황다랑어의 비늘로부터 콜라겐의 추출 및 물리화학적 특성 해석

Abstract

Scales of yellowfin tuna (Thunnus albacares) was studied to investigate the optimum condition of collagen extraction by using surface response methodology. The four independent variables of concentration and treatment time for both alkali and enzyme treatments were used to predict a model equation for the collagen yield. The determinant coefficient (R²) for the equation was 0.9056. The values of the independent variables for the maximum yield was 0.32 N NaOH concentration, 16.38hrs alkali treatment time, 0.18% enzyme concentration, and 31.02hrs enzyme treatment time. In the physicochemical properties of tuna scale collagen, SDS-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 FT-IR measurement was shown in the peaks of 3414 cm^(-1), 1645 cm^(-1), 1553 cm^(-1) and 1247 cm^(-1), respectively. The amount of imino acids for tuna scale collagen was 18.97% and the collagen denaturation temperature was 33℃. The collagen solubility on NaCl concentration was decreased until 4% NaCl (w/v) and the collagen solubility on pH was high at pH 2-4 and sharply decreased from pH 4 to pH 7. Viscosity of the collagen solution was continuously decreased until 30℃ and its decreasing rate was reduced in the temperature range of 35-50°C.