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 476884
Title Introducing enzyme selectivity: a quantitative parameter to describe enzymatic protein hydrolysis
Author(s) Butré, C.I.; Sforza, S.; Gruppen, H.; Wierenga, P.A.
Source Analytical and Bioanalytical Chemistry 406 (2014)24. - ISSN 1618-2642 - p. 5827 - 5841.
DOI https://doi.org/10.1007/s00216-014-8006-2
Department(s) Food Chemistry
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2014
Keyword(s) bovine beta-lactoglobulin - tryptic hydrolysis - substrate-specificity - mass-spectrometry - release kinetics - casein - peptides - identification - ph - proteases
Abstract Enzyme selectivity is introduced as a quantitative parameter to describe the rate at which individual cleavage sites in a protein substrate are hydrolyzed relative to other cleavage sites. Whey protein isolate was hydrolyzed by Bacillus licheniformis protease, which is highly specific for Glu and Asp residues. The molar concentration of all peptides (58) from ß-lactoglobulin formed during hydrolysis was determined from the UV214 signal. The quality of identification and quantification of the peptides were described by newly defined parameters: the peptide sequence coverage (on average 94 %) and the molar sequence coverage (on average 75 %). The selectivity was calculated from the rate of hydrolysis of each cleavage site, and showed differences of up to a factor of 5,000. The ability to quantitatively discriminate the enzyme preference towards individual cleavage sites is considered essential to the understanding of enzymatic protein hydrolysis.
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