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 445464
Title Modulation of the Gelation Efficiency of Fibrillar and Sherical Aggregates by Means of Thiolation
Author(s) Munialo, C.D.; Jongh, H.H.J. de; Broersen, K.; Linden, E. van der; Martin, A.H.
Source Journal of Agricultural and Food Chemistry 61 (2013)47. - ISSN 0021-8561 - p. 11628 - 11635.
Department(s) Physics and Physical Chemistry of Foods
Publication type Refereed Article in a scientific journal
Publication year 2013
Keyword(s) whey-protein isolate - bovine beta-lactoglobulin - sulfhydryl-groups - rheological properties - succinylated caseins - gels - heat - stability - ph - temperature
Abstract Fibrillar and spherical aggregates were prepared from whey protein isolate (WPI). These aggregates were thiolated to a substantial degree to observe any impact on functionality. Sulfur-containing groups were introduced on these aggregates which could be converted to thiol groups by deblocking. Changes on a molecular and microstructural level were studied using tryptophan fluorescence, transmission electron microscopy, and particle size analysis. The average size (nm) of spherical aggregates increased from 38 to 68 nm (blocked variant) and 106 nm (deblocked variant) after thiolation, whereas the structure of fibrillar aggregates was not affected. Subsequently, gels containing these different aggregates were prepared. Rheological measurements showed that thiolation decreased the gelation concentration and increased gel strength for both WPI fibrillar and spherical aggregates. This effect was more pronounced upon thiolation of preformed fibrillar aggregates. The findings suggest that thiolation at a protein aggregate level is a promising strategy to increase gelation efficiency.
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