Separation and Purification of Angiotensin Ⅰ-Converting Enzyme Inhibitor from Walnut Protein

doi:10.7506/spkx1002-6630-201309012

Abstract

Abstract:

An angiotensin Ⅰ-converting enzyme (ACE) inhibitor was separated and purified from pepsin hydrolysate of
walnut protein by ultrafiltration, gel permeation chromatography and HPLC. The inhibitory activity and in vitro digestive
stability of the ACE inhibitor were examined. Its structure was identified through N terminus amino acid sequencing as Tyr-
Glu-Pro. The IC50 of this inhibitor derived from walnut protein was 0.32 μg/mL. This activity was well maintained after
simulated digestion in vitro.

Key words: angiotensin Ⅰ-converting enzyme (ACE), pepsin, purification, separation, walnut protein

CLC Number:

Q555

GU Xin1,2，LI Di3，HOU Ya-kun1,2，CUI Jie1,2，WANG Jian-zhong1,2,*. Separation and Purification of Angiotensin Ⅰ-Converting Enzyme Inhibitor from Walnut Protein[J]. FOOD SCIENCE, 2013, 34(9): 52-55.

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