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Trypsin Inhibition Activity of Heat‐Denatured Ovomucoid: A Kinetic Study
Author(s) -
Plancken Iesel Van der,
Van Remoortere Marijke,
Van Loey Ann,
Hendrickx Marc E.
Publication year - 2008
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp034126m
Subject(s) - chemistry , trypsin , egg white , lysozyme , heat stability , kinetics , enzyme , chromatography , biochemistry , materials science , physics , quantum mechanics , composite material
Abstract A kinetic study was conducted on the effect of heating in the temperature range of 75–110 °C on the trypsin inhibition activity of ovomucoid. Heat treatment of isolated ovomucoid resulted in a time‐dependent decrease in trypsin inhibition activity that could accurately be described by a first‐order kinetic model. The magnitude and the temperature dependence of the rate constants was affected by the pH during heat treatment. The heat stability of ovomucoid was the lowest at pH 7.6. Heat treatments intended to decrease the trypsin inhibition activity should therefore be carried out as soon as possible after laying, because the ovomucoid was inactivated faster at the pH of fresh egg white (pH 7.6). The presence of the other egg white constituents decreased the heat stability of ovomucoid compared to that of the model system of ovomucoid in buffer, presumably by the formation of ovomucoid‐lysozyme complexes in the former.