• KSBB Journal
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• v.15 no.6
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• pp.635-643
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• 2000

To compare the antioxidative activities of fish skin and bovine skin gelatin hydrolysate, gelatin hydrolysates from Alaska pollack and bovine skin were prepared by various enzymatic hydrolysis methods (1st step, Alcalase; 2nd step, pronase E; 3rd step, collagenase) using a continuous three-step membrane reactor. The molecular weight distributions of the 1st, 2nd and 3rd step hydrolysates were 7∼10 kDa, 2∼5 kDa and 0.7∼0.9 kDa, respectively. The antioxidative activity of fish skin gelatin hydrolysate was stronger than that of bovine skin gelatin hydrolysate, and in particular, both of 2nd step hydrolysates showed more antioxidative activity than hydrolysates of any other step. The optimum antioxidative activity concentration of the 2nd step hydeolysates of fish and boving skin were 1% (w/w) in a linoleic acid water-alcohol emulsion. In cultured cells exposed to t-butyl hydroperoxide (t-BHP), the 2nd step hydrolysate of fish skin gelatin delayed cell death most. These results suggest that the antioxidative activity of fish skin gelatin hydrolysate is higher than that of bovine skin gelatin hydrolysate because of their different amino acid contents.

• Korean Journal of Food Science and Technology
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• v.26 no.6
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• pp.683-689
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• 1994

With a view to utilizing effectively fish skin wastes from marine manufactory, a gelatin solution extracted from yellowfin sole skin was fractionated by precipitation with ethanol, and then the functional and physico-chemical properties for the fractionated gelatin were determined. Ethanol was added up to 50% of ethanol content to a gelatin solution extracted from yellowfin sole skin, then the mixture was left to stand at $0^{\circ}C$ for 12 hours. Finally, the precipitates were dried by hot-air ($40^{\circ}C$). The gel strength and melting point of a 10% gel of gelatin prepared from yellowfin sole skin by precipitation with ethanol has 322.4g and $23.3^{\circ}C$, respectively. The physico-chemical properties of the ethanol treated fish skin gelatin were superior to those of fish skin gelatin prepared without ethanol treatment. Besides, the functional properties of the ethanol treated gelatin were lower in solubility and higher in water holding capacity, oil binding capacity, emulsifying activity, emulsifying stability, foam expansion and foam stability than those of pork skin gelatin sold on market as well as gelatin prepared without ethanol treatment. It may be concluded, from these results, that the fish skin gelatin prepared by precipitation with ethanol can be effectively utilized as a human food by improving the functional properties.

• Applied Biological Chemistry
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• v.38 no.2
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• pp.129-134
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• 1995

With a view to utilizing effectively fish skin wasted from marine manufactory, an extracted dover sole skin gelatin was fractionated by further ethanol fractional precipitation method, and then the functional and physicochemical properties for the modified gelatin were determined. Ethanol was added to the concentration of 30% in an extracted dover sole skin gelatin solution, and then the mixture was left to stand at $0^{\circ}C$ for 12 hours. Finally, the precipitates were dried by hot-air$(40^{\circ}C)$ blast. The yellowfin sole skin gelatin prepared by further ethanol fractional precipitation has 223.0 g in gel strength, $17.7^{\circ}C$ in the melting point, and $12.0^{\circ}C$ in the gelling point. The physicochemical properties of the ethanol treated fish skin gelatin were superior to those of fish skin gelatin prepared without ethanol adding, whereas inferior to those of animal skin gelatin. The functional properties of the ethanol treated fish skin gelatin were superior to those of fish skin gelatin prepared without ethanol adding, and were more similar to animal skin gelatin. It may be concluded, from these results, that the dover sole skin gelatin prepared by further ethanol fractional precipitation can be effectively utilized as a human food by improving the functional properties.

• 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.

• Applied Chemistry for Engineering
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• v.5 no.3
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• pp.547-559
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• 1994

To effectively utilize fish skin wastes from marine manufactory, the optimal extraction conditions to prepare gelatin from fish skins of Alaska pollack, cod and yellowfin sole were investigated. In addition, the physical properties of the fish skin gelatins prepared under the optimal extraction conditions were compared with the commercial animal skin gelatin. The conditions for extraction of gelatins from fish skins were as follows ; The skins were limed with 1.0~1.5%(w/v) calcium hydroxide solution. The fish skin gelatins were extracted with 6~7 volumes of water(pH 6.0~7.0) for 5hrs at $40{\sim}50^{\circ}C$, and the yield of Alaska pollack skin gelatin extracted under the above conditions was higher than those of cod and yellowfin sole skins. The heavy metal contents, jelly strength and electric conductivities of fish skin gelatins were lower than those of a commercial gelatin(bovine skin), but the viscosity and isoelectric point were higher. The amount of amino acid in fish skin, such as gelatin, glutamic acid, serine, threonine, methionine and cysteine, were higher than those in pig and ox skin. However, the contents of hydroxyproline and proline were lower.

• Applied Biological Chemistry
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• v.39 no.4
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• pp.282-286
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• 1996

To effectively utilize fish skin gelatin as a material for quality improvement in surimi gel from fish with a red muscle, conger eel skin gelatin was modified with succinic anhydride, and funtional properties such as emulsifying activity and emulsifying stability were determined. The degree of chemical modification incresed up to 0.3 g of succinic anhydride/g of gelatin, above this adding ratio a nearly constant value was reached. The maximum amount of modification was about 90%. The emulsifying activity and emulsifying stability of gelatin gradually increased up to 89.8% of succinylation extent, little changed above of succinylation extent. The other functional properties as solubility, water holding capacity, foam expansion and foam stability were improved following succinylation with 0.3 g of succinic anhydride/g of gelatin. Amino acid composition of succinylated gelatin was similar to that of unmodified gelatin. Heavy metal contents such as cadmium, lead, copper and zinc of succinylated gelatin were lower than those of unmodified gelatin.

• Journal of Life Science
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• v.6 no.1
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• pp.14-26
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• 1996

In order to effectively utilize fish(Cod, Gadus macrocephalus) bone obtained as fish waste in fish manufactory, the preparation of the fish bone gelatin were attempted by heat extracting method from collagen protein contained in the fish bone. The methods of two kinds pretreatments (the B-type by alkali pretreatment and the E-type by enzyme pretreatment) for fish bone and the optimal extraction conditions to prepare gelatin from pretreated fish bone were investigated. Physical properties and functionalities of the two type fish bone gelatins obtained were compared with the commercial gelatin and the fish skin gelatin. The optimal extraction conditions of the B-type and the E-type gelatins were 5 folds of added water with material(w/w), pH 5.0, 3 hrs of extraction time and 60$\circ$C of extraction temperature. The yield of the B-type and the E-type gelatins were 32.6% and 28.1 %, respectively. The B-type gelatin was superior to the E-type un all physical properties. Molecular weight of the B-type was larger than that of the E-type due to its pretreatment method. Among the composition of amino acids, the amino acids such as glycine, alanine, glutamic acid and imino acids(proline and hydroxyproline) were responsible for 68$\sim$70% of the total amino acids. Functionalities of the fish bone gelatin were almost similar to commercial gelatin.

• Fisheries and Aquatic Sciences
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• v.14 no.1
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• pp.1-10
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• 2011

This study was conducted to obtain hydrolysates with potent antioxidative activity from rockfish skin gelatin. Gelatin was extracted under high temperature/high pressure using a two-step enzymatic hydrolysis with commercial enzymes such as Alcalase, Flavourzyme, Neutrase, and Protamex. The second rockfish-skin gelatin hydrolysate (SRSGH) was prepared by further incubating the first gelatin hydrolysate (FRSGH), which had been hydrolyzed with Alcalase for 1-h (FRSGH-A1), with Flavourzyme for 2-h (SRSGH-F2). The second gelatin hydrolysate showed higher antioxidative activity of 3.72 as measured by a Metrohm Rancimat and superior angiotensin I-converting enzyme (ACE) inhibiting activity of 0.82 mg/mL. Compared with the gelatin, the relative proportion in SRSGH-F2 was markedly decreased in the 100-kDa peak, whereas it was increased in that less than 100-kDa. The amino acid composition of SRSGH-F2 was rich in glycine (25.9%), proline (10.8%), alanine (9.1%), and glutamic acid (9.1%). In contrast, it was poor in cystine (not detected), methionine (1.6%), tyrosine (0.4%), hydroxylysine (0.9%), and histidine (0.9%). In recent years, demand for natural functional foods has been increasing, and SRSGH-F2 can be used as a functional food ingredient in the food industries. However, further detailed studies on SRSGH-F2 with regard to its antioxidant activity in vivo and the various antioxidant mechanisms are needed.

• Applied Biological Chemistry
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• v.36 no.6
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• pp.440-448
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• 1993

To utilize effectively fish skin wasted from fish processing, a dover sole skin gelatin was prepared by alkaline extraction method and the physico-chemical properties were examined. Conditions for the suitable pretreatment, extraction and decolorization for gelatin preparation from dover sole skin are as follows: the skin is limed with 1.0% calcium hydroxide solution at $5^{\circ}C$ for 4 days, washed thoroughly for 2 days with tap water, extracted with 5 volumes of water $(pH\;5.0{\sim}7.0)$ to dehydrated skin for 3 hours at $50^{\circ}C$, and then bleached with 3% activated carbon. Though dover sole skin gelatin was prepared under above conditions, physico-chemical property values such the melting point and gelling point of that were lower than those of yellowfin sole skin gelatin as well as the commercial pork skin gelatin. Therefore, the purified dover sole skin gelatin requires a suitable modification operation for better quality gelatin manufacture.

• Applied Biological Chemistry
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• v.37 no.2
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• pp.85-93
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• 1994

The fish skin gelatin hydrolysates were produced using a continuous two-stage membrane (MWCO 10,000, MWCO 5,000) reactor, and molecular weights, amino acids and functional properties of the hydrolysates were investigated. The major molecular weights distribution of the major fractions were $8{\sim}10\;KDa$ and $4.5{\sim}6.5\;KDa$ in the 1st-step hydrolysates, $2{\sim}6\;KDa$ and $0.5{\sim}2\;KDa$ in the 2nd-step hydrolysates. Among the amino acids in the hydrolysates, glycine, proline, serine, alanine, hydroxyproline, glutamic acid and aspartic acid having sweet taste were responsible for $68{\sim}72%$ of the total amino acids. But valine, methionine, isoleucine, leucine, phenylalanine and histidine having a bitter taste were only $23{\sim}25%$ Taste evaluations show that the gelatin hydrolysates have a brothy and sweet taste, 2nd-step hydrolysate have more a favorable taste than 1st-step hydrolysate. The hydrolysates were completely soluble and clear over the entire pH range. Moisture sorption at intermediate water activities of the 2nd-step hydrolysate was much higher than the unmodified fish skin gelatin, but foaming and emulsification properties were poor. Buffer capacity of the 2nd-step hydrolysate was higher than the fish skin gelatin and 1st-step hydrolysate, while viscosities of the hydrolysates were lower than the fish skin gelatin.