Enzyme catalysis in the presence of nonaqueous solvents using chloroperoxidase

✍ Scribed by Charles L. Cooney; John Hueter

• Publisher: John Wiley and Sons
• Year: 1974
• Tongue: English
• Weight: 450 KB
• Volume: 16
• Category: Article
• ISSN: 0006-3592
• DOI: 10.1002/bit.260160805

✦ Synopsis

Abstract

Studies exploring the effect of two nonaqueous solvents on enzyme activity were done using chloroperoxidase as a model system. Chloroperoxidase produced by Caldariomyces fumago is a bifunctional enzyme with halogenating activity at pH 3 and peroxidation activity at pH 5 to 6. Methanol affected both of these activities similarly. Furthermore, methanol and the halogen acceptor, monochlorodimedon, competitively inhibit the reaction. These results are discussed in terms of the site of action of methanol. At 10% methanol concentration, the enzyme retained up to 33% of its activity depending on the monochlorodimedon concentration. Dimethylsulfoxide at 10% concentration permitted up to 47% retention of activity. Its effects on the enzyme are more complex than methanol and are discussed in terms of a transitory inactivation of the enzyme.