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 496593
Title Gelatin increases the coarseness of whey protein gels and impairs water exudation from the mixed gel at low temperatures
Author(s) Martin, A.H.; Bakhuizen, E.; Ersch, C.; Urbonaite, V.; Jongh, H.H.J. de; Pouvreau, L.A.M.
Source Food Hydrocolloids 56 (2016). - ISSN 0268-005X - p. 236 - 244.
Department(s) Physics and Physical Chemistry of Foods
FBR Food Technology
Publication type Refereed Article in a scientific journal
Publication year 2016
Keyword(s) Water holding - whey protein - gelatin - protein mixture - coarseness - gel stiffness
Abstract To understand the origin of water holding of mixed protein gels, a study was performed on water exudation from mixed whey protein (WP)-gelatin gels upon applied pressure. Mixed gels were prepared with varying WP and gelatin concentration and gelatin type to obtain gels with a wide range of gel properties. Gels were characterized for their water holding (maximum of exuded water, Amax, and ease with which water can be exuded, k), gel coarseness (from CLSM image analysis) and gel stiffness (Young's modulus) at 20 and 40 °C, below and above the melting temperature of gelatin. Gelatin caused an increase in gel coarseness of the WP network, as induced by phase separation between WP and gelatin. The effect of gel coarseness and gel stiffness on Amax was found to be intertwined but above all, dictated by the gelatin concentration and gelatin network. At 20 °C, a transition point in gelatin concentration was observed above which stiffness surpassed coarseness in importance for Amax. Above this concentration, gelatin dominates the mechanical response of the mixed system. At 40 °C, when gelatin is melted, coarser and less stiff networks, as set by the WP network, lead to higher Amax. Tailoring of the coarseness and stiffness and therefore Amax and k, can be achieved by selective mixing in terms of protein concentrations, and type of gelatin. By varying gelatin type from A to B, altered phase behavior leads to gels with higher coarseness and lower stiffness but similar Amax.
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