ACE-inhibitory activity of enzymatic protein hydrolysates from lupin and other legumes

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• 作者：Giovanna Boschin ; Graziana Maria Scigliuolo ; Donatella Resta ; Anna Arnoldi
• 关键词：ACE ; angiotensinconverting enzyme ; BSA ; bovin serum albumin ; E/S ; enzyme/substrate ; HA ; hippuric acid ; HHL ; hippuryl-histidyl-leucine ; HL ; histidyl-leucine ; LPI ; lupin protein isolate ; SDS&ndash ; PAGE ; sodium dodecyl sulphate&ndash ; polyacrylamide gel elect
• 刊名：Food Chemistry
• 出版年：2014
• 出版时间：15 February, 2014
• 年：2014
• 卷：145
• 期：Complete
• 页码：34-40
• 全文大小：618 K

文摘

The objective of this investigation was to compare the angiotensin converting enzyme (ACE)-inhibitory activity of the hydrolysates obtained by pepsin digestion of proteins of some legumes, such as chickpea, common bean, lentil, lupin, pea, and soybean, by using the same experimental procedure. The ACE-inhibitory activity was measured by using the tripeptide hippuryl-histidyl-leucine (HHL), as model peptide, and HPLC-DAD, as analytical method. The peptide mixtures of all legumes were active, with soybean and lupin the most efficient, with IC₅₀ values of 224 and 226 ¦Ìg/ml, respectively. Considering the promising results obtained with lupin, and aiming to identify the protein(s) that release(s) the peptides responsible for the activity, the peptides obtained from the pepsin digestion of some industrial lupin protein isolates and purified protein fractions were tested. The most active mixture, showing an IC₅₀ value of 138 ¦Ìg/ml, was obtained hydrolysing a mixture of lupin ¦Á + ¦Â conglutin.