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 121816
Title Mild isolation procedure discloses new protein structural properties of b-lactoglobulin
Author(s) Jongh, H.H.J. de; Groneveld, T.; Groot, J. de
Source Journal of Dairy Science 84 (2001)3. - ISSN 0022-0302 - p. 562 - 571.
Department(s) Food Chemistry Group
Publication type Refereed Article in a scientific journal
Publication year 2001
Abstract To explore the potentially available functional properties of β-lactoglobulin in, for example, the processing of food products, it is important to isolate the protein by a procedure that avoids all possible denaturing conditions, such as low pH, high ionic strength, or low or elevated temperatures that could cause the protein to undergo irreversible conformational changes. In this work, a mild isolation protocol for β-lactoglobulin from bovine milk is presented, applicable to semi large-scale isolations (50 to 200 g). The protein could be isolated with a high efficiency (>80€and a good purity (>98Ž Biochemical characterization of the material demonstrated no lactosylation of the protein, nor the formation of irreversibly associated dimers. Also, no proteose peptones could be detected. The ability of β-lactoglobulin to undergo conformational changes is studied by far and near-ultraviolet circular dichroism and differential scanning calorimetry. A βglobalβ unfolding of the protein is detected around 72 (tertiary level) and 77°C (secondary level). The dimer-monomer dissociation occurring around 52°C could also be monitored at a secondary structural level. Remarkably, a low temperature transition around 30°C was observed, where approximately 10 β-stranded residues unfold cooperatively, not been reported previously. This low temperature transition is irreversible at temperatures higher than 35°C or upon freezing the material at -20°C. The addition of 20␐lycerol could prevent this irreversible conformational change. The effect of the low temperature transition on the protein's functionality remains to be investigated.
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