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 405919
Title The effect of high pressure microfluidization on the structure and length distribution of whey protein fibrils
Author(s) Oboroceanu, D.; Wang, L.; Kroes-Nijboer, A.; Brodkorb, A.; Venema, P.; Magner, E.; Auty, M.A.
Source International Dairy Journal 21 (2011)10. - ISSN 0958-6946 - p. 823 - 830.
DOI http://dx.doi.org/10.1016/j.idairyj.2011.03.015
Department(s) Physics and Physical Chemistry of Foods
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2011
Keyword(s) transform infrared-spectroscopy - atomic-force microscopy - beta-lactoglobulin gels - amyloid fibrils - milk-proteins - heat - aggregation - rheology - flow
Abstract The effect of high pressure microfluidization on native ß-lactoglobulin (ß-lg) or whey protein isolate (WPI), both before and after heat-induced protein fibril formation at pH 2.0, was investigated using atomic force microscopy (AFM), shear birefringence, reversed phase high pressure liquid chromatography, attenuated total reflectance-Fourier transform infrared spectroscopy and fluorescence spectroscopy. The morphology and length distribution of the fibrils were determined using AFM and flow-induced birefringence, respectively. High pressure (= 50 MPa) microfluidization treatment of ß-lg induced ˜30% protein denaturation, accompanied by changes in secondary structure. Fibrils formed from high pressure treated ß-lg or WPI were similar in length to fibrils formed from non-pressure treated proteins. High pressure (= 50 MPa) microfluidization of fibrils formed from ß-lg or WPI resulted in their breakup into more uniformly sized and much shorter fibrils. Microfluidization pressures of up to 170 MPa resulted in slightly shorter fibrils but did not completely dissociate them.
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