抄録
In this paper, the detection of type I collagen degradation during the softening phenomenon of yellowtail muscle, was examined. Acid soluble collagen was isolated from dorsal ordinary muscle at death and after 24-h chilled storage. In the abundant ratio of subunit components, an increase in β12 chain (5.4 points) and a decrease in components with molecular weights larger than γ chain (7.0 points) after 24-h chilled storage, was found. Type I collagen was detected in the alkali-soluble fraction by SDS-PAGE. Its amount calculated from hydroxyproline contents in alkali-soluble fraction was increased from 0.097 mg/g muscle to 0.155 mg/g muscle during 24-h storage. The increased alkali-soluble collagen (0.058 mg/g muscle) was about 1.4% of whole collagen. These results suggest that a slight decomposition of type I collagen of yellowtail muscle may occur and subsequently becomes alkali-soluble corresponding to postmortem softening.
