Several penicillin-producing fungi were examined for ability to produce 6-aminopenicillanic acid (6-APA) and penicillin acylase. 6-APA was found in corn steep liquor fermentations of Trichophyton mentagrophytes, Aspergillus ochraceous, and three strains of Penicillium sp. 6-APA was not detected in fermentations of Epidermophyton floccosum although penicillins were produced. 6-APA formed a large...

Penicillin G acylase is an important enzyme in the commercial production of semisynthetic penicillins used to combat bacterial infections. Mutant strains of Providencia rettgeri were generated from wild-type cultures subjected to nutritional selective pressure. One such mutant, Bro1, was able to use 6-bromohexanamide as its sole nitrogen source. Penicillin acylase from the Bro1 strain exhibited...

penicillin acylase (ec 3.5.1.11) has been a target of study for a long time because of its pivotal role in the deacylation of the penicillin into the 6- aminopenicillanic acid (6-apa) and the side-chain organic acids. this property of penicillin acylase has been exploited commercially for large scale production of 6-apa, which is the key intermediate in the manufacture of semi-synthetic penicil...

Penicillin acylase (EC 3.5.1.11) has been a target of study for a long time because of its pivotal role in the deacylation of the penicillin into the 6- aminopenicillanic acid (6-APA) and the side-chain organic acids. This property of penicillin acylase has been exploited commercially for large scale production of 6-APA, which is the key intermediate in the manufacture of semi-synthetic penicil...

A new screening method for bacteria capable of producing penicillin acylase is described. The method is based on the use of Serratia marcescens sensitive to 6-aminopenicillanic acid but comparatively resistant to benzylpenicillin. It is simple, quite specific, and requires no special equipment. It can also be used to screen for phenoxymethylpenicillin acylase activity. We also suggest an acidim...

Aculeacin A acylase from Actinoplanes utahensis produced by Streptomyces lividans revealed acylase activities that are able to hydrolyze penicillin V and several natural aliphatic penicillins. Penicillin K was the best substrate, showing a catalytic efficiency of 34.79 mM(-1) s(-1). Furthermore, aculeacin A acylase was highly thermostable, with a midpoint transition temperature of 81.5 degrees C.

Penicillin acylase (EC 3.5.1.11) has been a target of study for a long time because of its pivotal role in the deacylation of the penicillin into the 6aminopenicillanic acid (6-APA) and the side-chain organic acids. This property of penicillin acylase has been exploited commercially for large scale production of 6-APA, which is the key intermediate in the manufacture of semi-synthetic penicilli...

Alcaligenes faecalis penicillin G acylase is more stable than the Escherichia coli enzyme. The activity of the A. faecalis enzyme was not affected by incubation at 50 degrees C for 20 min, whereas more than 50% of the E. coli enzyme was irreversibly inactivated by the same treatment. To study the molecular basis of this higher stability, the A. faecalis enzyme was isolated and its gene was clon...

Penicillin G acylase from E. coli TA1 was immobilized by Cross-Linked Enzyme Aggregates (CLEA), a new method for immobilization. This biocatalyst and commercial immobilized penicillin G acylase (PGA-450) were used to study the effect of pH, temperature and substrate concentration on the synthesis of ampicillin from phenyl glycine methyl ester (PGME) and 6-aminopenicillanic acid (6-APA). Compare...

Penicillin G acylase from E. coli TA1 was immobilized by Cross-Linked Enzyme Aggregates (CLEA), a new method for immobilization. This biocatalyst and commercial immobilized penicillin G acylase (PGA-450) were used to study the effect of pH, temperature and substrate concentration on the synthesis of ampicillin from phenyl glycine methyl ester (PGME) and 6-aminopenicillanic acid (6-APA). Compare...