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 326621
Title Heat-induced denaturation and aggregation of ovalbumin at neutral pH described by irreversible first-order kinetics
Author(s) Weijers, M.; Barneveld, P.A.; Cohen Stuart, M.A.; Visschers, R.W.
Source Protein Science 12 (2003). - ISSN 0961-8368 - p. 2693 - 2703.
Department(s) Physical Chemistry and Colloid Science
Publication type Refereed Article in a scientific journal
Publication year 2003
Keyword(s) differential scanning calorimetry - protein denaturation - beta-lactoglobulin - thermal-denaturation - globular-proteins - light-scattering - disulfide bonds - dsc data - gelation - gels
Abstract The heat-induced denaturation kinetics of two different sources of ovalbumin at pH 7 was studied by chromatography and differential scanning calorimetry. The kinetics was found to be independent of protein concentration and salt concentration, but was strongly dependent on temperature. For highly pure ovalbumin, the decrease in nondenatured native protein showed first-order dependence. The activation energy obtained with different techniques varied between 430 and 490 kJ.mole(-1). First-order behavior was studied in detail using differential scanning calorimetry. The calorimetric traces were irreversible and highly scan rate-dependent. The shape of the thermograms as well as the scan rate dependence can be explained by assuming that the thermal denaturation takes place according to a simplified kinetic process N -->(k) D where N is the native state, D is denatured (or another final state) and k a first-order kinetic constant that changes with temperature, according to the Arrhenius equation. A kinetic model for the temperature-induced denaturation and aggregation of ovalbumin is presented. Commercially obtained ovalbumin was found to contain an intermediate- stable fraction (IS) of about 20% that was unable to form aggregates. The denaturation of this fraction did not satisfy first-order kinetics.
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