Enzyme Hydrolysis Preparation Model of Collagen-derived ACE Inhibitory Peptides Based on Quadratic General Rotation Design
Fish-derived collagen was hydrolyzed by protamex R protease and measured by the degree of hydrol-ysis. The hydrolysis model of peptides from fish-derived collagen was established through quadratic general ro-tation design followed single factor experiment, subsequently ACE inhibitory activity and secondary structure of fish collagen-derived peptides was measured. The results showed that the equation for the optimal regression e-quation had a maximal value according to regression coefficient test, regression equation, and the lack of fit test. The optimal details of enzymatic hydrolysis was followed:substrate concentration 11.8%, enzymatic hy-drolysis pH value 8.7, the amount of enzyme 5.4%and hydrolysis temperature 53.6℃, and hydrolysis degree of fish-derived collagen was 16.6 % in one hour. In vitro ACE inhibitory activity of bioactive peptides from fish-derived collagen was performed by high performance liquid chromatography, and the value of activity a-gainst ACE was 45 %. In addition, secondary structure of fish collagen-derived ACE inhibitory peptide was random coil.
NETL
NSTL
万方数据
维普
