Keywords

Alkaline Protease, Casein Hydrolyzate, Protein-Like Reaction, Ace Inhibitory Activity

Abstract

Alkaline protease was used to hydrolyze casein, and a casein hydrolyzate with a degree of hydrolysis of 10.9% and an ic50 value of 52.6 ¦Ìg/ml was prepared. Response surface methodology was used to optimize the modification conditions of the proteinoid reaction catalyzed by alkaline protease. When the modification reaction time is fixed at 6 hours, the appropriate conditions are enzyme addition amount 3.1ku/gpro, substrate mass concentration 50g/100ml, and reaction temperature 25¡ãC. Nine modified products with different degrees of modification were prepared. The results showed that the ace inhibitory activity of the modified products was increased, and the ic50 of the modified product with the highest activity was reduced to 14.9 ¦Ìg/ml. After centrifugation and fractionation of the modified product, the ACE inhibitory activity of the supernatant and precipitated parts were lower and higher than the modified product respectively, indicating that the precipitated part was the main reason for improving the ACE inhibitory activity; tricine-sds-page electrophoresis analysis showed that the modified product and peptide molecules with larger molecular weight are generated in the precipitated part; further enzymatic hydrolysis treatment of the modified product, supernatant part, and precipitated part shows that enzymatic hydrolysis will cause their ace inhibitory activity to decrease, but it is still higher than the original casein Protein hydrolysates.

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Original research done by Sun Hui, Zhao Xinhuai

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