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 414330
Title Cross-Linking Behavior and Foaming Properties of Bovine a-Lactalbumin after Glycation with Various Saccharides
Author(s) Haar, R. ter; Westphal, Y.; Wierenga, P.A.; Schols, H.A.; Gruppen, H.
Source Journal of Agricultural and Food Chemistry 59 (2011)23. - ISSN 0021-8561 - p. 12460 - 12466.
Department(s) Food Chemistry Group
Publication type Refereed Article in a scientific journal
Publication year 2011
Keyword(s) maillard reaction - beta-lactoglobulin - formation pathways - proteins - stability - pentoses - hexoses - food
Abstract a-Lactalbumin was glycated via the Maillard reaction in the dry state using various mono- and oligosaccharides. The reaction resulted not only in coupling of the saccharides to a-lactalbumin but also in cross-linked proteins. The glycation rate and the extent of cross-link formation were highly dependent on the saccharide used. Glycation by arabinose and xylose led to a very fast protein cross-link formation, whereas glucose showed a relatively low protein cross-linking ability. The stability of foams, created using the various glycated protein samples, depended on the type of saccharide used, the extent of glycation, and possibly the amount of cross-linked protein. Compared to nonmodified a-lactalbumin, glycation with rhamnose and fucose improved foam stability, whereas application of glucose, galacturonic acid, and their oligosaccharides did not exert a clear effect. Mass spectrometric analysis revealed that dehydration of the Amadori products is an indicator of the formation of protein cross-links.
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