Purification and Identification of Angiotensin I-Converting Enzyme Inhibitory Peptides and the Antihypertensive Effect of Chlorella sorokiniana Protein Hydrolysates.

ABSTRACT: Hot water was used to obtain Chlorella sorokiniana hot water extract (HWE). Subsequently, this byproduct was freeze-dried, hydrolysed at 50 °C using Protease N to obtain C. sorokiniana protein hydrolysates (PN-1), and then digested with a gastrointestinal enzyme (PN-1G). The inhibitory effects of the HWE and hydrolysates against angiotensin I-converting enzyme (ACE) were investigated. The soluble protein and peptide contents were 379.9 and 179.7 mg/g, respectively, for HWE and 574.8 and 332.8 mg/g, respectively, for PN-1. The IC50 values of the HWE, PN-1, and PN-1G on ACE were 1.070, 0.035, and 0.044 mg/mL, respectively. PN-1G was separated into seven fractions through size exclusion chromatography. The sixth fraction of the hydrolysate had a molecular weight between 270 and 340 Da, and th

SUBMITTER: Lin YH 

PROVIDER: S-EPMC6213796 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature