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 407938
Title Characteristics and Effects of Specific Peptides on Heat-Induced Aggregation of ß-Lactoglobulin
Author(s) Kosters, H.A.; Wierenga, P.A.; Vries, R.J. de; Gruppen, H.
Source Biomacromolecules 12 (2011)6. - ISSN 1525-7797 - p. 2159 - 2170.
Department(s) Food Chemistry Group
Physical Chemistry and Colloid Science
Publication type Refereed Article in a scientific journal
Publication year 2011
Keyword(s) whey-protein isolate - bacillus-licheniformis protease - induced denaturation - thermal-stability - neutral ph - kinetics - gelation - hydrolysis - identification - fractions
Abstract A bovine ß-lactoglobulin hydrolysate, obtained by the hydrolysis by the Glu specific enzyme Bacillus licheniformis protease (BLP), was fractionated at pH 7.0 into a soluble and an insoluble fraction and characterized by LC-MS. From the 26 peptides identified in the soluble fraction, five peptides (A[f97–112] = [f115–128], AB[f1–45], AB[f135–157], AB[f135–158], and AB[f138–162]) bound to ß-lactoglobulin at room temperature. After heating of ß-lactoglobulin in the presence of peptides, eight peptides were identified in the pellet formed, three of them belonging to the previously mentioned peptides. Principle component analysis revealed that the binding at room temperature (to ß-lactoglobulin) was related to the total hydrophobicity and the total charge of the peptides. The binding to the unfolded protein could not be attributed to distinct properties of the peptides. The presence of the peptides caused a 50% decrease in denaturation enthalpy (from 148 ± 3 kJ/mol for the protein alone to 74 ± 2 kJ/mol in the presence of peptides), while no change in secondary structure or denaturation temperature was observed. At temperatures
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