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 406739
Title Modulation of rheological properties by heat-induced aggregation of whey protein solution
Author(s) Purwanti, N.; Smiddy, M.; Goot, A.J. van der; Vries, R.J. de; Alting, A.; Boom, R.M.
Source Food Hydrocolloids 25 (2011)6. - ISSN 0268-005X - p. 1482 - 1489.
DOI https://doi.org/10.1016/j.foodhyd.2011.02.027
Department(s) Food Process Engineering
Physical Chemistry and Colloid Science
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2011
Keyword(s) beta-lactoglobulin - induced gelation - disulfide bonds - particle-size - isolate - ph - polymers - strength - gels
Abstract Heat-induced protein aggregation at low protein concentrations generally leads to higher viscosities. We here report that aggregated protein can yield weaker gels than those from native protein at the same concentration. Aggregated protein was produced by heating a solution of whey protein isolate (WPI) at 3% and 9% w/w. The higher protein concentration resulted in a larger aggregate size and a higher intrinsic viscosity. The protein fraction in native WPI had the smallest size and the lowest intrinsic viscosity. The same trend was observed for the shear viscosity after concentrating the suspensions containing aggregates to around 15% w/w. Suspensions containing aggregates that were produced from a higher concentration possessed a higher viscosity. After reheating the concentrated suspensions, the suspension from the 9% w/w aggregate system produced the weakest gel, followed by the one from 3% w/w, while the native WPI yielded the strongest gel. Reactivity of the aggregates was also an important factor that influenced the resulting gel properties. We conclude that aggregation of whey protein solution is a feasible route to manipulate the gel strength of concentrated protein systems, without having to alter the concentration of the protein.
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