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 the lowest IC50 value on ACE was 0.015 mg/mL. The amino acid sequences of the ACE-inhibitory peptides were Trp-Val, Val-Trp, Ile-Trp, and Leu-Trp, of which the IC50 values were 307.61, 0.58, 0.50, and 1.11 µΜ, respectively. Systolic blood pressure and diastolic blood pressure were reduced 20 and 21 mm Hg, respectively, in spontaneously hypertensive rats after 6 h of oral administration with a dose of 171.4 mg PN-1 powder/kg body weight.

journal_name

Nutrients

journal_title

Nutrients

authors

Lin YH,Chen GW,Yeh CH,Song H,Tsai JS

doi

10.3390/nu10101397

subject

Has Abstract

pub_date

2018-10-01 00:00:00

issue

10

issn

2072-6643

pii

nu10101397

journal_volume

10

pub_type

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