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Physicochemical Properties of Gelatin from Jellyfish Rhopilema hispidum
조승목,안주련,구자성,김선봉 한국수산과학회 2014 Fisheries and Aquatic Sciences Vol.17 No.3
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°C, and melting point of 22.3°C. The gelatin was composed of α1-chain, α2-chain, β-chain, and γ-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.
한유나,우진욱,정철균,조승목,이양봉,김선봉,안주련 한국수산과학회 2010 Fisheries and Aquatic Sciences Vol.13 No.2
This study was conducted to investigate the optimal conditions of collagen extraction from scales of yellowfin tuna (Thunnus albacares) using surface response methodology. Four independent variables of NaOH concentration and pretreatment fime in alkali pretreatment and enzyme concentration and treatment time in enzyme hydrolysis were used to predict a model equation for the collagen yield. The determinant coefficient (R2) for the equation was 0.906. The values of the independent variables for the maximum yield were 0.32 N NaOH, 16.38 h alkali pretreatment time, 0.18% enzyme concentration, and 31.02 h enzyme treatment time. In the physicochemical properties of tuna scale collagen, sodium dodecyl sulfate-polyacrylamide gel electrophoresis of tuna scale collagen showed the same migration distances as that of calf skin collagen. The amide A, I, II, and III regions of tuna scale collagen in Fourier transform infrared measurements were shown in the peaks of 3,414 cm-1, 1,645 cm-1, 1,553 cm-1, and 1,247 cm-1, respectively. The amount of imino acids in tuna scale collagen was 18.97% and the collagen denaturation temperature was 33°C. The collagen solubility as a function of NaCl concentration decreased to 4% NaCl (w/v) and the collagen solubility as a function of pH was high at pH 2-4 and sharply decreased from pH 4 to pH 7. Viscosity of the collagen solution decreased continuously until 30°C and this decreasing rate slowed in the temperature range of 35-50°C.