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


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 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. Study holds ProTherm entries: 17399, 17400 Extra Details: peak 1 irreversible transitions; scan-rate dependence; scanning calorimetry; chromatography; protein denaturation; aggregation; globular proteins; ovalbumin

Submission Details

ID: gacg8KF24

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:49 p.m.

Version: 1

Publication Details
Weijers M;Barneveld PA;Cohen Stuart MA;Visschers RW,Protein Sci. (2003) Heat-induced denaturation and aggregation of ovalbumin at neutral pH described by irreversible first-order kinetics. PMID:14627731
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P
 

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)


Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Ovalbumin P01012 OVAL_CHICK
90.7 Ovalbumin O73860 OVAL_MELGA