Heat-induced changes in the susceptibility of egg white proteins to enzymatic hydrolysis: a kinetic study

Journal of Agricultural and Food Chemistry
Iesel Van der PlanckenMarc E Hendrickx

Abstract

A kinetic study was conducted on the effect of heating in the temperature range of 50-92 degrees C, on the susceptibility of ovalbumin and albumen solutions to enzymatic hydrolysis by a mixture of trypsin and alpha-chymotrypsin at 37 degrees C and pH 8.0. Heat treatment resulted in an increase in degree of hydrolysis after 10 min of enzymatic reaction of both ovalbumin and albumen, as measured using the pH-stat method. The time-dependent change in the susceptibility to enzymatic hydrolysis after heat treatment was described by a fractional conversion model (based on an apparent first-order reaction kinetic model). Different end levels of degree of hydrolysis were obtained after heating for a long time at different temperatures, which suggests that the final degree of unfolding of the protein is temperature dependent.

Citations

Oct 31, 2012·The British Journal of Nutrition·Juliet A GerrardNigel G Larsen
May 19, 2010·International Journal of Molecular Sciences·Mohamed Beva Kelfala FohWenshui Xia
Oct 8, 2008·Bioscience, Biotechnology, and Biochemistry·Takeshi MatsubaraTsukasa Matsuda
Oct 10, 2006·Journal of Bioscience and Bioengineering·Yasunori SuzukiKunihiko Watanabe
May 24, 2007·Molecular & Cellular Proteomics : MCP·Yun LiuBaohong Liu
Sep 11, 2010·Journal of the Royal Society, Interface·Jason T DeJongTammer Barkouki

Related Concepts

Alpha-chymotrypsin
Avazyme
Egg White Proteins
Hydrogen-Ion Concentration
Hydrolysis
Ovalbumin
Protein Denaturation
Substrate Specificity
Trypure

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