• Korean Journal of Fisheries and Aquatic Sciences
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• v.31 no.6
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• pp.829-834
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• 1998

It is well known that the native conformation of many proteins can be stabilized by carbohydrates or polyalcohols. However, the mechanism of the stabilization still remains unclear. In the present studies, to characterize the cryoprotective mechanism of corn starch enzyme hydrolysates on fish protin, solubility of hydrolysates, thermal behavior of hydrolysates and actomyosin solution, and enzyme kinetics in frozen system were investigated. The solubility of the hydrolysates increased with the increase in D.E. value. The $T_g^{'}$ of the hydrolysates were linearly correlated with D.E. value and the T-g value of the hydrolysates (D.E. 5,10,15,20) were reported to be $-7.2^{\circ}C\;-8.8^{\circ}C\;-11.9^{\circ}C$, and $-14.3^{\circ}C$, respectively. The results of enzyme experiments showed that the higher the D.E. value, the higher was the rate of reaction in frozen storage ($-12^{\circ}C$). It is found to support the cryostabilization mechanism that the hydrolysats act to enmesh the protein in a glass state where all deteriorative processes are greatly slowed down.