Selective enrichment of bioactive properties during ultrafiltration of a tryptic digest of 尾-lactoglobulin
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- 作者：O. Powera ; c ; A. Ferná ; ndezb ; R. Norrisa ; F.A. Rierab ; R.J. FitzGeralda ; c ; dick.fitzgerald@ul.ie" class="auth_mail
- 关键词：尾-lactoglobulin ; Trypsin ; Enzyme hydrolysis ; Membrane processing ; Bioactive peptides ; Dipeptidyl peptidase IV ; Antioxidant ; Angiotensin converting enzyme
- 刊名：Journal of Functional Foods
- 出版年：July 2014
- 年：2014
- 卷：9
- 期：Complete
- 页码：38-47
- 全文大小：777 K
文摘
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A 尾-lactoglobulin tryptic hydrolysate had antioxidant activity and inhibited dipeptidyl peptidase IV and angiotensin converting enzyme.
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Membrane fractionation selectively enhanced the bioactive properties of this hydrolysate.
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尾-lactoglobulin derived peptide 尾-lg f(15–20), VAGTWY, has multifunctional activity (antioxidant activity, dipeptidyl peptidase IV and angiotensin converting enzyme inhibition) and this is the first report of its potent antioxidant activity.
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尾-lactoglobulin peptides IIAEK and IPAVFK were inhibitors of angiotensin converting enzyme.
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尾-lactoglobulin peptides have potential as multifunctional ingredients for management of type 2 diabetes and cardiovascular disease.