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Appl Environ Microbiol. 1971 May; 21(5): 907-915
Copyright © 1971 American Society for Microbiology. All Rights Reserved.

Arylamidase of Cephalosporium acremonium and Its Specificity for Cephalosporin C

Antibiotic Manufacturing and Development Division, Eli Lilly and Company, Indianapolis, Indiana 46206

ABSTRACT

Three aggregational forms of arylamidase are produced by Cephalosporium acremonium. The exocellular enzyme, with an approximate molecular weight of 60,000, was purified 300-fold by diethylaminoethyl cellulose chromatography, gel filtration, and gel electrophoresis. With L-leucyl-ß-naphthylamide as the substrate, the K_m is 4.2 x 10^–4M; the optimum pH, 7.7; and the temperature optimum, 35 C. The enzymatic hydrolysis of L-leucyl-ß-naphthylamide is inhibited by a number of cephalosporins, whereas a variety of penicillins show no effect. Alternatively, the enzyme specifically catalyzes the ß-lactam hydrolysis of a number of cephalosporins; a number of penicillins are resistant. The K_m for cephalosporin C is 9.09 x 10^–4M.