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A simple and eco-friendly method of gelatin production from bone: One-step biocatalysis
Abstract
Conventional gelatin production based on liming is time-consuming and leads to significant land pollution and wastewater. Thus, an efficient and ecologically compatible method of gelatin production from bone has to be developed. In this study, a novel one-step enzymatic method was proposed, and the new method showed excellent results, with time reduction for ossein hydrolysis from 3–8 weeks to 3 h and without the need for liming and deliming, thereby reducing alkali usage substantially and saving nearly 60% water. In addition, 4 steps with low yield involved in conventional gelatin extraction were replaced by 1 step with relatively high yield in the new method. The gelatin obtained from the one-step enzymatic method possesses similar physicochemical properties except for the isoelectric point. Moreover, environmental assessment and financial analysis demonstrated the environmental benefit and economically feasible of the enzymatic method, suggesting the potential of one-step biocatalysis as alternative route to sustainable development for bone gelatin industry.
... By eliminating the lime treatment and demineralization steps found in traditional methods, this approach reduces environmental pollution. As a result, a high-quality gelatin product with improved physicochemical properties was obtained compared to the gelatin extracted by traditional methods [14]. Zaitsev et al. have demonstrated that the molecular weight distribution (MWD) of gelatin significantly influences its properties [15]. ...
... Additionally, the G ′ modulus of E gelatin remains higher than that of A and B samples across all temperature ranges, demonstrating superior gel-forming capability and structural stability. Ma et al. and Sarbon et al. reported that the intrinsic differences in the gelatin structure and the processing methods used in gelatin production can lead to variations in gelling ability [14,36]. Abedinia et al. also reported that the source of gelatin, breed and age of the animal, molecular weight, peptide chain cleaving position, and the concentration of amino acid residue in gelatin are the key contributors to the rheological properties of gelatin [36]. ...
... All three extraction methods displayed distinct bands at around 140 kDa, corresponding to the α1 and α2 chains, characteristic of collagen proteins. This result is consistent with previous studies on gelatin [14,[41][42][43]. However, the intensity and clarity of these bands varied, reflecting the degree of preservation or degradation of the collagen structure during extraction. ...
Yanbian cattle, a high-quality indigenous breed in China, were selected due to their unique biological characteristics, underutilized bone byproducts, and potential as a halal-compliant gelatin source, addressing the growing demand for alternatives to conventional mammalian gelatin in Muslim-majority regions. This study investigates the physicochemical and functional properties of gelatin extracted from Yanbian cattle bones using three different methods: acid, alkaline, and papain enzymatic hydrolysis. The extraction yields and quality of gelatin were evaluated based on hydroxyproline content, gel strength, viscosity, amino acid composition, molecular weight distribution, and structural integrity. Specifically, A gelatin, prepared using 0.075 mol/L hydrochloric acid, achieved the highest yield (18.64%) among the acid-extraction methods. B gelatin, extracted with 0.1 mol/L sodium hydroxide, achieved the highest yield (21.06%) among the alkaline-extraction methods. E gelatin, obtained through papain hydrolysis, exhibited the highest yield (25.25%) among the enzymatic methods. Gelatin extracted via papain enzymatic hydrolysis not only retained better protein structure but also exhibited higher hydroxyproline content (19.13 g/100 g), gel strength (259 g), viscosity (521.67 cP), and superior thermal stability. Structural analyses conducted using SDS-PAGE, GPC, FTIR, XRD, and CD spectroscopy confirmed that papain extraction more effectively preserved the natural structure of collagen. Furthermore, amino acid composition analysis revealed that gelatin extracted via papain hydrolysis contained higher levels of essential residues, such as glycine, proline, and hydroxyproline, emphasizing the mild and efficient nature of enzymatic treatment. These findings suggest that, compared with acid and alkaline extraction methods, enzymatic hydrolysis has potential advantages in gelatin production. Yanbian cattle bone gelatin shows promise as an alternative source for halal gelatin production. This study also provides insights into optimizing gelatin production to enhance its functionality and sustainability.
... They can cleave the telopeptide region of collagen, which is crucial in disrupting the intramolecular and intermolecular covalent cross-linking of native collagen. Currently, despite the lack of widespread market application, gelatin prepared by enzyme-aided degradation of collagen has high gel strength and viscosity [14], which can meet the requirements of Chinese pharmacopoeia and European pharmacopoeia, and is bound to become the main product classification in the future gelatin market. Furthermore, with the aid of enzyme, a complete gelatin extraction process can be shortened to just 3 days from about 40-60 days for the conventional alkaline extraction. ...
... The structures of the gelatin samples were analyzed using a circular dichroism spectrometer J-810 (Jasco Corporation, Tokyo, Japan). Spectra of solutions of the gelatin samples (0.5 mg·mL −1 ) were obtained in the far-UV region from 190 to 260 nm at room temperature [14]. ...
... Circular dichroism spectroscopy was used to evaluate the secondary and tertiary structures of the gelatin chains. As shown in Figure 4a, typical random coil dominated spectra were observed for all four samples, which may be attributable to the low concentration [14]. The band in the region of 220 nm was ascribed to the triple-helix structure [29], and it was readily apparent that this structure was more prominent in the enzymatic gelatin samples than in the alkaline gelatin sample. ...
To shorten the long process of conventional alkaline extraction of gelatin, an enzyme-aided method was demonstrated, which was simpler, more effective, and environmental friendly. The main properties of enzymatic gelatin and conventional alkaline gelatin were comprehensively analyzed, including rheological properties, foaming properties, emulsifying properties, water absorption capacity, and thermal stability. It was found that enzymatic gelatin exhibits neutral isoelectric points of 7.4–7.8, higher imino acid content (21.85%, on average), and excellent emulsifying properties, thermal stability, and foaming properties (181%, on average), but lower water absorption properties (5.8 g‧g ⁻¹ , on average). These findings would be beneficial for the future applications of enzymatic gelatin.
... Gelatin was extracted from leather solid waste for potential application in chemical sand-xation [10]. Bone can be used as a source to produce gelatin through the biocatalysis process [11]. Collagen is a special type of extracted protein from raw trimming waste of tannery for many applications like tissue engineering and the pharmaceutical industry [12]. ...
... The gel strength of extracted gelatin from sh or chicken gives 181 and 263, respectively [24]. In addition, horse mackerel gelatin shows bloom strength 280 [25] and 177 g [11]. The low value of sh gelatin may be due to hydroxyproline content being relatively low in sh skin [26]. ...
... The hydroxyproline and proline can form hydrogen bonding with free water and triple-helix of gelatin structure [15]. Also, the bloom strength of gelatin is affected by many factors like chemical handling of gelatin, type, form, concentration, and source of gelatin, besides the thermal history of the extracted gelatin [11]. ...
Extracted gelatin from the waste of fresh and grilled chicken skin was used to prepare films as a biodegradable packaging material from solutions of various gelatin concentrations using a casting approach. The thermal behavior of extracted gelatins was investigated by differential scanning calorimetric. The particle size and zeta potential of dispersed nanoparticles of gelatins were measured by dynamic light scattering. The surface area of lyophilized gelatin nanoparticles was calculated from the adsorption of N 2 gas. Mechanical properties, water vapor permeability (WVP), and oil uptake (OU) of all manufactured films were studied. Tensile strength values significantly increased for films manufactured from both gelatin sources when the concentration increased from 4 % to 6 % up to 5.1 MPa. The elongation of waste skin gelatin-based films was higher than waste grilled skin gelatin (WG)-based films using 4 % and 8 % concentrations up to 57 %. Films manufactured from WG had significantly lower WVP than waste skin gelatin (WS) analogous at a 4 % gelatin concentration. The WVP of films manufactured from gelatin significantly increased as gelatin concentration increased where OU showed higher oil resistance for films manufactured from WS up to 91 % using 4 % gelatin concentration. The morphological structure of the gelatin film was investigated with scanning electron microscopy (SEM). A homogenized and smooth film surface was observed. The percentage of heavy metal was examined by inductively coupled plasma (ICP). The results of this study showed that the films manufactured using higher concentrations of gelatin possessed promising mechanical properties, good barrier properties, and high safety as a recommended biopolymer packaging material for food contact and pharmaceutical applications.
... Available at www.veterinaryworld.org/Vol.14/September-2021/15.pdf According to Ma et al. [17], the traditional bone gelatin extraction method takes 20-60 days. In contrast, a bone also has a high ash content so that, if it is not pretreated with appropriate methods, it would significantly affect most physical, chemical, and functional characteristics of gelatin. ...
... Natural or commercial protease enzymes derived from plants, animals, and microorganisms have been shown to break down the collagen cross-linking by various extraction methods and gelatin production with various characteristics that are directly responsible for the physical, chemical, and functional properties of gelatin [20]. Enzymes with certain conditions can be used as a pretreatment of raw materials before extraction [17,21,22], or enzymes are dissolved and then used for extraction of raw materials [23][24][25]. Alcalase and neutrase are commercial enzymes and widely used in hydrolysis or protein modification. ...
... This is assumed because proteolytic enzymes have catalytic specificity and are able to degrade collagen in bone and separate other proteins and inorganic compounds. Ma et al. [17] used pepsin to demineralize pork bones and showed high yield, which is associated with perfect pretreatment. The ash content of the Aceh cattle scapular bone gelatin reported by Jelita et al. [14] with decalcification for 8 days and extracted from the acid was 4.67%. ...
Background and Aim: Gelatin is a dissolved protein that results from partial extraction of collagen, commonly from pig and bovine skin. There was no study on gelatin production from Kacang goat bones through enzymatic extraction. This study aimed to evaluate the chemical, physical, and functional properties of gelatin from bones of Kacang goat using alcalase and neutrase enzymes.
Materials and Methods: Male Kacang goat bones aged 6-12 months and two commercial enzymes (alcalase and neutrase) were used for this study. Descriptive analysis and completely randomized design (one-way analysis of variance) were used to analyze the chemical, physical, and functional properties of gelatin. Kacang goat bone was extracted with four concentrations of alcalase and neutrase enzymes, namely, 0 U/g (AG-0 and NG-0), 0.02 U/g (AG-1 and NG-1), 0.04 U/g (AG-2 and NG-2), and 0.06 U/g (AG-3 and NG-3) with five replications.
Results: The highest yield of gelatin extraction with alcalase obtained on AG-3 was 9.78%, and that with neutrase on NG-3 was 6.35%. The moisture content of alcalase gelatin was 9.39-9.94%, and that of neutrase gelatin was 9.15-9.24%. The ash and fat content of gelatin with alcalase was lower than that without enzyme treatment with higher protein content. The lowest fat content was noted in AG-1 (0.50%), with protein that was not different for all enzyme concentrations (69.65-70.21%). Gelatin with neutrase had lower ash content than that without neutrase (1.61-1.90%), with the highest protein content in NG-3 (70.89%). The pH of gelatin with alcalase and neutrase was 6.19-6.92 lower than that without enzymes. Melting points, gel strength, and water holding capacity (WHC) of gelatin with the highest alcalase levels on AG-1 and AG-2 ranged from 28.33 to 28.47°C, 67.41 to 68.14 g bloom, and 324.00 to 334.67%, respectively, with viscosity that did not differ, while the highest foam expansion (FE) and foam stability (FS) were noted in AG-1, which were 71.67% and 52.67%, respectively. The highest oil holding capacity (OHC) was found in AG-2 (283%). FS and OHC of gelatins with the highest neutrase levels in NG-2 were 30.00% and 265.33%, respectively, while gel strength, viscosity, FE, and WHC of gelatins with the highest neutrase levels did not differ with those without enzymes at all enzyme concentrations. B chain was degraded in all gelatins, and high-intensity a-chains in gelatin with alcalase and peptide fraction were formed in gelatin with neutrase. Extraction with enzymes showed loss of the triple helix as demonstrated by Fourier transform infrared spectroscopy.
Conclusion: Based on the obtained results, the Kacang goat bone was the potential raw source for gelatin production. Enzymatic extraction can increase the quality of gelatin, especially the alcalase (0.02-0.04 U/g bone) method. This can be used to achieve the preferable quality of gelatin with a higher yield.
... The degree of conversion of collagen to gelatin is associated with the intensity of both pre-treatment and boiling processes, commonly predicated on pH, temperature and time of extraction [48]. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.) ...
... (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.) [27,45,48]. As per gram cubes, the processed raw materials for gelatin from high fibril-forming collagen (generally from mammalian skins, connective tissue and cartilages) recovered stable pyrrolidine imino acids composition and high molecular weight polypeptides [49,50]. ...
... Thereby, Fig. 1(b) shows the current efficient one-step biocatalysts extraction process for commercial considerations. Ma et al. [48] proposed a one-step biocatalysis method for the production of gelatin from bone-based materials and concluded that the method' life-cycle assessment (LCA) for commercial and environmental impacts is effective and eco-friendly, with cost-effective benefits (BCR) 1.10 indicating that it is financially viable and economically feasible compared to the conventional method. As depicted in Fig. 1(b), the biocatalysis hydrolyses native collagen into gelatin through proteolytic enzymes (usually pepsin or bromelain) in a short time of treatment (at least 3 days of demineralisation) with higher yields (>10% than conventional) and less waste generation compared to conventional method [29,48]. ...
This review begins with a discussion of the general properties of gelatin and its sources, particularly in the food and health industries, and then briefly address the status quo of gelatin in today's market. Apart from the basic chemical compounds and gelatin types, this paper also discussed the commercialisation of gelatin. This study also highlights the production of conventional gelatin and its current method of processing, i.e. enzymatic hydrolysis. In addition, the variety of raw materials of collagen is outlined and briefly broached the plant hydrocolloids which have been labeled as 'veggie-gelatin'. With regard to the potential and market stability of gelatin, its recent studies are summarised in this paper. Accordingly, this paper focuses on assessing the general utilities of the various sources of collagen as gelatin derivatives. At that basis, the aim of this review is to provide an insight into gelatin in current applications , market value and progress in gelatin extraction.
... To the best of our knowledge, little information regarding the main influence factors in modification has been reported, and producing water-insoluble gelatin film with MTGase modification was still an area not elucidated. In a previous study, we have developed a one-step biocatalysis method to extract type E gelatin and found that the three existing gelatin production methods (the acid process, the liming process, and the enzymatic process) [17][18][19] could produce gelatin with different water solubility under MTGase modification. Furthermore, an innovative water-insoluble gelatin film can be produced while using type E gelatin. ...
... The preparation of type E gelatin was according to our previous method [19]. Briefly, the defatted bone was ground to 30 mesh and then immersed in 1 mol/L hydrochloric acid containing pepsin at 40 U/g bone powder with a solid: solvent ratio of 1:9 (w/v). ...
... Significant differences between means were calculated by ANOVA in SPSS ver. 19.0 (SPSS, Inc., Chicago, IL, USA). P < 0.05 was considered to be statistically significant. ...
Gelatin is a promising candidate for making bioplastic film; however, the water soluble property has limited its applications. Here, we have successfully fabricated a water-insoluble gelatin film with the assistance of biocatalysis. This innovative gelatin film could retain its original shape at ambient temperature (30 °C) or even in boiling water. Type E gelatin could form more covalent crosslinks when compared to that of conventional ones with the same amount of microbial transglutaminase (MTGase), and it exhibits obvious changes in terms of molecular weight, network structure, and mechanical strength. This work could provide a strategy for fabricating water-insoluble gelatin film and open routes for the development of bioplastic film using gelatin.
... After pretreatment with hydrochloric acid, the extraction yield of bovine bone gelatin was 4.76%. Ma et al. (2019) reported that the extraction first step yield of pork bone gelatin using traditional pretreatment method (hydrochloric acid) was only about 3%. Bovine bone collagen pretreated by acetic acid had the lowest gelatin yield (4.26%), while the yield obtained by citric acid pretreatment was 6%. ...
... The amide-III band of gelatin samples concentrated around 1246 cm −1 (Fig. 5A) is in agreement with Nguyen et al. (2012). According to Frushour and Koenig (1975) and Ma et al. (2019), amide-III is assigned to the triple-helix of collagen. A lower amplitude amide-III band indicates that the triple helix structure is lost due to the denaturation of collagen to gelatin (Sinthusamran et al., 2014). ...
... Gel strength depended on the molecular weight and molecular weight distribution of gelatin (Balti et al., 2011). At the same time, the complex interactions determined by the proportion of ␣/-chains in gelatin also play an important role in the formation of the gel network (Ma et al., 2019). As shown in Fig. 3, all gelatin samples had similar ratios of ␣/-chains indicating that the native structure of type I collagen was maintained. ...
Effects of different acids and pepsin on the properties of gelatins extracted from bovine bone collagen were investigated. Pretreatment of bovine bone by different acids (hydrochloric acid, acetic acid, and citric acid) with and without pepsin was performed at 70 °C for 7 h to extract gelatin. Under the different acid treatments, the yield of gelatin was significantly different (hydrochloric acid, 4.76%; acetic acid, 4.26%; citric acid, 6.00%). Compared to no pepsin incubation group, bovine bone collagen treated with pepsin presented a higher yield (P < 0.05). Scanning electron microscopy analysis showed that citric acid disrupted more of the collagen structure compared with acetic acid and hydrochloric acid. Raman spectra revealed that all extracted gelatins had the similar secondary structure. Rheological analysis indicated that gelatin extracted with citric acid exhibited the highest maximum elastic modulus, gelling and melting temperature. Overall, the gelatin yield was affected by the type of pretreatment acid and more optimal gelatin extraction and gel properties were obtained when citric acid was used for extraction. Collagen pretreated with acid and pepsin was more efficiently extracted for gelatin compared to treatment without pepsin.
... The third step involves a filtration procedure used to eliminate insoluble contaminants that might lower the quality of the gelatin (Mad-Ali et al., 2016). This traditional method requires a significant amount of water, energy, and time and results in the generation of substantial waste that can be potentially harmful to the environment (Ma et al., 2019;Zhang et al., 2020). New technologies and innovations have been developed to make gelatin production more environmentally friendly and sustainable. ...
... On the other hand, in the extraction of pangasius fish oil, protein components were usually removed to obtain high-purity fish oil (Minh et al., 2015;Sari et al., 2016;Santya et al., 2019). On top of that, these processes require large amounts of water and chemical solvents which generate waste for the environment (Ma et al., 2019). ...
This study explores the potential of hydrothermal extraction as an innovative valorisation method for the simultaneous production of gelatin and fish oil from fish byproducts. It offers an environmentally friendly alternative to conventional solvent‐based techniques by minimising the use of chemical solvents and water. We researched various major commercial freshwater fish species: striped catfish, catfish, and tilapia, and achieved a gelatin product that reflects commercial standards in chemical structure, gel strength, and pH level. The striped catfish gelatin showed the highest gel strength and viscosity (66.01 ± 0.83 g bloom and 15.3 ± 0.1 cP), but was produced at a lower yield than the catfish gelatin. On the other hand, striped catfish produced the highest yield of fish oil (13.56 ± 0.21%) and has the highest omega 3 content (3.72 ± 0.02%) than other fish oil. This innovative study demonstrates the potential of hydrothermal extraction as a sustainable method for producing gelatin and fish oil, offering eco‐friendly and nutritional benefits across a range of applications.
... The spectra were investigated in the bone matrix by an adapted method from Ma et al. (2019). The x-ray diffraction (XRD) (Bruker-AXS D8, Billerica, MA, USA) was used with CuKα radiation at 40 kV and 25 mA. ...
... The crude bone matrix showed 25.5% of nitrogen content and 64.7% of ash content (Table 1). Ossein represents the protein predominance (COL I) or organic fraction of bovine bone (Ferreira et al., 2012) and may present 25-30% in the bone matrix, as shown by the nitrogen content (Ferraro et al., 2017;Ma et al., 2019). Hydroxyapatite represents the minerals or inorganic fraction of bovine bone and may have 65%, as shown by the ash content (Dunning, 2002;Pacca et al., 2014). ...
Bovine bone is an animal‐origin matrix rich in type I collagen (COL I) and it necessitates prior demineralization and makes COL I available. This study investigated the ossein–hydroxyapatite physicochemical properties evaluation as a result of processing and solubilization by acids and revealed the bone matrix demineralization and making COL I available. The tibia residue from bovine sources was processed, ground, and transformed into bone matrix powder. The bone matrix was solubilized in acetic acid followed by lactic acid. The bone matrix was evaluated as a result of processing and solubilization by acids: ossein and hydroxyapatite percentages by nitrogen and ash content, mineral content, particle size distribution, Fourier‐transformation infrared spectroscopy, x‐ray diffraction, and scanning electron microscope. For the obtained residual extracts, pH and mineral content were evaluated. The solubilization by acids affected the ossein–hydroxyapatite physicochemical properties, and the bone matrix solubilized by acetic and lactic acid showed the preservation of the ossein alongside the loss of hydroxyapatite. The processing and the solubilization by acids were revealed to be a alternative to bone matrix demineralization and enabling the accessibility of bone COL I.
Practical Application
Bovine bone is an abundant type I collagen source, but processing maneuvers and demineralization effect present limitations due to the rigidity of the structural components. Exploring methodologies to process and demineralize will allow type I collagen to be obtained from the bone source, and direct and amplify the potentialities in the chemical and food industries. The research focused on bone sources and collagen availability holds paramount significance, and promotes repurposing agribusiness residues and development of protein–base products.
... Based on this, we developed a one-step biocatalytic type-E bone gelatin without the long-term liming process. The process conditions were relatively mild and environmentally friendly [19]. The amount of glutamate produced by glutamine deamination is lower than that of alkaline bone gelatin, so it has more potential to interact with MTGase. ...
... The extraction of type-E bone gelatin referred to our previous method: One-step biocatalysis [19]. Before extraction, defatted bone particles were crushed and passed through a 30-mesh sample sieve. ...
A novel gelatin prepared by enzymatic catalysis (type-E bone gelatin) was developed in our group. In this study, the high crosslinking activity of type-E bone gelatin with microbial transglutaminase (MTGase) was found and further used for the gelatinization properties of minced pork. The results showed that the contents of lysine and glutamine in type-E bone gelatin were higher than that of traditional gelatin prepared by acid (type-A gelatin) and alkali (type-B gelatin) methods, which are as action sites for MTGase. The crosslinking degree (79%) of type-E was approximately 4.9 times that of type-A and 5.6 times that of type-B at 1.44 U/g MTGase. Moreover, the type-E gel showed thermal irreversibility when the MTGase concentration was higher than 0.90 U/g due to high crosslinking activity. For minced pork gel, the water-holding capacity and texture properties of minced pork modified with type-E bone gelatin crosslinked by MTGase were improved and cooking loss was significantly reduced.
... Ma et. al., [34] reported that fragments produced during the protein degradation affected the α-chain's ability to form a gel network. In addition, shorter chains of gelatin protein cannot form a strong inter-junction zone, lowering gelling ability and gel strength [35]. ...
Salted sand-type jellyfish by-products are abundant in collagen, which may be processed into gelatin to decrease food waste. From the production standpoint, various factors affect gel qualities, including raw material used, pretreatment methods, and extraction times. So far, gelatin extracted from desalted sand-type jellyfish by-products (D-SJB) must be adequately characterized. Therefore, this research aimed to characterize gelatin from D-SJB using different pretreatment methods and extraction times. D-SJB was treated with 0.2 M hydrochloric acid (acid method) and extracted for 24 h at 60 °C (SA24), the optimal gelatin extraction condition with the highest gel qualities, while the jellyfish gelatin obtained after D-SJB was treated with pepsin and extracted for 48 h had the lowest gel qualities. The viscosity, gel strength, gelling temperature, and melting temperatures of SA24 were 20.80 cP, 352.22 g, 11.97 °C, and 22.70 °C, respectively. All jellyfish gelatin’s gelling and melting temperatures ranged from 6.13−11.97 °C and 15.85−22.70 °C, exhibiting a cold set gel and unstable gels at room temperature. The different pretreatment methods and extraction times during the jellyfish gelatin production resulted in the conversion of amides A, B, I, II, and III, especially the wavenumber of the amide I increased after pepsin pretreatment and increased with longer extraction time. Twenty-one collagen subtypes in bovine, fish, and jellyfish gelatin were analyzed using LC-MS/MS. The collagen alpha-2(I) chain, a key gelatin component, was identified in all gelatins. The research novelty showed the profound characterization results of gelatin gel produced from D-SJB. However, further experiments will be needed for pilot-scale production to be used in food and non-food applications.
... The by-product of the smooth-hound shark (Mustelus mustelus) was recovered following processing at a fish market located in Sfax, Tunisia. Gelatin was extracted from the fish skin using a process that included citric acid treatment as previously described [19], with minor adjustments made to the procedure. Briefly, the skin was washed with tap water and cut into small pieces measuring 1 × 1 cm. ...
This study aimed to investigate the ability of aqueous extract of Lepidium sativum seeds (LSE) to improve the wound healing process in rat models. The gelatin, extracted from the skin of smooth-hound shark using citric acid, was used as a support material for ointment. Animals were divided into four groups of six rats each: an untreated control group, a control group treated with Moist Exposed Burn Ointment (MEBO), a treated group with gelatin gel, and a treated group with gelatin gel fortified with 20 mg/mL LSE. Phenolics profile analysis showed that the major compounds in LSE were catechin (125 μg/g) and quinic acid (105 μg/g). In vitro antioxidant tests showed that LSE has interesting activities to scavenge ABTS•+ radicals (IC50 = 0.22 mg/mL) and inhibit the oxidation of linoleic acid. A significant decline in the antioxidant enzymes activities and an increase in the level of thiobarbituric acid reactive substances (TBARS) and inflammatory markers was observed within the injured tissues of the untreated rats compared to rats treated with MEBO. Interestingly, when the wounded tissue was treated with gelatin gel a remarkable reversal of this trend occurred. Further, by enrichment of gelatin gel with LSE, the levels of CAT, GPx and SOD activities significantly increased by 35, 126, and 212 %, respectively, whereas the TBARS level was reduced by 31 %. These results were consistent with the wound contraction percentage and histological analysis, which suggest the potential effect of LSE-enriched gelatin gels to regenerate damaged tissues.
... For protein content, all mixing ratios could successfully achieve the targeted protein content (6 g/100 g) in the mixed gels, which is a minimum requirement for senior-friendly foods in the Korean Industrial Standard [18]. Moreover, replacing pig gelatin with soy protein isolate and whey protein concentrate could increase the ash content of the mixed gelatin gels because commercial gelatin is generally demineralized [19]. The calorie content of the gelatin-only gel (control) was 26.16 kcal/100 g and replacing gelatin with the globular proteins could slightly increase the calorie content of the mixed gelatin gels (p < 0.05). ...
The physicochemical properties of the mixed gelatin gels with soy and whey proteins were investigated to develop the gel base with a soft texture and abundant essential amino acids for the elderly. Gelatin-only gel (control) was prepared at 6% (w/v), and mixed gelatin gels were formulated by replacing gelatin with soy protein isolate and whey protein concentrate at different mixing ratios [gelatin (G):soy protein isolate (S):whey protein concentrate (W)]. Results showed that replacing gelatin with the globular proteins in gelatin gels increased the pH value and processing yield (p < 0.05). Moreover, the mixed gelatin gels, particularly the G2:S1:W3 treatment, showed significantly higher essential amino acids than the gelatin-only control. The partial replacement of gelatin with the globular proteins could decrease the hardness of gelatin gel (p < 0.05), but there was no difference in hardness between the G2:G3:W1, G2:S2:W2, and G2:S1:W3 treatments (p > 0.05). The results of protein pattern, x-ray diffraction, and microstructure had no clear evidence for specific protein–protein interaction in the mixed gelatin gels. Therefore, this study indicates that mixed gelatin gels with the globular proteins at specific mixing ratios could be a practical approach to providing a soft texture and high-level essential amino acids to the elderly.
... Tulang kambing Kacang mengandung protein kolagen dan dapat diekstraksi menghasilkan gelatin. Keterbatasan utama pemakaian tulang sebagai bahan baku gelatin, khususnya hewan mamalia antara lain karena struktur tulang padat dan keras dengan kadar abu yang tinggi, sehingga memerlukan waktu perlakuan awal yang panjang, yaitu sekitar 20 sampai 60 hari untuk pembengkakan dan penghilangan kandungan mineral tulang, dengan hasil ekstraksi yang sangat rendah (Ma et al., 2019). Di samping tingginya kadar abu pada tulang, tentunya sangat mempengaruhi sebagian besar karakteristik fisik, kimia dan fungsional gelatin yang dihasilkan dan dapat melebihi batas yang ditetapkan untuk makanan, dengan demikian menarik untuk menggunakan metode ekstraksi yang tepat sesuai bahan baku tulang. ...
Penelitian ini bertujuan untuk mengevaluasi sifat kimia, fisik dan fungsional gelatin tulang kambing Kacang yang diekstraksi menggunakan bromelin dengan perlakuan konsentrasi yang berbeda, yaitu GB-0 (gelatin dengan bromelin 0 %), GB-1 (Gelatin dengan bromelin 10 U), GB-2 (Gelatin dengan bromelin 15 U dan GB-3 (Gelatin dengan bromelin 20 U). Tulang yang digunakan adalah tulang kambing kacang. Rancangan penelitian yang digunakan adalah rancangan acak lengkap pola searah dengan 4 perlakuan konsentrasi bromelin dengan 5 ulang. Parameter yang diamati adalah rendemen, analisis proksimat (kadar air, abu, lemak dan protein kasar), pH, distribusi berat molekul protein, profil gugus fungsional FTIR, morfologi, foaming expansion (FE) dan stability (FS) serta kapasitas dan stailitas emulsi gelatin. Hasil penelitian menunjukan bahwa rendemen tertinggi pada gelatin tulang kambing Kacang dengan perlakuan bromelin 20 U (GB-3), adalah 8,31%. Kadar air, protein, sifat foaming dan emulsi tertinggi dengan perlakuan bromelin 15 U (GB-2), dengan pH, kadar abu terendah. Rantai ß telah terdegradasi, rantai α1 dengan berat molekul 31,00 - 91,12 kDa, menghilangnya tripel heliks ditunjukkan FTIR dan struktur gel yang lebih halus, kompak dengan rongga yang lebih kecil pada gelatin GB-1 dan GB-2. Kesimpulan dari penelitian ini adalah bromelin 15 U/g tulang dapat digunakan untuk ekstraksi tulang kambing Kacang dengan menghasilkan gelatin dengan sifat fisiokimia dan fungsional yang dapat digunakan untuk aplikasi pangan. ABSTRACT This study aims to evaluate the chemical, physical, and functional properties of Kacang goat bone Kacang gelatin extracted using different concentrations of bromelain. The concentrations used were GB-0 (gelatin with 0% bromelain), GB-1 (gelatin with 10 U bromelain), GB-2 (gelatin with 15 U bromelain), and GB-3 (gelatin with 20 U bromelain). Kacang Goat bones were used for the extraction. The research design employed a completely randomized unidirectional design with 4 bromelain concentration treatments and 5 repetitions. The parameters observed included yield, proximate analysis (moisture, ash, fat, and crude protein content), pH, protein molecular weight distribution, FTIR functional group profile, morphology, foaming expansion (FE) and stability (FS), the capacity and stability gelatin emulsions. The results of the research showed that the highest yield of goat Kacang bone gelatin was obtained with the 20 U bromelain treatment (GB-3), which yielded 8.31%. The gelatin extracted with the 15 U bromelain treatment (GB-2) had the highest water content, protein content, foaming properties, and emulsion properties, as well as the lowest ash content and pH. The ß chain of the gelatin was degraded, while the α1 chain had a molecular weight of 31.00 - 91.12 kDa. The FTIR analysis showed the disappearance of the triple helix structure, and the gel structure of GB-1 and GB-2 gelatin was smoother and more compact with smaller cavities. In conclusion, bromelain at a concentration of 15 U/g bone can be used for the extraction of Kacang goat bones, resulting in gelatin with desirable physiochemical and functional properties suitable for food applications.
... These findings were comparable to those observed for gelatin extracted from bovine bone using pepsin and acid pretreatment [42]. Gelatin chain interactions, which were a key factor in the creation of the gel network, were impacted by the skin pretreatment [16,43]. ...
Gelatin derived from marine by-products could be an interesting alternative to classic mammalian gelatin. The pretreatment and extraction conditions could influence the size of the resulting peptide chains and therefore their techno-functional properties. Thus, it is important to optimize the production process to get a gelatin for the appropriate applications. Skin pretreatment was done by microwaves or oven-drying and the extracted gelatin was dried by spray- or freeze-drying. Freeze-dried gelatin extracted from untreated skin (FGUS) had the highest gelatin yield (10.40%). Gelatin proximate composition showed that proteins were the major component (87.12–89.95%), while lipids showed the lowest contents (0.65–2.26%). Glycine showed the highest level (299–316/1000 residues) in the extracted gelatins. Proline and hydroxyproline residues of gelatins from untreated skin were significantly higher than those from pretreated skin-gelatin. FTIR spectra were characterized by peaks of the amide A (3430-3284 cm⁻¹), B (3000-2931 cm⁻¹), I (1636–1672 cm⁻¹), II (1539–1586 cm⁻¹) and III (1000–1107 cm⁻¹). Spray-drying decreased the gelling properties of gelatins, since it reduced gelling and melting temperatures compared to freeze-drying. Skin pretreatment significantly reduced the gel strength of gelatin by about 50–100 g depending on the gelatin drying method. The FGUS showed better surface properties compared to other gelatins. The highest emulsion activity index (39.42 ± 1.02 m²/g) and foaming expansion (172.33 ± 2.35%) were measured at 3% FGUS. Therefore, the promising properties of freeze-dried gelatin derived from untreated skin, gave it the opportunity to be successfully used as a techno-functional ingredient in many formulations.
... Exhibit 2 shows that the by-products most used for the extraction of gelatin and collagen were the skin and scales of the fish because they are the residues generated in greater quantity and have a higher composition of collagen and gelatin (Bou-Gharios et al., 2020;Usman et al., 2021). In addition, different extraction methods have been reported and their use varies according to the fish waste (scales, fins, skin, viscera, and bones) and final product application, as they influence the physical characteristics such as bloom force, color, and pH, and may compromise or favor the application in food products (Ma et al., 2019). ...
The fishing industry is responsible for generating large amounts of organic waste rich in compounds of commercial interest. This review aimed to present the state of the art about the possibilities of using solid waste to obtain value-added products. Skins, fins, and scales have been used to obtain gelatin and collagen, a promising compound for use as an additive in yogurts and creams, as well as for the synthesis of biodegradable packaging that, if applicable, can reduce the environmental impact caused by petroleum packaging. Other parts, such as the head and the viscera, contain polyunsaturated fatty acids and other fat-soluble vitamins that have been studied for the production of omega-3 capsules for the pharmaceutical industry, but when the extracted oil does not fit the feeding parameters, it can be applied for the production of biodiesel. Furthermore , fishes are a promising source of astaxanthin, a carotenoid with high antioxidant properties. The use of combined techniques such as chemical and enzymatic methods can increase the extraction yield and favor the obtaining of more purified compounds, in addition to promoting the reduction of chemicals that are aggressive to the environment. In general, conscious production in the fishing industry through the valorization of waste generated for use as inputs for other value chains encompasses aspects of the circular economy, which can positively impact several Sustainable Development Goals.
... Gelatin was extracted from defatted bovine granules using the enzymatic method (27), as shown in Figure 1. Defatted bovine granules were soaked in 1 M hydrochloric acid (HCl) (Sinopharm Chemical Reagent Co., Ltd., Shanghai, China) at 25 • C for 3 h with continuous shaking at the solid-to-solvent ratio of 1:9 (w/v). ...
Geographical traceability is crucial to the quality and safety control of gelatin. However, currently, methods for gelatin traceability have not been established anywhere in the world. This study aimed to investigate the possibility of differentiating the geographical origins of gelatin from different regions in China using stable isotope technology. To achieve this objective, 47 bovine stick bone samples from three different regions (Inner Mongolia, Shandong, and Guangxi, respectively) in China were collected, and gelatin was extracted from these bones using the enzymatic method. The fingerprint characteristics of stable isotopes of δ¹³C, δ¹⁵N, and δ²H of gelatin from different regions in China were studied. Moreover, isotopic changes from the bone to gelatin during the processing were examined to evaluate the effectiveness of these factors as origin indicators. The results of the one-way analysis of variance (ANOVA) showed that the δ¹³C, δ¹⁵N, and δ²H of gelatin from different regions display significant differences, and using the linear discriminant analysis (LDA), the correct differentiation of origin reached 97.9%. Certain differences in stable isotope ratios were observed during the processing of bone to gelatin samples. Nonetheless, the fractionation effect caused by the processing of bone to gelatin samples was not sufficient to influence the identification of gelatin from different origins, which proves that δ¹³C, δ¹⁵N, and δ²H are effective origin indicators of gelatin. In conclusion, the stable isotope ratio analysis combined with the chemometric analysis can be used as a reliable tool for identifying gelatin traceability.
... The exception is for bones for which demineralization is necessary. This is done in an acidic environment [24]. Gelatin extraction is carried out with hot water (depending on the type of raw material at a temperature of 40 • C minimum) in extractors of various designs. ...
During the production of mechanically deboned chicken meat (MDCM), a by-product is created that has no adequate use and is mostly disposed of in rendering plants. Due to the high content of collagen, it is a suitable raw material for the production of gelatin and hydrolysates. The purpose of the paper was to process the MDCM by-product into gelatin by 3-step extraction. An innovative method was used to prepare the starting raw material for gelatin extraction, demineralization in HCl, and conditioning with a proteolytic enzyme. A Taguchi design with two process factors (extraction temperature and extraction time) was used at three levels (42, 46, and 50 °C; 20, 40, and 60 min) to optimize the processing of the MDCM by-product into gelatins. The gel-forming and surface properties of the prepared gelatins were analyzed in detail. Depending on the processing conditions, gelatins are prepared with a gel strength of up to 390 Bloom, a viscosity of 0.9–6.8 mPa·s, a melting point of 29.9–38.4 °C, a gelling point of 14.9–17.6 °C, excellent water- and fat-holding capacity, and good foaming and emulsifying capacity and stability. The advantage of MDCM by-product processing technology is a very high degree of conversion (up to 77%) of the starting collagen raw material to gelatins and the preparation of 3 qualitatively different gelatin fractions suitable for a wide range of food, pharmaceutical, and cosmetic applications. Gelatins prepared from MDCM by-product can expand the offer of gelatins from other than beef and pork tissues.
... The vast majority of researches have dealt with gelatin production by enzymes from animal bones Hosseini-Parvaret et al., used an optimized conditions for enzymatic extraction of edible gelatin from the cattle bones using response surface methodology [18]. In 2019, Ma and his co-workers proposed a simple and ecofriendly method for gelatin production from bones as one-step biocatalysis [21]. A number of US patents have been published for the same scope [22][23][24]. ...
... From the point of view of energy consumption and energy efficiency of production, the aim should be to maximize the value of At23 (at level IV, Figure 1) as the so-called energy input, i.e. simultaneously strive to increase the total energy transformation coefficient ηIII = At23/At2. Previous studies most often present the consumption of heat or electricity separately at level III [22,28,29]. It should be noted that from the point of view of costs and the choice of a specific technology, it is important to use the cumulative energy consumption of a product or an indicator that would include the total energy consumption both in the production plant (At2) as well as converted to primary energy (At1). ...
Nexus water-energy-food can be represented on a micro scale using the example of gelatine production in a rendering plant. The article presents the results of research on the variability of energy and water consumption in a rendering plant producing food gelatin. Monthly production was 565.2–631.3 Mg of gelatin and on average 18.89 Mg of gelatin was produced per day. The power of the installed electrical devices was 1150 kW. The average unit consumption of water was 18.97 m3/Mg, heat energy 22.39 GJ/Mg and electricity 1174.76 kWh/Mg. The influence of gelatine production on energy and water consumption was determined. It has been shown that in the examined plant there is an increased by about 20–30% non-production consumption of energy and water, which in the future should be reduced by introducing technological innovations. Moreover, it has been shown that there is a possibility of increasing production efficiency. The obtained energy efficiency and unit consumption indicators can be used to define environmental standards as well as eco-efficiency and production costs important for management of the enterprise.
... The use of protease enzyme in gelatin manufacturing especially in the pre-treatment (swelling process) stage, is consequently attracting significant attention of researchers to reduce the environmental impact and also towards the ability of the enzyme to increase the yield and quality of gelatin extracted . Here, modified enzymatic pre-treatment is often used to substitute the acid or liming process to hydrolyse the native collagen which demonstrates shorter processing time, higher yield and generating less water (Damrongsakkul et al., 2008;Ma et al., 2019). ...
This study was carried out to extract gelatin from the bone of Buffalo (Bubalus bubalis) by incorporating enzymatic pre-treatment. Papain-aided extraction (PE) (9.1 ppm of papain at 50 °C water) was employed in the pre-treatment step, in which non-enzymatic extraction (NE) was carried out for comparison. The gelatin obtained were next evaluated for their physicochemical properties such as moisture, protein, and ash content, colour, and UV-vis absorption. Functional properties of the gelatin which included emulsifying and foaming properties were also determined. Four-fold increments in yield (wet basis) were obtained for PE (29.92 %) as compared to NE (7.5 %). Moreover, no significance difference (p > 0.05) in moisture content was observed for both PE and NE, although the protein content of the gelatin was observed in the range between 70-90 %. The resulting gelatin from both extractions was generally yellowish in appearance and was confirmed by the colourimetry data where no significant difference (p > 0.05) was observed for both samples. The maximum absorption peak for both PE and NE were observed at 210 nm, which was in the range commonly reported for gelatin. In addition, the emulsifying and foaming capacity of PE and NE had no significant difference (p > 0.05), although emulsion stability for PE was shown to be significantly higher (p < 0.05) compared to NE. The present study was an attempt to evaluate the potential use of local buffalo bone as raw material for gelatin production, which found that extractability could be improved with enzymatic pre-treatment in obtaining acceptable gelatin qualities.
... Different researches have investigated the effects of different enzymatic reactions on the physicochemical characteristics of gelatin obtained from various sources including fish, bovine, and porcine (Ahmad et al., 2020;Gaspar-Pintiliescu et al., 2019;Kouhdasht et al., 2018). In a study performed by Ma, Zeng, Ma, Yang, and Zhao (2019), a novel single-step enzymatic procedure was suggested to extract the gelatin from porcine bones by which the 3 to 8 weeks hydrolysis of ossein was reduced to 3 hr. However, there is still a gap between the enzymatic procedures and gelatin extracted from different fish species. ...
The objective of this study was to investigate the effects of the enzymatic aided acid‐swelling process on gelatin obtained from fish by‐products. For this purpose, gelatin was extracted by an acidic swelling procedure in the presence of protease extracted from Rainbow trout pyloric caeca. The yield of gelatin extraction and the most important physicochemical characteristics of the fish gelatin samples were investigated and compared with those of commercial bovine gelatin (CBG). The yields of gelatin from Epinephelus coioides skin (ESG) either with or without crude protease from pyloric caeca (15 units/g alkaline treated) were 14.98% and 50.89%, respectively. The yields of gelatin from Cyprinus carpio scales (CSG) with crude protease from pyloric caeca (15 units/g) were 49.97%. The gel strength of the CSG (259.66 g) was significantly higher than that of CBG (228.30 g) and ESG (187.75 g). Similarly, the gelling and melting points, foaming capacity and stability, and the SDS‐PAGE pattern of gelatins were compared. The electrophoretic pattern confirmed the results of gel strength which was due to the narrower alpha and beta bands in fish skin and commercial bovine gelatins than that of fish scales gelatin. The results of this research showed that the production of high‐quality gelatin can be achieved by the enzymatically aided acid‐swelling procedure from fish scales and skin. In this study, gelatin extraction efficiency was improved by an acid‐swelling process in the presence of protease extracted from Rainbow trout pyloric caeca. The results of this research showed that the production of high‐quality gelatin can be achieved by the enzymatically aided acid‐swelling procedure from fish scales and skin.
... This may be explained by the fact that collagenase degrades native collagen by targeting the polar zone of the molecule with a (Gly-Pro-y)n sequence, whereas chitosan can only be degraded by enzymes that hydrolyze glucosamine-glucosamine, glucosamine-N-acetyl-glucosamine, and N-acetyl-glucosamine-N-acetyl-glucosamine bonds, such as chitinases and lysozymes [37]. Therefore, chitosan improved the ability to resist collagenase degradation, preventing the action of the enzyme [38]. The lowest EDD value observed for collagen scaffolds with LMW chitosan may be related to the crosslinking between collagen and chitosan. ...
Native collagen scaffolds were prepared in this work, in which both materials and environmental approaches were considered with the aim of providing a global strategy towards more sustainable biomaterials. From the environmental perspective, it is worth mentioning that acid and enzymatic treatments have been avoided to extract collagen, allowing the reduction in the use of resources, in terms of chemicals, energy, and time, and leading to a low environmental load of this step in all the impact categories under analysis. With the incorporation of chitosan into the scaffold-forming formulations, physical interactions occurred between collagen and chitosan, but the native collagen structure was preserved, as observed by Fourier transform infrared (FTIR) and X-ray diffraction (XRD) analyses. The incorporation of chitosan also led to more homogenous porous microstructures, with higher elastic moduli and compression resistance for both dry and hydrated scaffolds. Furthermore, hydrated scaffolds preserved their size and shape after some compression cycles.
... Сировина для виробництва желатину є постійно відновлюваною, доступною, оскільки у багатьох технологіях є відходами (кістки тварин, шкіра, луска риби тощо) (Karim & Bhat, 2009;Rbii et al., 2011;Ma et al., 2019). ...
Великий попит на кисломолочні продукти, зокрема йогурт, вимагає використання якісної сировини. Наявність у молоці факторів, які негативно впливають на мікроорганізми закваски йогурту, потребує використання біотехнологічних методів їх іммобілізації. Для дослідження використано модифікований желатин, на якому іммобілізували різні дози закваски для йогурту (від 5 мг до 100 мг), розчиняючи в різних об’ємах розчинника 0,2 см3, 0,3 та 0,4 см3 дистильованої води. Маса носія залишалася сталою – 1000 мг. Свіжовиготовлені препарати відразу висушували, застосовуючи активне вентилювання і перемішування. Встановлювали вміст вологи у іммобілізованих заквасках через 15 хвилин висушування, а також визначали час, протягом якого вологість іммобілізованих заквасок досягала 7–9%. Експериментально встановлено, що за 15-хвилинного висушування іммобілізована на модифікованому желатині закваска йогурту, де використовували 0,2 см3 розчинника, мала вологість на рівні 11,5–12,6%. Вологість заквасок, іммобілізацію яких проводили із застосуванням 0,3 та 0,4 см3 дистильованої води, після 15-хвилинного висушування становила, відповідно, 17,2–18,3% та 22,4–24,8%. Підвищення об’єму дистильованої води для розчинення різних доз заквасок супроводжувалося збільшенням вологи у препаратах за 15-хвилинного висушування, відповідно, до 22,4–24,8% від загальної маси. При відпрацюванні технології іммобілізації клітин мікроорганізмів закваски для йогурту на модифікованому желатині встановили, що найшвидше проходить висушування препаратів (32,4–37,2 хвилини), для створення яких використовували 0,2 см3 розчинника на 1 г носія. Підвищення об’єму розчинника до 0,3 см3 веде за собою збільшення часу висушування до 43,5–54,2 хвилини. Висушування іммобілізованих заквасок до вмісту в них вологи 7–9%, для конструювання яких застосовували 0,4 см3 дистильованої води, тривало більше однієї години. Доведено, чим більша маса закваски іммобілізована на модифікованому желатині, тим час висушування препаратів збільшується. Таким чином, з технологічної точки зору, розчинення 5–100 мг закваски для йогурту у 0,2 см3 дистильованої води є оптимальним.
... Nevertheless, chemical pretreatment is often harmful to the environment. In addition, the overall extraction efficiency of gelatin is typically low, limiting industrial output [9]. Taken together, the conventional methods used for the preparation of gelatin hydrolysates are generally reactant-, cost-and time-consuming and even bad for the environment. ...
Protein hydrolysates from fish by-products have good process suitability and bioavailability in the food industry. The objective of this work was to develop a method for protein recovery from fish scales and evaluate the hydrolysis of the scale protein. The effect of the hydrothermal process on protein recovery, degree of hydrolysis (DH) and structural properties of the hydrolysates was investigated. Results showed that hydrothermal treatment could enhance protein recovery of tilapia scales without demineralization and dramatically improve the DH of the hydrolysates. The hydrothermal treated scales showed a better protein recovery (84.81%) and DH (12.88%) and released peptides more efficiently than that of the conventional treated samples. The obtained gelatin hydrolysates mainly distributed in the range of 200–2000 Da with an angiotensin I-converting enzyme (ACE) IC50 value of 0.73 mg/mL. The ACE inhibitory activity of gelatin hydrolysates was stable under high temperature, pH and gastrointestinal proteases. Hydrothermal treatment followed by enzymatic hydrolysis offers a potential solution for preparation of gelatin hydrolysates for food ingredients from fish processing by-products.
Gelatin adalah protein yang dihasilkan dari proses hidrolisis kolagen, merupakan biomaterial penting dengan berbagai aplikasi industri. Kolagen, protein struktural utama pada jaringan ikat hewan, diperoleh dari kulit, tulang, dan jaringan ikat. Kemampuan gelatin untuk menyerap air 5-10 kali beratnya dan membentuk gel yang dapat dilelehkan kembali membuatnya ideal untuk berbagai aplikasi. Struktur molekul gelatin yang kompleks memberikannya karakteristik unik seperti kekuatan dan stabilitas, berasal dari asam amino prolin atau hidroksiprolin, dan fleksibilitas dari glisin. Kombinasi ini memungkinkan gelatin untuk membentuk gel yang kuat dan elastis, ideal untuk berbagai aplikasi. Secara tradisional, gelatin diperoleh dari dua sumber utama: gelatin sapi dan gelatin babi dengan metode asam (tipe A) atau metode alkali (tipe B). Namun, saat ini, kulit dan tulang dari berbagai hewan seperti kambing, kerbau, domba, ayam, dan ikan juga menjadi alternatif sumber bahan baku gelatin. Bagian dermis kulit sering dipilih karena kandungan kolagennya yang tinggi, sementara tulang rawan, tulang sumsum, dan tulang kompak merupakan sumber kolagen yang baik untuk produksi gelatin. Sebelum proses ekstraksi, bahan baku harus melalui pretreatment. Pretreatment biasanya melibatkan penggunaan bahan kimia seperti asam, alkali, atau enzim untuk mempersiapkan bahan baku sehingga gelatin dapat diekstraksi secara efisien. Beberapa teknologi modern yang digunakan dalam ekstraksi gelatin termasuk metode Ultrasound-Assisted Extraction (UAE), Subcritical Water Extraction (SWE), High-Pressure Processing (HPP), dan Microwave-Assisted Extraction (MAE). Teknologi seperti UAE dan MAE telah terbukti dapat meningkatkan hasil ekstraksi dan menjaga kualitas gelatin dengan lebih baik, sekaligus mengurangi risiko degradasi termal. Meskipun metode konvensional masih sering digunakan karena biaya operasional yang lebih rendah dan kemudahan dalam produksi skala besar, metode modern menawarkan beberapa keunggulan. Keunggulan ini termasuk ramah lingkungan dan kualitas fungsional gelatin lebih baik. Oleh karena itu, metode modern menjadi alternatif menarik untuk dipertimbangkan dalam produksi gelatin, terutama untuk aplikasi yang membutuhkan kualitas gelatin yang lebih tinggi.
In the present work, lignin nanospheres (LNS, average diameter 166.43 nm) were prepared and the affecting parameters, the absorbed types, and mechanisms of their interactions with type-A gelatin (AG) were explored. The findings demonstrated that upon AG coating, the ζ-potential of LNS sharply decreased and concluded a negative-to-positive shift, while the average diameter and polydispersity index increased significantly. AG presented the highest coating capacity (0.32 mg/mg, db) onto LNS (0.5 mg/mL) at an optimum pH of 4.0 and an AG concentration of 1.0 mg/mL. The adsorption of AG onto LNS could be well described by the Hill model (R2 = 0.9895), which was characterized as positive synergistic adsorption by the Hill coefficient (1.32) and physical adsorption by the free energy (3.70 kJ/mg). The spectral analysis revealed that the interactions between AG and LNS were mainly driven by electrostatic forces (ΔG < 0, ΔH < 0, and ΔS > 0) together with the assistance of hydrogen bonds and hydrophobic interactions, which companied a decrease of α-helix (4.04 %) and β-turn (0.60 %) and an increase of β-sheet (3.10 %) and random coil (1.53 %) of the secondary structure of AG. The results herein certainly favored the hydrophilic/hydrophobic change of LNS/AG and the quality control of a binary system consisting of lignin and gelatin.
Gelatin is one of the most important multifunctional biopolymers and is widely used as an essential ingredient in food, pharmaceutical, and cosmetics. Porcine gelatin is regarded as the leading source of gelatin globally then followed by bovine gelatin. Porcine sources are favored over other sources since they are less expensive. However, porcine gelatin is religiously prohibited to be consumed by Muslims and the Jewish community. It is predicted that the global demand for gelatin will increase significantly in the future. Therefore, a sustainable source of gelatin with efficient production and free of disease transmission must be developed. The highest quality of Bovidae‐based gelatin (BG) was acquired through alkaline pretreatment, which displayed excellent physicochemical and rheological properties. The utilization of mammalian‐ and plant‐based enzyme significantly increased the gelatin yield. The emulsifying and foaming properties of BG also showed good stability when incorporated into food and pharmaceutical products. Manipulation of extraction conditions has enabled the development of custom‐made gelatin with desired properties. This review highlighted the various modifications of extraction and processing methods to improve the physicochemical and functional properties of Bovidae‐based gelatin. An in‐depth analysis of the crucial stage of collagen breakdown is also discussed, which involved acid, alkaline, and enzyme pretreatment, respectively. In addition, the unique characteristics and primary qualities of BG including protein content, amphoteric property, gel strength, emulsifying and viscosity properties, and foaming ability were presented. Finally, the applications and prospects of BG as the preferred gelatin source globally were outlined.
Biopolymers are natural polymers sourced from plants and animals, which include a variety of polysaccharides and polypeptides. The inclusion of biopolymers into biomedical hydrogels is of great interest because of their inherent biochemical and biophysical properties, such as cellular adhesion, degradation, and viscoelasticity. The objective of this Review is to provide a detailed overview of the design and development of biopolymer hydrogels for biomedical applications, with an emphasis on biopolymer chemical modifications and cross-linking methods. First, the fundamentals of biopolymers and chemical conjugation methods to introduce cross-linking groups are described. Cross-linking methods to form biopolymer networks are then discussed in detail, including (i) covalent cross-linking (e.g., free radical chain polymerization, click cross-linking, cross-linking due to oxidation of phenolic groups), (ii) dynamic covalent cross-linking (e.g., Schiff base formation, disulfide formation, reversible Diels-Alder reactions), and (iii) physical cross-linking (e.g., guest-host interactions, hydrogen bonding, metal-ligand coordination, grafted biopolymers). Finally, recent advances in the use of chemically modified biopolymer hydrogels for the biofabrication of tissue scaffolds, therapeutic delivery, tissue adhesives and sealants, as well as the formation of interpenetrating network biopolymer hydrogels, are highlighted.
Lipase immobilization processes have the potential to drive large-scale industrial applications through cost savings. Among them, the Pickering emulsion system has recently emerged as an ecofriendly technique for enhanced enzymatic activity. In this study, a novel and facile immobilization of lipase in an ultrasoundassisted Pickering emulsion system was developed. The lipase loading amount and yield
was 177.3 mg/g and 41.3%, respectively. In the enzymatic synthesis of four sterol lipoates, the immobilized lipase (UIP-HMSS@CRL) achieved the highest catalytic efficiency (CE) of 6.4 mmol/g·h among the reported methods, which was 9.1-fold higher than that of free lipase and 32.0-fold higher than that of previous methods. UIPHMSS@CRL performed with much higher Vm and lower Km, indicating the excellent catalytic rate and stronger affinity. Moreover, UIP-HMSS@CRL displayed satisfying thermal stability and recyclability, retaining 88.6% of enzyme activity after 10 cycles. The lipase lid was opened at the oil−water interface by both ultrasound and interfacial
synergistic activation effect, which provided easier access to an active site and thus achieved excellent catalytic performance. This
ultrasound-assisted interface immobilization would open new opportunities for preparation of high-performance and sustainable
biocatalysts.
The first ever ecological and ethical assessment of animal gelatin in analogue photographic film, calculating the environmental impact of film and the moral quandary that arises from using a product so tied to the structural violence of industrial animal agriculture - ultimately asking, is art a legitimate reason to exploit nonhumans and devastate our natural environment?
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