Abstract
Cephalosporin C acetyl-hydrolase, which had not yet been found in Cephalosporium acremonium cultures, was partially purified from the culture fluid of the mutant No. 81 by ammonium sulfate fractionation, dialysis and DEAE-cellulose column chromatography. The optimum pH and temperature of the enzyme reaction were found to be about 8.0 and 50°C, respectively. The enzyme activity was hardly affected by Mg2+, Mn2+, Zn2+, Co2+, Ni2+, Na+, K+, EDTA, PCMB and 2, 4-dinitrophenol, but markedly inhibited by diisopropylfluoro-phosphate at 1mM. The product formed from cephalosporin C by the enzyme reaction was proved to be deacetylcephalosporin C by physical and chemical analyses and chromatographic behaviors.
