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 407963
Title Identification of the Peroxidase-Generated Intermolecular Dityrosine Cross-Link in Bovine a-Lactalbumin
Author(s) Heijnis, W.H.; Dekker, H.L.; Koning, L.J.; Wierenga, P.A.; Westphal, A.H.; Koster, C.G. de; Gruppen, H.; Berkel, W.J.H. van
Source Journal of Agricultural and Food Chemistry 59 (2011)1. - ISSN 0021-8561 - p. 444 - 449.
Department(s) Food Chemistry Group
Publication type Refereed Article in a scientific journal
Publication year 2011
Keyword(s) microbial transglutaminase - mass-spectrometry - wheat-flour - proteins - tyrosine - dough
Abstract The peroxidase-mediated oxidation of calcium-depleted bovine a-lactalbumin generates a mixture of covalently bound protein oligomers with interesting foaming properties. Here, we isolated the initially formed covalent a-lactalbumin dimer and studied its mode of cross-linking. Liquid chromatography-Fourier transform mass spectrometry (LC-FTMS) of proteolytic digests revealed the unambiguous identification of a peroxidase-catalyzed covalent link between Tyr18 and Tyr50. This shows that, although the radical reaction is often regarded as a random reaction, the initial product formation is specific. Protein structural modeling indicates that the conjugation reaction between these tyrosines is sterically favored and involves initial noncovalent protein complex formation through charge compensation, facilitating intermolecular cross-linking. The identification of the Tyr18-Tyr50 cross-link supports the view that the peroxidase-mediated oxidation of apo a-lactalbumin is a sequential process, involving the formation of linear trimers and higher order oligomers.
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