Angiotensin-I-converting Enzyme Inhibitory Peptides from Tryptic Hydrolysates of Sodium Caseinate

Abstract

Abstract: Sodium caseinate contained peptidic angiotensin I-converting enzyme (ACE) inhibitors, which were released during hydrolysis by trypsin. The molecular mass distributions of the hydrolysates were identified by high performance size exclusion chromatography (HPSEC). ACE-inhibitory peptides were separated by ultrafiltration in terms of molecular weight. The ACE inhibitory activity of the permeates was IC50=0.42 mg/ml.Ultrafiltration was a effective tool for purification the hydrolysates to obtain thigh ACE-inhibitory activity peptides.

Key words: sodium caseinate, tryptic hydrolysates, HPSEC, ultrafiltration, ACE-inhibitor

XU Xin, ZHAO Mou-Ming, WANG Jin-Shui, YANG Xiao-Quan. Angiotensin-I-converting Enzyme Inhibitory Peptides from Tryptic Hydrolysates of Sodium Caseinate[J]. FOOD SCIENCE, 2005, 26(8): 185-188.

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Angiotensin-I-converting Enzyme Inhibitory Peptides from Tryptic Hydrolysates of Sodium Caseinate

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