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 417748
Title Modeling peptide formation during the hydrolysis of beta-casein by Lactococcus lactis
Author(s) Munoz-Tamayo, R.; Groot, J. de; Wierenga, P.A.; Gruppen, H.; Zwietering, M.H.; Sijtsma, L.
Source Process Biochemistry 47 (2012)1. - ISSN 1359-5113 - p. 83 - 93.
DOI https://doi.org/10.1016/j.procbio.2011.10.012
Department(s) Food Chemistry Group
Food Microbiology Laboratory
FBR Bioconversion
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2012
Keyword(s) proteins - identification - degradation - kinetics
Abstract Hydrolysis of milk proteins by lactic acid bacteria leads to the formation of a large number of peptides. In this work, the hydrolysis of ß-casein by the protease PrtPI of Lactococcus lactis was studied. Experiments were carried out at different initial enzyme/substrate ratios. Identification and quantification of peptides were performed by MS and RP-UHPLC analyses. Nine low molecular weight (LMW) peptides were quantified absolutely. Additionally, semi-quantification of six high molecular weight peptides (HMW) was provided. To describe the dynamics of peptides concentrations, an aggregated model was developed. This model links peptide formation to the breakdown of intact protein by introducing the concept of virtual intermediate peptides (VIP). The model represented the experimental data with an average error of 14% (comparable with the experimental error). By using the model, three dynamic pools of peptides were identified. The model suggests that LMW peptides have similar dynamic characteristics as their counterpart HMW peptides in the ß-casein sequence. This study indicates that the presence and structure of micelles affect the hydrolysis dynamics and that, for some peptides, the enzyme/substrate ratio appears to affect the hydrolysis stoichiometry. The model developed is parsimonious and has a basic mechanistic component. It allows for a rational study of protein hydrolysis. --------------------------------------------------------------------------------
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