Revalorisation of bovine collagen as a potential precursor of angiotensin I-converting enzyme (ACE) inhibitory peptides based on in silico and in vitro protein digestions

Revalorisation of bovine collagen as a potential precursor of angiotensin I-converting enzyme (ACE) inhibitory peptides based on in silico and in vitro protein digestions

In silico proteolysis using 27 proteases theoretically released numerous ACE-inhibitory peptides from collagen alpha-1(I) and alpha-2(I) sequences. Papain was the most effective protease to release ACE-inhibitory peptides. Two quantitative structure–activity relationship (QSAR) models for ACE-inhibi...

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Bibliographic Details
Main Authors: Yu Fu, Jette Feveile Young, Mette Marie Løkke, René Lametsch, Rotimi E. Aluko, Margrethe Therkildsen
Format: Article
Language:English
Published: Elsevier 2016-06-01
Series:Journal of Functional Foods
Subjects:
In silico analysis
Collagen
ACE-inhibitory peptides
BIOPEP
QSAR
Online Access:http://www.sciencedirect.com/science/article/pii/S1756464616300470

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http://www.sciencedirect.com/science/article/pii/S1756464616300470

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