Study on Stablization and Inhibitory Mechanism of Antihypertensive Peptide Derived from Bovine Casein

Abstract

Abstract: In vitro simulation experiment and peptide analysis showed that angiotensin converfing enzyme (ACE) inhibitory activity still contains 94% of initiall activity after antihypertensive peptide digestion with pepsin and trypsin.This also showed that these peptides survive the degradation by gastronintestinal proteinases and peptdases.After antihypertensive peptide reaction with angiotensin converting enzyme, there are very little changes in the ACE inhibitory activity and peptide chromatography. This proved that the antipertensive peptide is the true inhibitor. Antihypertensive inhibitory mechanism was studied by the enzyme inhibition dynamics.This also showed that the antipertensive peptide is of non-competition inhibition according to Lineweaver-Burk equation.

Key words: antihypertensive peptide, stablization, inhibitory mechanism

JIANG Zhan-Mei, WU Gang, LIU Li-Bo, TIAN Bo, HUO Gui-Cheng. Study on Stablization and Inhibitory Mechanism of Antihypertensive Peptide Derived from Bovine Casein[J]. FOOD SCIENCE, 2008, 29(4): 249-252 https://doi.org/

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Study on Stablization and Inhibitory Mechanism of Antihypertensive Peptide Derived from Bovine Casein

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