• Korean Journal of Fisheries and Aquatic Sciences
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• v.41 no.6
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• pp.419-426
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• 2008

Physicochemical characteristics of gelatin extracted from abdominal skin of yellowfin tuna (Thunnus albacares), were investigated by comparing its proximate composition, pH, amino acid composition, viscoelastic properties, gel strength and SDS-PAGE patterns, with those of bovine and porcine gelatins. The effects of gelatin concentration, maturation time, heat and freeze treatments on the gel strength of yellowfin tuna abdominal skin gelatin were studied. Amounts of $\alpha$-chains, $\beta$- and $\gamma$-components of yellowfin tuna abdominal skin gelatin were higher than those of the two mammailan gelatins. Yellowfin tuna abdominal skin gelatin had the lowest imino acids (proline and hydroxyproline) content, which was consistent with that of other fishes. However, yellowfin tuna abdominal skin gelatin was highest in glycine, alanine, and lysine. The gel strengths of all gelatins were proportional to the concentration of gelatin, but yellowfin tuna abdominal skin gelatin exhibited the greatest gel strength at each concentration. Yellowfin tuna abdominal skin gelatin required a longer maturation time than the two mammalian gelatins to form a firm gel. Higher heating temperature decreased the gel strength of yellow fin tuna abdominal skin gelatin more than in the two mammalian gelatins. Freezing decreased the gel strength of bovine gelatin only slightly, but longer freezing times resulted in greater reductions in gel strength in the yellowfin tuna abdominal skin and porcine gelatins.

• Fisheries and Aquatic Sciences
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• v.17 no.3
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• pp.299-304
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• 2014

The objective of this study was to elucidate the physicochemical characteristics of gelatin extracted from jellyfish Rhopilema hispidum. We investigated the proximate composition, amino acids, gel strength, gelling/melting points, dynamic viscoelastic properties, and viscosity of jellyfish gelatin. Jellyfish gelatin contained 12.2% moisture, 1.5% lipid, 2.1% ash, and 84.8% protein. Glycine, hydroxyproline, proline, and alanine were the predominant amino acids. The gelatin showed a gel strength of 31.2 kPa, a gelling point of $18.0^{\circ}C$, and melting point of $22.3^{\circ}C$. The gelatin was composed of ${\alpha}_1$-chain, ${\alpha}_2$-chain, ${\beta}$-chain, and ${\gamma}$-chain. During cooling and heating process, jellyfish gelatin showed lower elastic modulus (G') and loss modulus (G") values than mammalian gelatin. Jellyfish gelatin did not show superior rheological properties to mammalian gelatin, like other fish gelatin; however, it can be used in various food and cosmetic products not requiring high gel strength.

• Asian-Australasian Journal of Animal Sciences
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• v.29 no.6
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• pp.845-854
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• 2016

Characteristics and properties of gelatin from goat skin pretreated with NaOH solutions (0.50 and 0.75 M) for various times (1 to 4 days) were investigated. All gelatins contained ${\alpha}$-chains as the predominant component, followed by ${\beta}$-chain. Gelling and melting temperatures of those gelatins were $23.02^{\circ}C$ to $24.16^{\circ}C$ and $33.07^{\circ}C$ to $34.51^{\circ}C$, respectively. Gel strength of gelatins increased as NaOH concentration and pretreatment time increased (p<0.05). Pretreatment for a longer time yielded gelatin with a decrease in $L^*$-value but an increase in $b^*$-value. Pretreatment of goat skin using 0.75 M NaOH for 2 days rendered the highest yield (15.95%, wet weight basis) as well as high gel strength (222.42 g), which was higher than bovine gelatin (199.15 g). Gelatin obtained had the imino acid content of 226 residues/1,000 residues and the gelatin gel had a fine and ordered structure. Therefore, goat skin gelatin could be used as a potential replacer of commercial gelatin.

• Food Science of Animal Resources
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• v.39 no.4
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• pp.576-584
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• 2019

This study was performed to evaluate the physicochemical properties of myofibrillar protein (MP) gels containing pork skin gelatin at different salt concentrations. MP gels were prepared to the different salt levels (0.15, 0.30, and 0.45 M) with or without 1.0% of pork skin gelatin. Cooking yield (CY), gel strength, shear stress were measured to determine the physical properties, and SDS-polyacrylamide gel electrophoresis, scanning electron microscopy, fourier transform infrared spectroscopy, sulfhydryl group and protein surface hydrophobicity was performed to figure out the structural changes among the proteins. The addition of gelatin into MP increased CYs and shear stress. MP at 0.45 M salt level had the highest CY and shear stress, as compared to MPs at lower salt concentrations. As the salt concentration of MP gels increased, the microstructure became the compact and wet structures, and decreased the amount of ${\alpha}-helix$/unordered structures and ${\beta}-sheet$. MP with gelatin showed a decreased amount of ${\alpha}-helix$/unordered structures and ${\beta}-sheet$ compared to MP without gelatin. The addition of gelatin to MP did not affect the sulfhydryl group, but the sulfhydryl group decreased as increased salt levels. MP mixtures containing gelatin showed a higher hydrophobicity value than those without gelatin, regardless of salt concentration. Based on these results, the addition of gelatin increased viscosity of raw meat batter and CY of MP gels for the application to low salt meat products.

• Food Science of Animal Resources
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• v.39 no.2
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• pp.229-239
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• 2019

The objectives of this study were to determine the interaction between porcine myofibrillar proteins and various gelatins (bovine hide, porcine skin, fish skin, and duck skin gelatins) and their impacts on gel properties of porcine myofibrillar proteins. Porcine myofibrillar protein was isolated from pork loin muscle (M. longissimus dorsi thoracis et lumborum). Control was prepared with only myofibrillar protein (60 mg/mL), and gelatin treatments were formulated with myofibrillar protein and each gelatin (9:1) at the same protein concentration. The myofibrillar protein-gelatin mixtures were heated from $10^{\circ}C$ to $75^{\circ}C$ ($2^{\circ}C/min$). Little to no impacts of gelatin addition on pH value and color characteristics of heat-induced myofibrillar protein gels were observed (p>0.05). The addition of gelatin slightly decreased cooking yield of heat-induced myofibrillar protein gels, but the gels showed lower centrifugal weight loss compared to control (p<0.05). The addition of gelatin significantly decreased hardness, cohesiveness, gumminess, and chewiness of heat-induced myofibrillar gels. Further, sodium dodecyl poly-acrylamide gel electrophoresis (SDS-PAGE) showed no interaction between myofibrillar proteins and gelatin under non-thermal conditions. Only a slight change in the endothermic peak (probably myosin) of myofibrillar protein-gelatin mixtures was found. The results of this study show that the addition of gelatin attenuated the water-holding capacity and textural properties of heat-induced myofibrillar protein gel. Thus, it could be suggested that well-known positive impacts of gelatin on quality characteristics of processed meat products may be largely affected by the functional properties of gelatin per se, rather than its interaction with myofibrillar proteins.

• KSBB Journal
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• v.10 no.2
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• pp.166-169
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• 1995

Spores of Trichoderma harzianum TCC 52445 for control of Rhlzocronia stem canker on potato were immobilized in various natural matrix, and germination rate and some rheological properties of the spore-matrix complex were Investigated. Germination rate of gelatin gel-spore complex and potato starch gel-spore complex were 2.8% and 2.9%, respectively, but hardness and cohesiveness of the gelstin gel-spoke complex were better than those of potato starch-spore complex. The hardness and cohesiveness were increased when the spores were immobilized in hybrid gelatin gel made by mixing several different types of natural matrix, but decreased their germination rate. Addition of corn steep liquor (1%) as spore nutrient in gelatin gel-spore complex was helpful for increasing the germination rate.

• Polymer(Korea)
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• v.30 no.6
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• pp.563-567
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• 2006

Poly(vinyl alcohol) (PVA) and gelatin (GEL) blend membranes were prepared by solution casting method under a high electric field. SEM observation of the membrane showed that gelatin rich domains were elongated and oriented to the direction of the applied electric field in PVA matrix. This can be attributed to the electrostatic emulsifying effects due to a reduction in interfacial tension. In addition, it was observed through WAXD and swelling measurements that the degree of crystallinity of membranes increased with applied electric field strength. This may be interpreted to be caused by the orientation effect of GEL domains in the blend membrane, and the self-annealing effect due to some heat generated from high electric field during casting.

• Korean Journal of Food Science and Technology
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• v.34 no.5
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• pp.911-915
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• 2002

This study was conducted to determine optimum levels of flavoring materials for gel-type dessert using chicken feet gelatin. Effects of levels of sucrose, citric acid and strawberry flavoring on the consumer acceptability of gelatin desserts were examined and the optimum levels were determined using response surface methodology. The optimum levels of flavoring materials determined for gelatin dessert containing 2% gelatin powder, were 19, 0.50, and 0.35% for sucrose, citric acid, and strawberry flavoring, respectively.

• Korean Journal of Food Science and Technology
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• v.27 no.4
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• pp.483-486
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• 1995

With a view to increase utility of ethanol fractionated fish skin gelatin as a food source, the effect of gelation condition on physical properties of the gelatin was investigated. The physical properties of gelatins treated with or without ethanol were improved with a concentration of gelatin increased. The properties such as gel strength, melting point and gelling point of 10% gelatin sol or gel were reached to maximum at pH 6.0 in ethanol treated gelatin and pH 5.0 in non treated one, respectively. Gel strength and melting point of both gelatin gels chilled for long time at low temperature were superior to those of both gelatin gels chilled for short time at high temperature. Gel strength, melting point and gelling point of ethanol treated gelatin gel or sol prepared under optimized gelation conditioning were superior to those of non treated one.

• Food Science of Animal Resources
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• v.43 no.1
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• pp.61-72
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• 2023

The practical use of Korean native black goat skin as a source of gelatin extraction is limited. The objective of this study was to optimize the extraction temperature and time of gelatin from Korean native black goat skin, and to compare the quality characteristics of goat skin gelatin and other commercial gelatin products. Response surface methodology was applied to optimize the extraction temperature and time of gelatin obtained from native Korean black goat skin. The effects of temperature (50℃-70℃) and time (2-4 h) on extraction yield and gel strength were investigated using a face-centered central composite design with 13 experiments. Gelatin extraction from Korean native black goat skin was prepared through the serial processes of alkali pre-treatment, bleaching, neutralization, hot-water extraction, and freeze-drying. Using the optimization plot of Minitab software, the optimized conditions for extracting temperature and time of goat skin gelatin were 59.49℃ and 3.03 h, and the optimized values of extraction yield and gel strength were 12.52% and 263.37 g, respectively. Based on a quality comparison of goat skin gelatin with commercial gelatin, the pH value of gelatin extracted from Korean native black goat skin was 5.57. The color of gelatin extracted from Korean native black goat skin was darker than that of commercial gelatin (p<0.05). Higher emulsifying properties and gel strength of goat skin gelatin were observed when compared to those of commercial gelatin (p<0.05). Therefore, the results of this study indicate that Korean native black goat skin may be a valuable source for gelatin extraction.