| pubmed-article:6805183 | pubmed:abstractText | 1. Penicillin amidase from Proteus rettgeri was purified 580-fold by a four-step chromatographic procedure. Titration with phenylmethanesulphonyl fluoride showed that the purified preparation contains 53% of the enzyme. 2. The molecular weight of the amidase was found to be 65.000. The enzyme is strongly inhibited by N-bromosuccinimide and zinc ions. It hydrolyses penicillins, cephalosporins and some synthetic substrates, and in addition it catalyses synthesis of ampicillin from methyl ester of phenylglycine and 6-aminopenicillanic acid. 3. The immobilized amidase obtained by copolymerization of the chemically modified enzyme with acrylamide was applied for preparative hydrolysis of benzylpenicillin. | lld:pubmed |
