Inhibitory Effects of Almond Protein Hydrolysate against AngiotensinI-converting Enzyme
Miao Li-li
Abstract
Miao Li-li
Abstract
Almond protein was respectively hydrolyzed with Protamex, Alcalase, Neutrase, Flavourzyme, Proleather FG-F and Papain, and then the angiotensin I-converting enzyme (ACE) inhibitories activities of obtained hydrolysates were detected by high performance liquid chromatography (HPLC). With the degree of hydrolysis (DH) and the ACE-inhibitory activity of hydrolysate as evaluation indexes, the hydrolysis course and the digestion stability in vitro of the hydrolysate were studied. The results indicated that Proleather FG-F and Alcalase have better hydrolysis ability to almond protein than other proteases, and the IC50 values of their hydrolysates to ACE are 1.24 mg/ml and 0.98 mg/ml, respectively. Moreover, after simulated gastrointestinal digestion their hydrolysates still have high ACE-inhibitory activity.
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Almond protein was respectively hydrolyzed with Protamex, Alcalase, Neutrase, Flavourzyme, Proleather FG-F and Papain, and then the angiotensin I-converting enzyme (ACE) inhibitories activities of obtained hydrolysates were detected by high performance liquid chromatography (HPLC). With the degree of hydrolysis (DH) and the ACE-inhibitory activity of hydrolysate as evaluation indexes, the hydrolysis course and the digestion stability in vitro of the hydrolysate were studied. The results indicated that Proleather FG-F and Alcalase have better hydrolysis ability to almond protein than other proteases, and the IC50 values of their hydrolysates to ACE are 1.24 mg/ml and 0.98 mg/ml, respectively. Moreover, after simulated gastrointestinal digestion their hydrolysates still have high ACE-inhibitory activity.
Key concepts: Hydrolysate, Papain, Chemistry, Hydrolysis, Chromatography, Proteases, Enzymatic hydrolysis, Enzyme