based and chitosan-based films. By incorporating other biopolymers and bioactive compounds, the composite films’ overall physicochemical and mechanical characteristics are improved. Additionally, by incorporating bioactive compounds (polyphenolic compounds, natural extracts, and essential oils), the composite films present important biological properties, such as antioxidant and antimicrobial activities.
Article
Vinyl polymers are widely used in biological, textile and industrial applications and are currently attracting research attention for specialized bio-based applications. Polyvinyl alcohol (PVA) hydrogels show great advantages as a material with high biocompatibility, permeability, hydrophilicity, and low-friction coefficient, allowing applications as smart materials, wound dressings, and flexible sensors. However, the poor mechanical properties of PVA hydrogels and biocompatibility less than natural polymers make them unsuitable in practical applications. Additives are often added to PVA hydrogels to enhance mechanical properties, endow more compatibility, functionality and expand their application range. Among them, bio-additives such as nanocellulose, natural polysaccharides and proteins are biodegradable, biocompatible, and inexpensive , broadening their applications in the biomedical and tissue engineering fields. This work reviews the synthesis of PVA hydrogels, methods to enhance their mechanical properties, types of bio-additives incorporated for biocompatibility, their mechanism of interaction with PVA and future prospects of PVA composite bio-hydrogels for application in various fields. Representative cases are carefully selected and discussed with regard to their composition and pros and cons are discussed. Finally, future requirements, as well as the opportunities and challenges of these bio-additives for improving the multifunctionality of PVA hydrogels are also presented.
Chapter
Full-text available
There are number of food packaging materials such as glass, paper and cardboard, metals and plastic are available. However, the plastic is a mostly used non-biodegradable packaging material which causes environmental pollution. To overcome these problems, the biodegradable/edible food packaging is currently into focus for use. Edible packaging can be used in film as well as coating form. The materials are used for preparation of edible packaging varies in their function according to their sources. Some examples of edible film (packaging) are starch-based, collagen-based, zein-based, gluten-based, etc. Additives are added during the formation of film to enhance their positive role for packed food. Each additive has their unique role when combined with film material. These types of films have various functions, which would help to increase shelf life of food by acting barrier between food and external environment. The main advantage of edible packaging over synthetic packaging is that this may be safely eaten as a part of food product and thus, may reduce packaging waste and pollution. Edible film is physically and nutritionally better that the synthetic food packaging. Edible film used in food packaging should be passed by FDA as GRAS, then it can be used in food packaging. Edible packaging has several applications in dairy, food, confectionary, meat and also in pharmaceutical industry.
Article
Full-text available
Jellyfish gelatin was hydrolyzed by different proteases to obtain antioxidative poly-peptides. The gelatin hydrolysate obtained by progressive hydrolysis using trypsin and Properase E exhibited the highest hydrolysis degree and antioxidant activity. Three series of gelatin polypeptides (SCP1, SCP2 and SCP3) were obtained by ultrafiltrating the gelatin hydrolysate through molecular mass cut-off membranes of 10, 6 and 2 kDa, respectively. Amino acid composition analysis showed that SCP3 had the highest total hydrophobic amino acid content. The in vitro antioxidant tests demonstrated that SCP2 had the stron-gest hydroxyl radical and hydrogen peroxide scavenging activities and metal chelating ability, while SCP3 showed the highest reducing power, antioxidant activity in linoleic acid emulsion system and superoxide anion radical scavenging activity. The results support the feasibility of jellyfish gelatin as a natural antioxidant polypeptide provider, and enzymatic hydrolysis and ultrafiltration could be potent future processing technologies to utilize the abundant jellyfish resource.
Article
Full-text available
To identify the antioxidative peptides in the gelatin hydrolysate of bovine skin, the gelatin was hydrolyzed with serial digestions in the order of Alcalase, pronase E, and collagenase using a three-step recycling membrane reactor. The second enzymatic hydrolysate (hydrolyzed with pronase E) was composed of peptides ranging from 1.5 to 4.5 kDa, and showed the highest antioxidative activity, as determined by the thiobarbituric acid method. Three different peptides were purified from the second hydrolysate using consecutive chromatographic methods. This included gel filtration on a Sephadex G-25 column, ion-exchange chromatography on a SP-Sephadex C-25 column, and high-performance liquid chromatography on an octadecylsilane chloride column. The isolated peptides were composed of 9 or 10 amino acid residues. They are: Gly-Glu-Hyp-Gly-Pro-Hyp-Gly-Ala-Hyp (PI), Gly-ProHyp-Gly-Pro-Hyp-Gly-Pro-Hyp-Gly (PII), and Gly-ProHyp-Gly-Pro-Hyp-Gly-Pro-Hyp (PIII), as characterized by Edman degradation and fast-atom bombardment mass spectrometry. The antioxidative activities of the purified peptides were measured using the thiobarbituric acid method, and the cell viability with a methylthiazol tetrazolium assay The results showed that PII had potent antioxidative activity on peroxidation of linoleic acid. Moreover, the cell viability of cultured liver cells was significantly enhanced by the addition of the peptide. These results suggest that the purified peptide, PII, from the gelatin hydrolysate of bovine skin is a natural antioxidant, which has potent antioxidative activity.
Article
Full-text available
Gelatin hydrolysates with a high inhibitory activity against angiotensin I-converting enzyme (ACE) were fractionated from Alaska pollock surimi refiner discharge. The ACE-inhibitory activity, expressed as (mg/mL), was highest (0.49 mg/mL) in gelatin hydrolysates formed by sequential 2-hr treatments of Pronase and Flavourzyme. After fractionation through four different membrane filters with molecular weight cut-offs of 3, 5, 10, and 30 kDa, the highest ACE-inhibitory activity (0.21 mg/mL) was observed with the 3-kDa filtrate.
Article
Full-text available
A bovine-hide gelatin and a tuna-skin gelatin, both characterized on the basis of their amino acid composition and molecular weight distribution, were used to prepare edible films by casting with glycerol and sorbitol added as plasticizers. The molecular weight distribution of the tuna-skin gelatin exhibited appreciably higher quantities of β-components (covalently linked α-chain dimers), whereas bovine-hide gelatin showed a certain degradation of α1-chains being indicative of a greater proteolysis. Intrinsic differences in the gelatin attributes affected in diverse manner some of the physical properties of the films. Thus, water vapour permeability was higher in the bovine-hide gelatin film, whereas deformability was considerably higher (10 times higher) in the tuna-skin gelatin film. In contrast, breaking force and water solubility were basically unaffected by gelatin origin. Analysis of the thermal properties revealed both films to be wholly amorphous with similar glass transition temperature values thanks to the plasticizing effects of the glycerol and sorbitol and the low moisture contents.
Article
Of all the hydrocolloids in use today surely none has proved as popular with the general public and found favour in as wide a range of food products as gelatine. A sparkling, clear dessert jelly has become the archetypal gel and the clean melt-in-the-mouth texture is the characteristic that has yet to be duplicated by any polysaccharide. Despite its apparently unfashionable status, more gelatine is sold to the food industry than any other gelling agent. It is relatively cheap to produce in quantity, and there is a ready supply of suitable raw material.
Article
Enzymic hydrolysis was applied for the efficient recovery of the protein sources from the fish processing by-product, cod frame. The enzyme used for the hydrolysis was crude proteinase extracted from tuna pyloric caeca. The resultant hydrolysate, cod frame protein hydrolysate (CFPH), was separated based on the molecular weight of the peptides in the hydrolysate and several functional properties were examined, including physicochemical properties (emulsifying and foaming property) and bioactivities (antioxidative and angiotensin I converting enzyme (ACE) inhibitory activity) to determine its potential functions. CFPH was processed through a series of ultrafiltration (UF) membranes with molecular weight cut-off(MWCO) of 30, 10, 5 and 3 kDA, and four types of permeates including 30-K (permeate from 30 kDA), 10-K (permeate from 10 kDA), 5-K (permeate from 5 kDA) and 3-K hydrolysate (permeate from 3 kDA) were obtained. 10- and 30-K hydrolysates showed excellent emulsion properties and whippability. The 10-K hydrolysate showed high antioxidative activity, while the 3-K hydrolysate had excellent ACE inhibitory activity. In terms of all functional properties tested, the fractionated hydrolysates were superior to the original non-separated hydrolysate. These results suggested that separating hydrolysate enhanced several functional properties.
Article
Aim. Microencapsulation of bioactive food ingredients like probiotics is done in order to protect these valuable additives against destructive factors. This work lines out how specific capsule material interactions can influence the protective effect of microcapsules. Methods. Single materials are often not able to meet the requirements. Therefore, combinations of capsule materials are used. Often, when choosing the materials to be combined, only the properties of the single materials are regarded without taking into consideration that specific capsule material interactions can occur. This study presents a systematic examination of the influence of capsule material interactions on their suitability to protect lactic acid bacteria against harmful conditions during processing of the powders, loss of viable cells during storage and residence time in a model food system and finally against the aggressive conditions of the stomach. Results. The processing of capsules loaded with lactic acid bacteria by extrusion and then spray drying of the gained capsules leads to additives with dissimilar properties depending on the materials used for the inclusion. Strong interactions either attractive or repulsive can be identified, which might have caused the different protective effects. Strong interaction either - attractive or repulsive - between the capsule materials enhance the protection compared to formulations based on materials with weak interaction or the single material. Conclusion. This study clearly indicates that the choice of the capsule materials has a pronounced effect on the stability of microencapsulated lactic acid bacteria. Therefore a proper choice of capsule material combinations can lead to customized food additives.
Article
The study was carried out to examine on the refiner discharge from Alaska pollock as a collagen resource by characterizing biochemical and functional properties of collagen. The refiner discharge from Alaska pollock surimi manufacturing was a good resource for collagen extraction according to the results of total protein, heavy metal, volatile basic nitrogen, collagen content, amino acid composition, and thermal denaturation temperature (TDT). TDT of acid soluble collagen from refiner discharge showed 20.7°C, which was similar to that of collagen from Alaska pollock muscle and was higher than that of collagen from Alaska pollock skin. TDT of acid-soluble collagen from refiner discharge was, however, lower than those of skin collagens from warm fish and land animal. Acid-soluble collagen from refiner discharge of Alaska pollock could be used as a functional ingredient for food and industrial applications according to the results of water and oil absorption capacities, and emulsion properties. In addition, if the thermal stability of the acid-soluble collagens is improved, collagen from refiner discharge from Alaska pollock could be more effectively used.
Article
Half-Title page1807-2007 Knowledge for GenerationsTitle pageCopyright pageContentsGelatine - An Element of Our Life
Article
Response surface methodology was used to study the effects of pH, temperature and enzyme - substrate ratio (E/S) on the degree of hydrolysis (DH) of dogfish muscle protein. The effect of the hydrolysis variables was described using a three-level Box-Behnken factorial design giving a mathematical model that shows the influence of each variable and their interactions. Based on degree of hydrolysis (DH) of the original substrate, the hydrolysis variables were optimized at a pH of 8.3, a hydrolysis temperature of 53.6°C and an E/S of 3.6% (w/w). The coefficient of determination (R2ad) was greater than 95%, and a lack-of-fit test revealed a non-significant value for the DH model equation, indicating that the regression equation was adequate for predicting the degree of hydrolysis under any combination of values of the variables.
Conference Paper
To study the potential antioxidant activity and the protective effects of gelatin hydrolysate (GH) against hydrogen peroxide (H(2)O(2))-induced rat pheochromocytoma line PC12 oxidative damage. Gelatin extracted from the body wall of the sea cucumber (Stichopus japonicus) was hydrolyzed with flavourzyme. Fragmented GH was produced using an ultrafiltration membrane bioreactor system. The potential antioxidant activity and the protective effects of GH against hydrogen peroxide (H(2)O(2))-induced rat pheochromocytoma line PC12 oxidative damage were evaluated. Following exposure of cells to H(2)O(2) (200 mu M), a marked decrease in PC12 cell survival and activities of superoxide dismutase (SOD), glutathione peroxidase (GSH-Px) and catalase (CAT), as well as increased levels of reactive oxygen species (ROS), lactate dehydrogenase (LDH) release and maleic dialdehyde (MDA) content. In parallel, H(2)O(2) caused a significant elevation in intracellular caspase-3 activity. However, pretreatment of the PC12 cells with GH prior to H(2)O(2) exposure prevented these H(2)O(2)-induced cellular events noticeably. In conclusion, our result identified that GH possesses good antioxidant activity and exerts neuroprotective effects against H(2)O(2) mediated cell damage in vitro.
Article
Gelatin extracted from tuna skins and giant squid tunics were hydrolysed with Alcalase at 50ºC for 3h. Two peptide fractions (1-10K and ≤1K) were obtained from each gelatin hydrolysate by subjecting them to centrifugal ultrafiltration using successively a 10 kDa and a 1 kDa membrane. The peptide fractions were characterized in terms of amino acid composition and Fourier transform infrared (FTIR) spectroscopy. Antioxidant properties were tested according to the Ferric Reducing Antioxidant Power (FRAP) assay and the radical scavenging capacity (ABTS) assay. A disk diffusion test was performed to test antimicrobial action against a panel of Gram-positive and Gram-negative pathogenic and fish spoilage-associated microorganisms. Although antioxidant and antimicrobial properties could be detected in all tested peptide fractions, the lowermost molecular weight fraction from squid hydrolysate presented the highest reducing and radical scavenging capacities, whereas microbial growth inhibition was found to be specifically related to the type of microorganism.
Article
Several novel peptides with demonstrated antihypertensive activity have been identified in milk fermented with Enterococcus faecalis CECT 5727. Two of the identified peptides, corresponding to β-casein f(133–138) (LHLPLP) and β-casein f(58–76) (LVYPFPGPIPNSLPQNIPP), showed angiotensin converting enzyme-inhibitory (ACEI) activity (IC50) values as low as 5 μm. These peptides demonstrated antihypertensive activity when they were orally administered to spontaneously hypertensive rats. In particular, β-casein f(133–138), yielded a significant antihypertensive effect in these animals. The maximal decreases in systolic blood pressure (21.87±4.51 mmHg, n=8) and diastolic blood pressure (28.5±3.20 mmHg, n=8) were observed 4 and 2 h, respectively, after the administration of 2 mg kg−1 of this peptide. The presence of these antihypertensive peptides in fermented milk prepared with other selected strains of E. faecalis (CECT 5728, 5826 and 5827) was confirmed by HPLC-MS.
Article
The microstructure, phase composition, mechanical properties and shape memory effect of the Ti–16 at.%Nb alloy were investigated by means of TEM, XRD, bending test and tensile test. The XRD results showed that the Ti–16 at.%Nb alloy is mainly composed of two phases: α″ phase and β phase at room temperature. TEM observation proved that there is also a little amount of ω phase in the Ti–16 at.%Nb alloy solid solution treated at 750 °C for 0.5 h. The martensite lath with a sub-structure of (111) type I twin was found in the Ti–16 at.%Nb alloy solid solution treated at 750 °C for 0.5 h by TEM observation. While solid solution treated at 750 °C, the Ti–16 at.%Nb alloy has the best combination of mechanical properties. The Ti–16 at.%Nb alloy has a certain shape memory effect. When the pre-strain is less than 2%, the deformed alloy can completely recover to the original shape. The SME of the Ti–16 at.%Nb alloy has an acceptable reproducibility, because when pre-deformed with 3.26% strain, after more than 20 times deformation cycling, the recovery ratio is still more than 40%.
Article
The present paper describes the formation of hydrogels by reaction of gelatins with periodate oxidized dextrans. The effect of a number of reaction parameters on the rate of gelation is investigated. It is demonstrated that the time to onset of gelation depends on the nature of the gelatin, the nature of the dextran dialdehyde, the type of buffer, the ionic strength and the presence of added salts. The gelation time decreases with increasing concentration of aldehydes, increasing pH and increasing molecular weight of the dextran dialdehyde. In general, the gelation occurs more rapidly with decreasing concentration of indifferent electrolytes, except for the reaction in phosphate buffer where an increase in gelation is observed with increasing buffer strength. Ammonium and calcium salts are found to retard significantly the crosslinking reaction.
Article
We studied the antihypertensive effect of an octapeptide (Gly-Ala-Hyp-Gly-Leu-Hyp-Gly-Pro), which is derived from chicken collagen hydrolysates and has strong angiotensin I-converting enzyme (ACE)-inhibitory activity, on spontaneously hypertensive rats (SHRs). 6 h after a single oral administration of the octapeptide (4.5 mg/kg SHR body weight), the systolic blood pressure was significantly reduced. The octapeptide was not digested by digestive enzymes from the epithelia of the porcine small intestines in vitro. These results suggest that this ACE-inhibitory peptide is absorbed by SHRs in the peptide form and that it lowers blood pressure.
Article
In the present study, gelatin was extracted from sardine scales using a novel pressurized hot water extraction method, and the extraction behavior and properties of of the extracted gelatin were investigated. The present method enabled stable extraction using only water, and no clogging of extraction tube filters was observed. The hydrolysis reaction became more pronounced at an extraction tube outlet temperature of 143-153°C, and virtually all sardine scale collagen was eluted within 8 min at an extraction tube inlet temperature of 225°C (tube outlet temperature, 156-203°C). Extracted proteins consisted mostly of gelatin, but also a small percentage of ash thought to be apatite. In addition, no significant amino acid thermal decomposition was observed. Molecular weights of extracted gelatin ranged from approximately 443 to 6.5 kDa at the peaks of the GPC curve, and decreased as extraction temperature increased. Gelatins in the peptide region that had narrow molecular weight distributions were obtained in the 400-1000 mL fraction at an inlet temperature of 225°C.
Article
The extracts from cartilage and skin of chum salmon were prepared using a pressure cooker. As a result, protein and collagen contents in extracts from cartilage and skin was higher than those only in cartilage. The inhibition activity of linoleic acid oxidation was high in extract from cartilage. The scavenging activity of cartilage extract was higher than those of cartilage and skin against all reactive oxygen species, such as superoxide anion, hydroxyl, and DPPH radicals. On the other hand, angiotensin I-converting enzyme inhibitory activity of cartilage extract was about seven times as high as that of cartilage and skin extract. The present studies indicate that the extracts, particularly from cartilage, have angiotensin I-converting enzyme inhibitory activity that functions to depress hypertension, and antioxidant activity, which acts to prevent of life-style related diseases such as cancer, cardiovascular diseases, and diabetes. The data should be useful for developing a novel type of functional seasoning.
Article
Proteolytic activity of pyloric caeca extract (PCE) from bigeye snapper (Priacanthus macracanthus) was studied. The highest activity was observed at 55°C and pH 8.0 when casein, Nα-Benzoyl-dl-arginine-p-nitroanilide (BAPNA) and Nα-p-Tosyl-l-arginine methyl ester hydrochloride (TAME) were used as the substrates. The activity was inhibited markedly by 1mg/ml soybean trypsin inhibitor, whereas E-64, pepstatin A and EDTA exhibited a negligible effect on activity. The results suggested that a trypsin-like enzyme was most likely the major proteinase in PCE. As determined by activity staining, two proteolytic activity bands with apparent molecular weights of 55 and 24kDa were found. Gelatin hydrolysate from bigeye snapper skin prepared using PCE exhibited the increases in 2,2-Diphenyl-1-picrylhydrazyl (DPPH), 2,2-Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging activities and ferric reducing antioxidative power (FRAP) as degrees of hydrolysis (DHs) increased (P
Article
Gelatin was extracted from the skin of farmed giant catfish (Pangasianodon gigas) with a yield of 20.1g/100g skin sample on the basis of wet weight. The chemical composition and properties of gelatin were characterised. The gelatin had high protein (89.1g/100g) but low fat (0.75g/100g) content and contained a high number of imino acids (proline and hydroxyproline) (211 residues per 1000 residues). Giant catfish skin gelatin had a slightly different amino acid composition than calf skin gelatin. The bloom strength of the gelatin gel from giant catfish skin gelatin (153g) was greater than that of calf skin gelatin (135g) (P
Article
An edible film plasticized with glycerol and sorbitol was successfully prepared from a sole skin gelatin. Some physico-chemical properties of the films (water vapour permeability, water solubility, opacity) were similar to those from a commercially acquired catfish skin gelatin, whereas the breaking force was significantly lower (11.4±2.1 vs. 28.1±3.1 N) and the breaking deformation significantly higher (18.1±1.0 vs. 14.5±2.1%). A borage extract was prepared and its antioxidant properties (total phenolics, reducing ability by the FRAP assay, radical scavenging capacity by the ABTS assay, iron (II) chelation activity) were determined. The incorporation of the borage extract into the films gave rise to a pronounced increase of their antioxidant properties irrespective of the gelatin origin, with minor modifications of their physico-chemical properties: decrease of the breaking force and increase of film opacity. The antioxidant properties of films incorporated with borage extract were higher than those of films incorporated with α-tocopherol and BHT.
Article
Type II collagen was purified from sternal cartilage of the chick using a combination of pepsin digestion, NaCl precipitation and DEAE-sepharose CL 6B ion exchange chromatography. Pepsin-solubilized type II collagen of higher stability can be obtained with the extraction time of 32h, 0.5% pepsin concentration at 20°C. The purified preparation showed a single peak on RP-HPLC and a single band (α-chain) and its dimers (β-chains) on SDS-PAGE with a subunit Mr of 110kDa. The amino acid composition of the type II collagen derived from chick cartilage was closer to that of reference Sigma-Aldrich type II collagen which contains more imino acid. Analysis by differential scanning calorimetry (DSC) and Fourier transform infrared spectroscopy (FTIR) revealed that type II collagen from chick sternal cartilage retains more intermolecular crosslinks during the purification process. Collagen purified from chick sternal cartilage was typical type II collagen and may find applications in functional foods. Copyright © 2007 Elsevier Ltd. All rights reserved.
Article
To make more effective use of underutilised resources, collagens from skin, scale and bone (SKC, SCC and BOC) of deep-sea redfish were isolated with acetic acid and characterised for their potential in commercial applications. The abundant ash and fat in the materials could be removed effectively by EDTA and hexane treatment in 24h, with high recoveries of protein. The yield of SKC (47.5%) was significantly higher than that of SCC and BOC (6.8% and 10.3%, respectively). The denaturation temperatures of SKC, SCC and BOC were 16.1°C, 17.7°C and 17.5°C, respectively, which were lower than those of most other fish species. The amino acid profiles of these collagens were similar with a low imino acid content, which might be the reason for the low denaturation temperature. All the collagens were type I mainly and maintained their triple helical structures well with slight molecular structure differences. SKC possessed a higher degree of intermolecular cross-linking and molecular order, but the extent of peptide chain unwinding was also higher, due to the existence of fewer hydrogen bonds, compared to SCC and BOC. Copyright © 2007 Elsevier Ltd. All rights reserved.
Article
The aim of the investigations was to optimize the procedure of gelatin extraction from the skins of Baltic cod (Gadus morhua) and to modify the properties of fish gelatin, using transglutaminase, to form gels at room temperature. A temperature of 45 °C and 30 min of extraction was established as optimal conditions for preparing gelatin from cod skins. Fish gelatin in 5% solutions formed gels at room temperature in the presence of transglutaminase (0.15–0.7 mg of enzyme protein/ml), depending on the reaction time. Transglutaminase was also active in crosslinking of fish gelatin at 4–5 °C. The deformation of gels obtained from 5% gelatin solutions after a 24-h incubation with transglutaminase, at concentration 0.25 mg/ml, measured at 6–8 °C, was the same as or slightly lower than in control samples (without enzyme). Fish gelatin gels, enzymatically crosslinked, did not melt after 30 min of heating in a boiling water bath.
Article
The relationship between collagen concentration and emulsifying capacity as well as the effect of pH and sodium chloride concentration on the development of this functional property were studied. Due to what is known as the dilution effect, emulsifying capacity, when expressed in terms of the quantity of soluble protein, decreased as collagen concentration increased. When expressed in terms of total protein, emulsifying capacity decreased as the NaCl concentration increased and was highest at pH levels of between 1 and 3. A power function that described the behaviour of this functional property in terms of soluble protein independently of the factors considered, i.e., concentration, pH, and percentage sodium chloride, was found. Generally speaking, emulsifying capacity, expressed in terms of the quantity of soluble protein, can be regarded as higher in the collagenous material from the hake than in that from the trout, and higher in the muscle connective tissue than in the dermal connective tissue.
Article
Food aeration has become one of the fastest growing unit operations practiced in the food industry. Dispersed air (or other gases) provides an additional phase within the gel that may accommodate new textural and functional demands. This paper addresses the relationships between structural characteristics and fracture properties of gas-filled gelatin gels (GGG), and compare these properties with those of control gelatin gels (CGG). Three gases were used in the fabrication of GGG: air, nitrogen and helium. Experimental methods to determine density, gas hold-up, bubble sizes and bubble size distributions as well as fracture properties of GGG are presented. Increasing protein concentration produced higher density, lower gas hold-up and decreased polydispersity of bubbles due to its effect on increased solution viscosity. Type of gas affected density and gas hold-up due to the different diffusivities of gases and structures (bubble size, size distribution and number of bubbles per area) formed in GGG. Fracture values increased for both GGG and CGG with increasing protein concentration for the three gases used. GGG were weaker and less ductile than CGG, the decrease in stress and strain at fracture being between 70 and 80%, and 40 and 65%, respectively. A power law relationship (σf=2.73×10−12ρG4.76) was found between the fracture stress and gel density for the three gases studied. This study shows that the presence of bubbles in gel-based food products results in unique textural properties conferred by the additional gaseous phase.
Article
The objective of this study was to illustrate the correlation between the physical properties and nanostructure of gelatins made of channel catfish (Ictalurus punctatus) skins. The gelatin samples were first pretreated with sodium hydroxide, acetic acid, or water, and then extracted with hot water before the measurement. Physical properties including the yield of protein, viscosity and textural properties were determined on gelatins obtained with different pretreatment conditions. The acid pretreatment group showed the highest gel strength and protein yield, and a reasonable viscosity. The water pretreatment group showed the lowest values for all of the physical properties. Four samples including water, 0.1M acid and 0.25 and 1.0M alkaline-pretreated groups’ nanostructures were then studied using atomic force microscopy (AFM). The AFM images showed that the acid-pretreated gelatin was composed of sponge-like aggregates, while the others showed separated individual aggregates. Annular pores were only found in the alkaline pretreatment group. There was no significant correlation between the diameters of the spherical aggregates and the physical properties; however, the different AFM patterns may relate to the gelatin's physical properties.
Article
This study assessed the effectiveness of using hydroxylpropylmethylcellulose (HPMC) to enhance mechanical strength and thermal stability in fish skin gelatin (FG). The significant increase in absorbance (A400) observed after HPMC had been added to FG and then matured indicated successful formation of a composite gel. Increased gel strength and storage modulus (G′) indicated the enhanced gelation ability of the matured composite gel, while increased melting temperature (Tm) and enthalpy (ΔH) indicated its improved thermal stability. Maturation-related rheological property improvements were more noticeable at 4 °C than 10 °C, but no apparent differences in Tm improvement were observed between 4 °C and 10 °C maturation. Nevertheless, the composite gel exhibited reversible cold and thermal gelation properties.
Article
The influence of transglutaminase crosslinking on the rheology of gelatin gels has been investigated. We find that the gel strength may be either reduced or enhanced depending on whether covalent crosslinking occurs predominantly before or after development of triple helix junction zones. A striking result is that, following extensive covalent crosslinking during cold-set gelation and afterwards in the melted state, the gelatin gel's characteristic thermoreversible character is almost completely lost.
Article
Tests were conducted to evaluate the inhibitory effects of collagen peptides in the hydrolysate of sea bream scales on the activity of angiotensin I converting enzyme (ACE, EC3.4.15.1). The scales were hydrolyzed using an alkaline protease treatment by which 92% of the peptides were degraded to form hydrolysate. The 50% inhibitory concentration of the peptides was as high as 0.57 mg ml−1. In addition, using spontaneously hypertensive rats, oral administration of 300 mg of the peptides (kg of body weight)−1 d−1 was shown to decrease blood pressure significantly (P