Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 536920
Title Comparison of Protein Hydrolysis Catalyzed by Bovine, Porcine, and Human Trypsins
Author(s) Deng, Yuxi; Gruppen, Harry; Wierenga, Peter A.
Source Journal of Agricultural and Food Chemistry 66 (2018)16. - ISSN 0021-8561 - p. 4219 - 4232.
DOI http://dx.doi.org/10.1021/acs.jafc.8b00679
Department(s) Food Chemistry Group
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2018
Keyword(s) LC-MS - peptide release kinetics - protein digestibility - secondary specificity - tryptic hydrolysis
Abstract Based on trypsin specificity (for lysines and arginines), trypsins from different sources are expected to hydrolyze a given protein to the same theoretical maximum degree of hydrolysis (DHmax,theo). This is in contrast with experiments. Using α-lactalbumin and β-casein, this study aims to reveal if the differences among experimental DHmax (DHmax,exp) by bovine, porcine, and human trypsins are due to their secondary specificity. Peptide analysis showed that ∼78% of all the cleavage sites were efficiently hydrolyzed by porcine trypsin, and ∼47 and ∼53% were efficiently hydrolyzed by bovine and human trypsins, respectively. These differences were explained by the enzyme secondary specificity, that is, their sensitivities to the amino acids around the cleavage sites. The DHmax predictions based on the secondary specificity were 4 times closer to the DHmax,exp than the predictions based on trypsin specificity alone (DHmax,theo). Proposed preliminary relations between binding sites and trypsin secondary specificity allow DHmax,exp estimations of tryptic hydrolysis of other proteins.
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