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Science 14 June 1985:
Vol. 228. no. 4705, pp. 1280 - 1284
DOI: 10.1126/science.4001942
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Articles

Science, Vol 228, Issue 4705, 1280-1284
Copyright © 1985 by American Association for the Advancement of Science

articles

The mechanisms of irreversible enzyme inactivation at 100C

TJ Ahern and AM Klibanov

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.


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Antibody-catalyzed rearrangement of the peptide bond.
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