Purification of angiotensin I-converting enzyme (ACE) inhibitory peptides from casein hydrolysate by IMAC-Ni2+
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 µM 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.
KeywordsCasein hydrolysate IMAC-Ni2+ ACE inhibitory peptide Purification
This work was supported by Key Project of Guangxi Natural Science Foundation (2016GXNSFAA380055) and Key project of Guangxi Key Laboratory of Functional Phytochemicals Research and Utilization (FPRU2013-8).
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Conflict of interest
Shanguang Wu, Xuezhen Feng, Yuan Lu, Yuting Lu, Saisai Liu and Yuhong Tian confirm that this article content has no conflicts of interest.
The article does not contain any studies in patients by any of the authors.
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