Preparation of Angiotensin-I Converting Enzyme Inhibition Peptides from Porcine Hemoglobin
Yongkang Luo
Abstract
Yongkang Luo
Abstract
This experiment adopted six kinds of commercial protease Alcalase 2.4L, trypsin, pepsin, flavourzyme, nuetrase AS1398 and papain to hydrolyze porcine hemoglobin in optimum reaction conditions for 12 hours respectively, and the hydrolysates were assayed for the inhibitory activity of angiotensin-I converting enzyme(ACE) and the protein hydrolysis degree.The results showed that the ACE inhibitory activity of pepsin-derived hydrolysates was highest in all the proteases.The condition of enzymatic hydrolysis of pepsin was:substrate concentration was 5%, enzyme/substrate ratio was 3%, temperature was 37℃, pH 2.0, and in the 4th hour the inhibitory activity of ACE reached 81.10% and the degree of hydrolysis was 6.64%.
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This experiment adopted six kinds of commercial protease Alcalase 2.4L, trypsin, pepsin, flavourzyme, nuetrase AS1398 and papain to hydrolyze porcine hemoglobin in optimum reaction conditions for 12 hours respectively, and the hydrolysates were assayed for the inhibitory activity of angiotensin-I converting enzyme(ACE) and the protein hydrolysis degree.The results showed that the ACE inhibitory activity of pepsin-derived hydrolysates was highest in all the proteases.The condition of enzymatic hydrolysis of pepsin was:substrate concentration was 5%, enzyme/substrate ratio was 3%, temperature was 37℃, pH 2.0, and in the 4th hour the inhibitory activity of ACE reached 81.10% and the degree of hydrolysis was 6.64%.
Key concepts: Papain, Pepsin, Hydrolysate, Chemistry, Trypsin, Hydrolysis, Protease, Enzyme