Inactivation of Lysozyme By Alkylperoxyl Radicals

Abstract

Thermolysis of 2, 2′-azo-bis-(2-amidinopropane) under air in the presence of lysozyme leads to extensive inactivation of the enzyme. The number of inactivated enzyme molecules per radical produced increases with the enzyme concentration up to values considerably larger than one. Enzyme inacitivation is accompanied by extensive tryptophan modification. Over the enzyme concentration range considered (1.7 to 130μM) nearly 4 tryptophan groups are modified per enzyme molecule inactivated. Both the inactivation and tryptophan modification are prevented by micromolar concentrations of propyl gallate. The results are interpreted in terms of an efficient inactivation of the enzyme by the alkylperoxyl radicals generated by thermolysis of the azocompound.

Key Words:

• Lysozyme inactivation
• alkylperoxyl radicals
• tryptophan modification
• 2 2′-azo-bis-(2-amidinopropane)