Heat-induced denaturation and aggregation of ovalbumin at neutral pH described by irreversible first-order kinetics

被引:118
作者
Weijers, M
Barneveld, PA
Stuart, MAC
Visschers, RW
机构
[1] Wageningen Univ, Lab Phys Chem & Colloid Sci, Dept Agrotechnol & Nutr Sci, NL-6703 HB Wageningen, Netherlands
[2] Wageningen Ctr Food Sci, NL-6700 AN Wageningen, Netherlands
[3] NIZO Food Res, NL-6718 ZB Ede, Netherlands
关键词
irreversible transitions; scan-rate dependence; scanning calorimetry; chromatography; protein denaturation; aggregation; globular proteins; ovalbumin;
D O I
10.1110/ps.03242803
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:2693 / 2703
页数:11
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