Articles

The mechanisms of irreversible enzyme inactivation at 100C

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Science  14 Jun 1985:
Vol. 228, Issue 4705, pp. 1280-1284
DOI: 10.1126/science.4001942

Abstract

The mechanism of irreversible thermoinactivation of an enzyme has been quantitatively elucidated in the pH range relevant to enzymatic catalysis. The processes causing irreversible inactivation of hen egg-white lysozyme at 100 degrees C are deamidation of asparagine residues, hydrolysis of peptide bonds at aspartic acid residues., destruction of disulfide bonds, and formation of incorrect (scrambled) structures; their relative contributions depend of the pH.