Trypsin inhibition activity of heat-denatured ovomucoid: a kinetic study.
A kinetic study was conducted on the effect of heating in the temperature range of 75-110 degrees 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.
Van der Plancken
Iesel
I
Laboratory of Food Technology, Department of Food and Microbial Technology, Faculty of Agricultural and Applied Biological Sciences, Katholieke Universiteit Leuven, Kasteelpark Arenberg 22, B-3001 Heverlee, Belgium.
Van Remoortere
Marijke
M
Van Loey
Ann
A
Hendrickx
Marc E
ME
D004789:Enzyme Activation / Q000528:radiation effects; D004795:Enzyme Stability / Q000528:radiation effects; D006358:Hot Temperature; D007700:Kinetics; D010059:Ovomucin / Q000737:chemistry* / Q000528:radiation effects*; D011489:Protein Denaturation; D013696:Temperature; D014357:Trypsin / Q000737:chemistry*; D014361:Trypsin Inhibitors / Q000737:chemistry* / Q000528:radiation effects*
D014361:Trypsin Inhibitors; D010059:Ovomucin; D014357:Trypsin