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 60594
Title Heat-induced deamidation, dephosphorylation and breakdown of caseinate
Author(s) Boekel, M.A.J.S. van
Source International Dairy Journal 9 (1999). - ISSN 0958-6946 - p. 237 - 241.
DOI http://dx.doi.org/10.1016/S0958-6946(99)00068-0
Department(s) Integrated Food Science and Food Physics
VLAG
Publication type Refereed Article in a scientific journal
Publication year 1999
Abstract The kinetics of deamidation, dephosphorylation and protein breakdown in heated caseinate solutions were studied. The extent of deamidation corresponded to the level of the amide present in asparagine. The order with respect to concentration was 1, the order with respect to time could not be established unequivocally. The temperature dependence was in accordance with a mechanism in which a succinimide intermediate was formed. The extent of protein breakdown, measured as formation of non-protein nitrogen (NPN), was also characterized by an order of 1 with respect to concentration. The temperature dependence was in accordance with peptide bond hydrolysis (the order with respect to time could not be established unequivocally). Formation of inorganic phosphate and dehydroalanine was determined in heated -casein solutions. More phosphate than dehydroalanine was formed, and based on literature results for lysinoalanine formation from dehydroalanine, it was concluded that hydrolysis of phosphoserine occurred more extensively than -elimination of phosphoserine. The order with respect to time for dephosphorylation seemed to increase with temperature, possibly due to a different temperature sensitivity of hydrolysis and -elimination.
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