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 PDB Entries

Structure ID Release Date Resolution Structure Title
1UHG 2003-07-22 1.9 Crystal Structure of S-Ovalbumin At 1.9 Angstrom Resolution
1OVA 1992-04-15 1.95 CRYSTAL STRUCTURE OF UNCLEAVED OVALBUMIN AT 1.95 ANGSTROMS RESOLUTION
3P9L 2011-10-19 2.0 Crystal Structure of H2-Kb in complex with the chicken ovalbumin epitope OVA
3P9M 2011-10-19 2.0 Crystal Structure of H2-Kb in complex with a mutant of the chicken ovalbumin epitope OVA-G4
3PAB 2011-10-19 2.2 Crystal Structure of H2-Kb in complex with a mutant of the chicken ovalbumin epitope OVA-E1
1JTI 2001-09-05 2.3 Loop-inserted Structure of P1-P1' Cleaved Ovalbumin Mutant R339T
1VAC 1996-06-20 2.5 MHC CLASS I H-2KB HEAVY CHAIN COMPLEXED WITH BETA-2 MICROGLOBULIN AND CHICKEN OVALBUMIN
3CVH 2008-09-23 2.9 How TCR-like antibody recognizes MHC-bound peptide
3C8K 2008-04-15 2.9 The crystal structure of Ly49C bound to H-2Kb
1P4L 2003-11-11 2.9 Crystal structure of NK receptor Ly49C mutant with its MHC class I ligand H-2Kb
4HKJ 2012-11-14 3.0 Structure of Cowpox CPXV203 in complex with MHCI (H-2Kb)
1P1Z 2003-11-11 3.26 X-RAY CRYSTAL STRUCTURE OF THE LECTIN-LIKE NATURAL KILLER CELL RECEPTOR LY-49C BOUND TO ITS MHC CLASS I LIGAND H-2Kb

Relevant UniProtKB Entries

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