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 497954
Title Setting the conditions for protein exchangeability by the energy balance and mechanical responses
Author(s) Martin, A.H.; Jose, J.; Tonneijck, L.; Jongh, H.H.J. de; Pouvreau, L.A.M.
Event ISFRS 2015, Zurich, 2015-06-07/2015-06-11
Department(s) Physics and Physical Chemistry of Foods
VLAG
FBR Food Technology
Publication type Poster (scientific)
Publication year 2015
Abstract The understanding of (oral) breakdown properties or macroscopic functionalities such as water holding capacity is essential in relation to sensory properties. During (oral) processing, applied force can either be stored or dissipated via a number of physical processes. The balance between dissipation modes as fracture events and flow of water through or from the gel during deformation,
and the amount of energy stored was compared for plant proteins (soy, pea) and animal proteins (whey, plasma, egg white, casein). Fracture properties (fracture stress and strain, Young’s modulus), water holding (WH) and recoverable energy (RE, as a measure for the amount of energy stored) were determined for protein gels with varying morphology (CLSM, SEM). Whereas plant proteins typically have low fracture stress/Young’s modulus and a wide range in RE, animal proteins
are limited in variation in RE but show high fracture stress/Young’s modulus. In general, the occurrence of fracture events results in low values for RE. To facilitate protein exchangeability it is essential to bridge the gap in mechanical responses between plant proteins and animal proteins. Selectively mixing of plant proteins with other proteins, or tuning the processing conditions were amongst others identified as applicable strategies to modulate the mechanical
responses of the gels formed. We illustrate this with findings on how to direct fracture behavior and other energy dissipation mechanisms for various protein systems and mixtures thereof.
Aggregation behavior and network morphology are investigated in order to explain changes in mechanical properties. Insights from this study open up opportunities for broader applicability of plant proteins and provide the next step towards protein exchangeability.

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