Mammalian Gelatin Research Articles

Preparation and Characterization of Waste Fish Bone-Derived Gelatin/Chitosan Plastic Film Incorporated with Green Tea Extract

Fish-derived gelatin has recently been spotlighted as an alternative source following the negative issues of mammalian gelatin, but unfortunately it has poor mechanical properties that limit its application. Herein, an environmental-friendly film was prepared from milkfish (Chanos chanos) bone waste-derived gelatin and modified by adding chitosan, glycerol and sorbitol plasticizers as well as green tea extract to improve its mechanical properties. Gelatin was processed from milkfish bone waste using various concentrations of H2SO4 solution (2%, 3%, and 5%) (v/v) and soaking times of 18 h and 36 h for each of the solutions. The measurement test of pH, ash content, and moisture content were conducted on the gelatin product, and the characteristic functional groups were investigated using Fourier- Transform Infrared Spectroscopy (FTIR). The effect of green tea addition was also evaluated on the thickness, tensile strength, and elongation of the resulting films. The results showed that treatment using H2SO4 concentration of 3% with 36 hours of immersion time produced the best gelatin quality with a pH value of 5.9. Water content and ash content were 14.286% and 3.09%, respectively. The plastic film from this study has mechanical properties similar to polypropylene plastic so that it is expected to be a potential material for food packaging applications.

Comparative analysis of red skin Tilapia and bovine gelatins as halal alternatives in food industry

Gelatin plays a vital role in the food industry, serving as a thickening agent, emulsifier, wetting agent, and stabiliser. However, conventional sources like mammalian gelatin pose health and societal issues, while poultry gelatin can present risks related to avian flu. Our work was motivated by recent studies focusing on alternative gelatin sources, which prompted further investigation. Our study aimed to extract gelatin from red-skin Tilapia and bovine sources. Both types of gelatin underwent pre-treatment using 0.2 M sodium hydroxide (NaOH) and 0.05 M acetic acid (CH3COOH) at 27ºC, followed by water extraction at 60°C for 3 hours. Fourier-transform infrared (FTIR) analysis confirmed that the extracted gelatins exhibited peaks similar to commercial gelatin. The extracted fish gelatin (EFG) demonstrated superior gel strength compared to commercial fish gelatin (CFG), whereas commercial bovine gelatin (CBG) exhibited superior gel strength than extracted bovine gelatin (EBG). The protein content of EFG and EBG was comparable, but the fat content was significantly higher in EFG. The foaming capacity was also evaluated, with EFG showing greater capacity than EBG. Our work demonstrates excellent potential of alternative gelatin for usage in various applications and creates new opportunities for the food sector, particularly for halal food production.

Rheological Properties of Fish and Mammalian Gelatin Hydrogels as Bases for Potential Practical Formulations.

Hydrogels have the ability to retain large amounts of water within their three-dimensional polymer matrices. These attractive materials are used in medicine and the food industry; they can serve as the basis for structured food products, additives, and various ingredients. Gelatin is one of widely used biopolymers to create hydrogels that exhibit biocompatibility and tunable rheological properties. In this study, we offer a comparative analysis of rheological properties of gelatin-based hydrogels (C = 6.67%), including mammalian gelatins from bovine and porcine skins and fish gelatins from commercial samples and samples extracted from Atlantic cod skin. Mammalian gelatins provide high strength and elasticity to hydrogels. Their melting point lies in the range from 22 to 34 °C. Fish gelatin from cod skin also provides a high strength to hydrogels. Commercial fish gelatin forms weak gels exhibiting low viscoelastic properties and strength, as well as low thermal stability with a melting point of 7 °C. Gelatins were characterized basing on the analysis of amino acid composition, molecular weight distribution, and biopolymer secondary structure in gels. Our research provides a unique rheological comparison of mammalian and fish gelatin hydrogels as a tool for the re-evaluation of fish skin gelatin produced through circular processes.

Complex coacervation of low methoxy pectin with three types of gelatins for the encapsulation of fish oil

Herein, the complex coacervation of low methoxy pectin (LMP) with three types of gelatins was explored to encapsulate fish oil. The fish oil@gelatin-LMP complex coacervates with good precipitation separation could be obtained at low gelatin concentrations (Fish gelatin, FG: 10–80 mg/mL; porcine skin gelatin, PSG: 10–40 mg/mL; bovine skin gelatin, BSG: 10–80 mg/mL), high gelatin: fish oil mass ratios (4:1–1:1), appropriate gelatin: LMP mass ratios (3:1–12:1 for FG and PSG, 6:1 for BSG), and appropriate pH (FG: 4.90–5.50; PSG: 4.80–5.40; BSG: 4.10–4.50). FG induced similar loading ability, lower encapsulation ability, and comparable peroxide values to the mammalian gelatins. FG induced higher or similar free fatty acid released percentages to mammalian gelatins in the in vitro gastrointestinal model at low gelatin concentrations (10–40 mg/mL). These results provided useful information to understand the protein-polysaccharide complex coacervation to encapsulate oil-based bioactive substances.

In Vitro Hemostatic Activity of Novel Fish Gelatin-Alginate Sponge (FGAS) Prototype.

A hemostatic sponge prototype was successfully synthesized from fish gelatin as an alternative to mammalian gelatin; it was mixed with alginate in certain combinations, double cross-linked with calcium ions, and gamma irradiated at a dose of 20 kGy to improve the characteristics and effectiveness of its function as a local hemostatic agent. There were improvements in the physicochemical and mechanical properties, porosity index, absorption capacity, biodegradation properties, biocompatibility, and hemocompatibility of the fish gelatin-alginate sponge (FGAS) prototypes compared with the pure fish gelatin sponge. Hemostatic activity tests showed that the means for clotting time, prothrombin time, and activated partial thromboplastin time were shorter in the FGAS prototype than in the negative control, and there was no significant difference compared with the commercial gelatin sponge. The hemostatic mechanism of the FGAS prototype combined a passive mechanism as a concentrator factor and an active mechanism through the release of calcium ions as a coagulation factor in the coagulation cascade process.

Extraction and physicochemical characterization of native and broiler chicken feet gelatin.

Poultry processing generates a large amount of industrial waste, which is rich in collagen content. This waste can be utilized for the extraction of valuable components such as gelatin, which can be used as an alternative to mammalian gelatin (porcine and bovine). Gelatins were analyzed for their yield, proximate analysis, pH, color, viscosity, bloom strength, and texture profile analysis. The yield of broiler chicken feet gelatin (BCFG) was slightly higher (7.93%) as compared to native chicken feet gelatin (NCFG) (7.06%). The protein content was 85.92% and 82.53% for BCFG and NCFG. Both gelatin had moisture content in the standard range (< 15) as given by Gelatin Manufacturers of Europe (GME). Both gelatins showed higher bloom strength (326 g for NCFG and 203 g for BCFG) at 6.67% gelatin concentration, classified as high bloom. Fourier-transform infrared (FTIR) analysis showed amide I, amide A, amide B at 1636 cm-1, 3302 cm-1, 2945 cm-1 for NCFG and 1738 cm-1, 3292 cm-1, 2920 cm-1 for BCFG. At 6.67% gelatin concentration, hardness and cohesiveness values were also higher than commercial gelatin previously studied. The pH values for NCFG were 5.43 and BCFG was 5.31. Both NCFG and BCFG viscosities (4.43 and 3.85 cP) were in the optimum range of commercial gelatins (2-7 cP). Hence, the present study concluded that both NCFG and BCFG have a huge potential to replace commercial mammalian gelatins (porcine and bovine) in the food industries. However further studies should be done to optimize the extraction process. © 2024 Society of Chemical Industry.

Elucidating the rheological and thermal properties of mixed fish and pork skin gelatin gels: Effects of cooling conditions and incubation times

Gelatin is an important hydrocolloid in food and biotechnological applications. There are two basic sources of gelatins; mammalian and fish-derived gelatins, but fish gelatins are less appreciated due to their weak gel properties. Hence, to reinforce the gel properties of fish gelatin, mixtures of gelatins are used. In this study, the mixtures of cold-water ocean fish scale (OFS) and pork skin (PS) gelatin were studied via rheological measurements, micro differential scanning calorimetry (DSC), and particle tracking at different cooling conditions and incubation times to understand the gelation mechanism and the network structure of the gels. The rheological and micro-DSC measurements provide a detailed understanding of the gelation mechanism of gelatin gels under different cooling conditions while particle tracking revealed the local physical properties of the gels. A single or two-step melting was demonstrated in the mixed gelatin gels depending on the cooling conditions suggesting that the aggregation of PS in the mixtures influences the physical and thermal properties of the gels. Under rapid cooling, co-aggregation of OFS and PS chains is considered to cause a single-step melting of the mixed gels. Under gradual cooling, conversely, the PS may form aggregates independently before the OFS. This is evidenced by a two-step decrease in moduli and two clear endothermic peaks in the micro-DSC measurement. Particle tracking further reveals information on the local physical properties of pure and mixed gelatin gels on reheating, indicating that the local structures of mixed gels resemble those of pure PS gels. This suggests that mixed OFS and PS gels may form a cooperative aggregation, thereby improving the physical and thermal properties of the mixed gelatin gels.

Utilization of Blackmouth Catshark (Galeus melastomus) Skins as an Alternative Source of Gelatin: Extraction and Physicochemical Characterization in Comparison to Porcine Skin Gelatin

The present study investigated the potential use of blackmouth catshark (Galeus melastomus) skins for gelatin production by employing a combined alkaline and acidic process. The yield of dry gelatin was relatively high (13.95%), showing a high protein content (87.80%), but low moisture (10.64%), ash (1.34%) and lipid (0.03%) contents, on a wet weight basis. Fish skin gelatin showed better color properties (&gt;L*, &lt;+b* values) than porcine skin gelatin and exhibited similar gel strength (315.4 g) and higher viscosity (5.90 cP) than the latter (p &lt; 0.05). Although the electrophoretic study revealed that fish skin gelatin was degraded to a lesser extent than its mammalian counterpart, the resulting fish skin gelatin gels melted at a significantly lower temperature (Tm = 21.5 °C), whereas the reverse process (i.e., gelling) also occurred at a lower temperature (Ts = 10.6 °C) and required more time (ts = 29.5 min) compared to porcine skin gelatin gels (Tm = 30.4 °C, Ts = 19.4 °C and ts = 20.7 min). These differences were attributed to the different imino acid content, which was greater in mammalian gelatin (p &lt; 0.05). The results suggested that the skins from blackmouth catshark can be potentially used as an alternative raw material for gelatin production, which will fill the needs of more diverse cultures that do not consume pork- or cow-related products.

Marine polymers in tissue bioprinting: Current achievements and challenges

Abstract Bioprinting has a critical role in tissue engineering, allowing the creation of sophisticated cellular scaffolds with high resolution, shape fidelity, and cell viability. Achieving these parameters remains a challenge, necessitating bioinks that are biocompatible, printable, and biodegradable. This review highlights the potential of marine-derived polymers and crosslinking techniques including mammalian collagen and gelatin along with their marine equivalents. While denaturation temperatures vary based on origin, warm-water fish collagen and gelatin emerge as promising solutions. Building on the applications of mammalian collagen and gelatin, this study investigates their marine counterparts. Diverse research groups present different perspectives on printability and cell survival. Despite advances, current scaffolds are limited in size and layers, making applications such as extensive skin burn treatment or tissue regeneration difficult. The authors argue for the development of bioprinting, which includes spherical and adaptive printing. In adaptive printing, layers differentiate and propagate sequentially to overcome the challenges of multilayer printing and provide optimal conditions for the growth of deeply embedded cells. Moving the boundaries of bioprinting, future prospects include transformative applications in regenerative medicine.

Thermal stability of water-in-oil microemulsions containing solubilized nutritional protein gelatin

To develop new food and pharma technologies, various combinations of encapsulation and delivery of biological macromolecules are used. Proteins, polysaccharides, fats and lipids must be conveyed inside living organism, protecting them during the stages of storage and preparation from exposure of aggressive external environment. Some of the most common food protein compositions are various gels and emulsions. In the present study, we focused our attention on the influence of protein molecules on the properties and dynamical stability of water-inoil microemulsion. Microemulsions, the oil dispersion of surfactant-based reverse micelles, each carrying nanosized water core with embedded protein. We studied the result of protein encapsulation in the water core of surfactant reverse micelles, namely, the fish and mammalian gelatin. The method of electric conductivity was explored to detect the properties of reverse micelles as containers for food proteins. We have shown that a rather high protein content does not destroy microemulsion structure, which retain reverse micelles, though the properties of the system undergo definite alterations, in particular, it substantively lost thermal stability accelerating exchange processes between reverse micelles at lower temperatures which have to be taken into account in nutritional and pharmacy objectives.

Extraction and characterization of collagen and gelatin from body wall of sea cucumbers Stichopus horrens and Holothuria arenicola.

Marine invertebrates, including sponges, molluscs, jellyfish, mussels, and sea cucumbers, are abundant sources of high-quality collagen and offer advantages such as availability, ease of processing, lower inflammatory response, and good metabolic compatibility. Approximately 70% of the total protein in the body wall of sea cucumbers is collagen. Gelatin is a water-soluble protein produced from heat-denatured collagen and has various industrial applications. Pepsin-solubilized collagen was extracted from the body wall of two sea cucumber Stichopus horrens and Holothuria arenicola, species found in the Oman Sea and characterized with SDS-PAGE and amino acid composition. Then gelatin was extracted from pepsin-solubilized collagen of S. horrens and some rheological properties were measured. Amino acid composition and SDS-PAGE analysis showed that the collagen from both species was type I, with one α1 chain and β chains, with molecular weights of 125 and 250 kDa, respectively. Glycine was the most abundant amino acid in the collagen from both sea cucumber species. The pepsin-soluble collagens from both species had high levels of glycine, proline, alanine, glutamic acid, and hydroxyproline. The gelatin from S. horrens had a melting point of 30 °C and displayed exceptional thermal stability, surpassing that of mammalian gelatin. Its gelling point was 5 °C, like that of cold-water fish gelatin, with a viscosity of 2.065 cp-lower than mammal gelatins. These findings suggested that collagen and gelatin from sea cucumbers could be useful in nutraceutical, pharmaceutical and cosmetic industries.

Underused Marine Resources: Sudden Properties of Cod Skin Gelatin Gel.

The main object of this work was to characterize the structure and properties of laboratory-made fish gelatin from cod skin in comparison with known commercial gelatins of fish and mammalian origin. This is one way we can contribute to the World Food Program and characterize foodstuff resources from alternative natural sources. Our research was based on the combination of an expanded set of complementary physical-chemical methods to study the similarities and distinctions of hydrogels from traditional and novel gelatin sources from underused marine resources. In this work, we have compared the morphology, supramolecular structure and colloid properties of two commercial (mammalian and fish) gelatins with gelatin we extracted from cold-water cod skin in laboratory conditions. The obtained results are novel, showing that our laboratory-produced fish gelatin is much closer to the mammalian one in terms of such parameters as thermal stability and strength of structural network under temperature alterations. Especially interesting are our experimental observations comparing both fish gelatins: it was shown that the laboratory-extracted cod gelatin is essentially more thermally stable compared to its commercial analogue, being even closer in its rheological properties to the mammalian one.

Techno-functional characterization of gelatin extracted from the smooth-hound shark skins: Impact of pretreatments and drying methods

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.

Controlling the supramolecular ordering of fish gelatin via simultaneous assembly with fucoidan resulting in nanostructural modification and enhanced rheological performance

Fish gelatin (FG) has been identified as a promising alternative to mammalian gelatin for the formation of materials, yet it has poor rheological performance and usually requires extensive modification. Therefore, the aim of this study is to overcome this problem through coassembling FG with a polyanion polysaccharide fucoidan, thereby exploiting intermolecular forces to strengthen the resultant material. Coassembly was superior in the improvement of the rheological properties of composite hydrogels compared with post gelation mixing. When the fucoidan concentration was at 2 and 4 mg/mL, the storage moduli were 476.7 Pa and 537.7 Pa, respectively, both were about twice that of FG (218.3 Pa), and similar to that of porcine gelatin (479.9 Pa). The microscopic morphology observation revealed denser networks and thicker bundles formed of the FG-fucoidan composite hydrogels, indicating the incorporation of fucoidan may bind single FG nanofibrils together creating thicker bundles during the coassembly process. The increased formation of intermolecular hydrogen bonds induced helical structures and a partial renaturation of the triple helix-like structure of collagen. This provides a facile, easily adapted and scalable approach for the coassembly of non-mammalian gelatins with other polysaccharides.

Ultrasonic-assisted glycosylation with κ-carrageenan on the functional and structural properties of fish gelatin.

Fish gelatin (FG) has multifunctional properties similar to mammalian gelatin (MG), and it has been recognized as the optimal alternative to MG. While its poor surface-active and gelling properties significantly limit its application values, glycosylation has been successfully used to increase surface-active properties of FG, but the influence of ultrasonic-associated glycosylation (UAG) on the gelling and structural characteristics of FG is still rarely reported. This article explores UAG (100-200 W, 0.5-1 h) with κ-carrageenan (κC) on the functional properties (emulsifying, gelling and rheological properties) and structural characteristics of FG. The longer time and higher power of ultrasonics accelerated the glycosylation reaction with an increase in glycosylation degree and browning index values. Compared with original FG, FG-κC mixture and bovine gelatin, UAG-modified FG possessed higher emulsification activity index, emulsion stability index, gel strength, hardness and melting temperature values. Among them, gelatin modified by appropriate ultrasonic conditions (200 W, 0.5 h) had the highest emulsifying and gelling properties. Rheological results showed that UAG contributed to the gelation process of gelatin with advanced gelation time and endowed it with high viscosity. Structural analysis indicated that UAG promoted κC to link with FG by the formation of covalent and hydrogen bonds, restricting more bound and immobilized water in the gels, exhibiting higher gelling properties. This work showed that UAG with κC is a promising method to produce high gelling and emulsifying properties of FG that could replace MG. © 2023 Society of Chemical Industry.

Understanding the Molecular Conformation and Viscoelasticity of Low Sol-Gel Transition Temperature Gelatin Methacryloyl Suspensions.

For biomedical applications, gelatin is usually modified with methacryloyl groups to obtain gelatin methacryloyl (GelMA), which can be crosslinked by a radical reaction induced by low wavelength light to form mechanically stable hydrogels. The potential of GelMA hydrogels for tissue engineering has been well established, however, one of the main disadvantages of mammalian-origin gelatins is that their sol-gel transitions are close to room temperature, resulting in significant variations in viscosity that can be a problem for biofabrication applications. For these applications, cold-water fish-derived gelatins, such as salmon gelatin, are a good alternative due to their lower viscosity, viscoelastic and mechanical properties, as well as lower sol-gel transition temperatures, when compared with mammalian gelatins. However, information regarding GelMA (with special focus on salmon GelMA as a model for cold-water species) molecular conformation and the effect of pH prior to crosslinking, which is key for fabrication purposes since it will determine final hydrogel's structure, remains scarce. The aim of this work is to characterize salmon gelatin (SGel) and salmon methacryloyl gelatin (SGelMA) molecular configuration at two different acidic pHs (3.6 and 4.8) and to compare them to commercial porcine gelatin (PGel) and methacryloyl porcine gelatin (PGelMA), usually used for biomedical applications. Specifically, we evaluated gelatin and GelMA samples' molecular weight, isoelectric point (IEP), their molecular configuration by circular dichroism (CD), and determined their rheological and thermophysical properties. Results showed that functionalization affected gelatin molecular weight and IEP. Additionally, functionalization and pH affected gelatin molecular structure and rheological and thermal properties. Interestingly, the SGel and SGelMA molecular structure was more sensitive to pH changes, showing differences in gelation temperatures and triple helix formation than PGelMA. This work suggests that SGelMA presents high tunability as a biomaterial for biofabrication, highlighting the importance of a proper GelMA molecular configuration characterization prior to hydrogel fabrication.

Application of Poultry Gelatin to Enhance the Physicochemical, Mechanical, and Rheological Properties of Fish Gelatin as Alternative Mammalian Gelatin Films for Food Packaging.

This study aimed to describe the properties of cold water fish gelatin (FG) blended with poultry gelatin (PG) for a production of a sachet containing olive oil. To find a desirable film, the different ratio of FG-PG-based films were characterized in terms of mechanical properties. As the proportion of PG in PG-FG-based increased, the tensile strength and Young's modulus were increased, and the elongation at break and heat seal strength of the films were decreased. The 50-50 film had favorable characteristics to use as a sachet. The amount of acid index and peroxide of the oil stored in the sachets after 14 days showed that there is a significant difference (p < 0.05) between the films. The barrier properties of the films including the water vapor permeability and oxygen permeability of films were increased from 1.21 to 4.95 × 10-11 g m-1 Pa-1 s-1 and 48 to 97 cm3 mµ/m2 d kPa, respectively. Dark, red, yellow, and opaque films were realized with increasing PG. Fourier transform infrared (FTIR) spectra approved a wide peak of approximately 2500 cm-1. The rheological analysis indicated that, by adding PG, viscosity, elastic modulus (G') and loss modulus (G'') were increased significantly (p < 0.05) about 9.5, 9.32 and 18 times, respectively. Therefore, an easy modification of FG with PG will make it suitable for oil sachet packaging applications for the food industry.

An advanced biphasic porous and injectable scaffold displays a fine balance between mechanical strength and remodeling capabilities essential for cartilage regeneration.

An important challenge in tissue engineering is the regeneration of functional articular cartilage (AC). In the field, biomimetic hydrogels are being extensively studied as scaffolds that recapitulate microenvironmental features or as mechanical supports for transplanted cells. New advanced hydrogel formulations based on salmon methacrylate gelatin (sGelMA), a cold-adapted biomaterial, are presented in this work. The psychrophilic nature of this biomaterial provides rheological advantages allowing the fabrication of scaffolds with high concentrations of the biopolymer and high mechanical strength, suitable for formulating injectable hydrogels with high mechanical strength for cartilage regeneration. However, highly intricate cell-laden scaffolds derived from highly concentrated sGelMA solutions could be deleterious for cells and scaffold remodeling. On this account, the current study proposes the use of sGelMA supplemented with a mesophilic sacrificial porogenic component. The cytocompatibility of different sGelMA-based formulations is tested through the encapsulation of osteoarthritic chondrocytes (OACs) and stimulated to synthesize extracellular matrix (ECM) components in vitro and in vivo. The sGelMA-derived scaffolds reach high levels of stiffness, and the inclusion of porogens impacts positively the scaffold degradability and molecular diffusion, improved fitness of OACs, increased the expression of cartilage-related genes, increased glycosaminoglycan (GAG) synthesis, and improved remodeling toward cartilage-like tissues. Altogether, these data support the use of sGelMA solutions in combination with mammalian solid gelatin beads for highly injectable formulations for cartilage regeneration, strengthening the importance of the balance between mechanical properties and remodeling capabilities.

Physical modification on gelation of fish gelatin by incorporating Nicandra physalodes (Linn.) Gaertn. pectin: Effect of monovalent and divalent cation ions

Fish gelatin (FG) is more appreciated by religious people than mammalian gelatin. However, the relatively poor gelling capacity of FG limits its applicability in the food industry. In this study, Nicandra physalodes (Linn.) Gaertn. pectin (NPGP) was incorporated into FG to modify its gelling capacity, and the effect of monovalent (Na+) and divalent cations (Ca2+) on the gelation process of FG/NPGP mixtures was investigated. At a fixed concentration of FG (5.0 %, w/v) and NPGP (0.2 %, w/v), mixing the two polymers at natural pH condition (pH ≈ 6.0) led to significant intermolecular electrostatic association, which increased the gel hardness by producing an FG-dominant network augmented by NPGP molecules. When Na+ and Ca2+ were introduced, the electrostatic association was greatly decreased, which further weakened the gels. At low Ca2+ concentration (5 mM), however, FG, NPGP and Ca2+ formed tertiary complexes, which provided additional crosslinks and thus increased the gel strength.

The impact of sugar alcohols and sucrose on the physical properties, long-term storage stability, and processability of fish gelatin gels

Fish gelatin is becoming a popular alternative to mammalian gelatins due to religious restrictions, cultural preferences, ecological, and ethical concerns. Warm water fish gelatins (WWFG), as opposed to gelatins from cold water fish species, have more similar physical properties, and hence represent an alternative, to mammalian gelatins albeit a lower sol/gel transition temperature and gel strength. In warm climates, WWFG gels may therefore exhibit reduced storage stability at temperatures above this transition temperature because of e.g., a more pronounced acid hydrolysis of the sol fraction. To improve the long-term storage stability of WWFG, gels were prepared with two different sugar alcohols, sorbitol and xylitol, and a non-reducing sugar, sucrose. The change in the sol/gel transition temperature, gelling and melting kinetics, and gel strength of the gels were analyzed using small amplitude oscillatory shear measurements. Short-term and long-term storage stability tests at ambient temperature, 30 °C and 40 °C indicated improved stability of gels with co-solutes without significant differences between the type of sugar alcohol or sucrose. The stability of the gels increased with increasing concentrations of sugar alcohols. The degree of hydrolysis of the gelatin in the gels were investigated using SEC-MALS analyses which supported the bulk rheology stability results. Using sucrose led to browning and high viscosity, which may pose challenges regarding the processability and industrial applications.