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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    Modification of Ovalbumin with Fructooligosaccharides: Consequences for Network Morphology and Mechanical Deformation Responses
    Munialo, C.D. ; Ortega, R.G. ; Linden, E. van der; Jongh, H.H.J. de - \ 2014
    Langmuir 30 (2014)46. - ISSN 0743-7463 - p. 14062 - 14072.
    protein gels - rheological properties - beta-lactoglobulin - maillard reaction - pea protein - neutral ph - mixed gels - gelation - aggregation - perception
    The Maillardation of proteins has been used as a natural alternative to improve its functionality by covalent coupling of proteins with saccharides. However, the impact of Maillard reaction on the structural aspects of protein networks and, as a consequence, the mechanical breakdown properties of the gel networks has not been reported. The objective of this study was to evaluate how the attachment of linear oligo-sugar moieties onto ovalbumin affects its aggregation, network morphology, and consequently the mechanical deformation properties including the ability of the networks to elastically store energy in this material. To potentially alter the morphology of the network structure, ovalbumin was modified by conjugating some of its amino groups with fructooligosaccharide (FOS) moieties via the Maillard reaction. It was demonstrated that the attachment of FOS to ovalbumin does not affect the integrity of the secondary and tertiary structure as characterized using circular dichroism and tryptophan fluorescence. Differences in the network morphology were observed by scanning electron microscopy for FOS-modified ovalbumin variants. Upon increased modification, the microstructure of the gels had more and larger pores and had thinner strands than nonmodified variants. Evaluation of the large deformation properties of the gels demonstrated that FOS-modified gels were less strong and less brittle and showed lower stiffness than nonmodified variants. The recoverable energy (elastically stored energy) of gels reduced with an increase in the degree of modification. The results show that the attachment of FOS to ovalbumin alters the structural and mechanical (large) breakdown properties of the protein gels. The consequences of the alteration of the network structure and large deformation properties of FOS-modified ovalbumin offer opportunities to efficiently design food materials with desirable techno-functional applications
    Qualitative methodology for efficient food chain design
    Apaiah, R.K. ; Hendrix, E.M.T. ; Meerdink, G. ; Linnemann, A.R. - \ 2005
    Trends in Food Science and Technology 16 (2005)5. - ISSN 0924-2244 - p. 204 - 214.
    pea protein - functional-properties - denaturation - fractions - flour - texturization - extrusion - heat
    This paper presents a methodology to efficiently design food supply chains. The goals of quality, cost and environmental load are looked at independently of each other. Food chains are made up of links and are designed to deliver a particular product with consumer-specified attributes. These attributes are used to select the goals (quality, cost and environment load) to optimise the chain. The methodology presents a systematic way to identify problem areas in supply chains. The entire chain from primary production up to and including consumer processing influences the final product; but the relative contribution of the links varies according to the goal for which the chain is being designed and optimised. Case studies on a novel protein food made from pea protein are presented to showcase the methodology
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