Purification of angiotensin I-converting enzyme (ACE) inhibitory peptides from casein hydrolysate by IMAC-Ni2+

被引：12

作者：

Wu, Shanguang ^{[1
]}

Feng, Xuezhen ^{[1
]}

Lu, Yuan ^{[1
]}

Lu, Yuting ^{[1
]}

Liu, Saisai ^{[1
]}

Tian, Yuhong ^{[1
]}

机构：

[1] Guangxi Univ Sci & Technol, Liuzhou 545006, Guangxi, Peoples R China

来源：

AMINO ACIDS | 2017年 / 49卷 / 10期

关键词：

Casein hydrolysate; IMAC-Ni2+; ACE inhibitory peptide; Purification; AFFINITY PURIFICATION; PROTEIN; IDENTIFICATION;

D O I：

10.1007/s00726-017-2475-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Casein proteins were hydrolyzed by papain to identify inhibitory peptides of angiotensin I-converting enzyme (ACE). The hydrolysate was fractionized by immobilized metal affinity chromatography (IMAC-Ni2+). The fraction with high ACE inhibitory activity was enriched and further chromatographed on a reverse-phase column to yield four fractions. Among the fractions, the L4 fraction exhibited the highest ACE inhibitory activity and was identified by sequence analysis as Trp-Tyr-Leu-His-Tyr-Ala (WYLHYA), with IC50 value of 16.22 +/- 0.83 A mu M in vitro. This peptide was expected to be applied as an ingredient for preventing hypertension and IMAC-Ni2+ may provide a simple method for purification of ACE inhibitory peptides.

引用

页码：1787 / 1791

页数：5

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