期刊
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 51, 期 19, 页码 5680-5687出版社
AMER CHEMICAL SOC
DOI: 10.1021/jf034097v
关键词
ACE inhibitory peptides; pea protein; whey protein; response surface methodology
Gastrointestinal digestion is of major importance in the bioavailability of angiotensin I converting enzyme (ACE) inhibitory peptides, bioactive peptides with possible anti hypertensive effects. In this study, the conditions of in vitro gastrointestinal digestion leading to the formation and degradation of ACE inhibitory peptides were investigated for pea and whey protein. In batch experiments, the digestion simulating the physiological conditions sufficed to achieve the highest ACE inhibitory activity, with IC50 values of 0.076 mg/mL for pea and 0.048 mg/mL for whey protein. The degree of proteolysis did not correlate with the ACE inhibitory activity and was always higher for pea than whey. In a semicontinuous model of gastrointestinal digestion, response surface methodology studied the influence of temperature and incubation time in both the stomach and small intestine phases on the ACE inhibitory activity and degree of proteolysis. For pea protein, a linear model for the degree of proteolysis and a quadratic model for the ACE inhibitory activity could be constituted. Within the model, a maximal degree of proteolysis was observed at the highest temperature and the longest incubation time in the small intestine phase, while maximal ACE inhibitory activity was obtained at the longest incubation times in the stomach and small intestine phase. These results show that ACE inhibitory activity of pea and whey hydrolysates can be controlled by the conditions of in vitro gastrointestinal digestion.
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