Angiotensin I-converting enzyme inhibitory and antioxidant properties of rapeseed hydrolysates

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• 作者：Sari Mä ; kinen^a ; ^{sari.makinen@mtt.fi} ; Tessa Johannson^a ; ¹ ; ^{tessa.johansson@fi.nestle.com} ; E. Vegarud Gerd^b ; ^{gerd.vegarud@umb.no} ; Juha Matti Pihlava^a ; ^{juha-matti.pihlava@mtt.fi} ; Anne Pihlanto^a ; ^{anne.pihlanto@mtt.fi}
• 关键词：Rapeseed by-product hydrolysates ; Bioactive peptides ; Protein ; Angiotensin I-converting enzyme inhibition ; Enzymatic hydrolysis
• 刊名：Journal of Functional Foods
• 出版年：2012
• 期刊代码：P18_17564646
• 类别：bio
• 出版时间：July, 2012
• 卷：4
• 期：3
• 页码：575-583
• 文件大小：437 K

摘要

This study investigates the angiotensin I-converting enzyme (ACE) inhibitory and antioxidative activities of protein hydrolysates prepared from industrial defatted rapeseed meal using various proteolytic enzymes. The hydrolysate generated by Alcalase displayed the highest ACE-inhibitory activity (IC₅₀ 0.02 mg/ml) as well as high inhibitory capacity against lipid oxidation in a liposomal model. The Alcalase hydrolysate was fractionated using stepwise solid-phase extraction into three fractions (SP10, SP30, SP60), of which the hydrophobic fractions possessed the highest ACE-inhibitory activity. Subjecting these fractions to ultra filtration with 3000 Da molecular weight cut off (MWCO) membrane revealed that ACE-inhibitory activity was concentrated in the permeate. The ACE-inhibitory peptides in Alcalase hydrolysate exhibited good stability in an in vitro digestion model using human gastric and duodenal fluids. Kinetics studies gave moderate K_i values (0.2-0.3 mg/ml) and an uncompetitive pattern of ACE inhibition for the Alcalase hydrolysate and peptide fractions. Our results indicate the defatted rapeseed meal is a potential source of ACE-inhibitory compounds for use in functional foods.