In order to reveal whether the difference in the blood pressure regulation function of animal and plant-derived proteins is caused by the angiotensin conversion enzyme (ACE) inhibitory activity of protein peptides, animal and plant proteins inhibited the ACE activity of protein peptides after digestion in vitro. research. The pepsin-trypsin two-step digestion method is used to hydrolyze plant proteins (rice, oats, soybeans, peas), red meat proteins (pork, beef) and white meat proteins (chicken). The degree of hydrolysis, molecular mass distribution, amino acid composition and ACE inhibition rate of the obtained protein peptides were determined. The results showed that as the degree of protein hydrolysis increased and the molecular weight decreased, the ACE activity inhibition rates of the three types of protein digestion products increased accordingly. Among them, the ACE inhibition rate of plant protein digestion products is the highest (60.41%), and red meat protein is the lowest (40.13%). The amino acid composition of protein digestion products was analyzed. The results showed that the hydrophobic amino acid content of plant protein and white meat protein digestion products was significantly higher than that of red meat protein. The higher the hydrophobic amino acid content of the digestion products in the 3 types of proteins, the higher the ACE inhibitory activity, indicating that the high hydrophobic amino acid content may be one of the main reasons why plant protein peptides have high ACE inhibitory activity

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Original research was done by Tong Litao, Zhou Sumei, Zhou Xianrong, Liang Tingting, Wang Lili, Pu Huayin, Ju Zhiyuan, Huang Junrong

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