Maintenance of penicillin G acylase expression by B. megaterium: preservation methods and activity recovery

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MAINTENANCE OF PENICILLIN G ACYLASE EXPRESSION BY B. megaterium: PRESERVATION METHODS AND ACTIVITY RECOVERY

This work reports the influence of different culture preservation methods on the production of penicillin G acylase (PGA) by Bacillus megaterium ATCC 14945. The initial stock culture, presenting PGA activity of 97 IU l, was preserved for two years using different procedures: monthly subculturing and storage in refrigerator (S), freeze-drying using skim milk 10%, plus inositol 5% as cryoprotecto...

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Improved X-ray diffraction from Bacillus megaterium penicillin G acylase crystals through long cryosoaking dehydration.

Penicillin G acylase from Bacillus megaterium (BmPGA) is currently used in the pharmaceutical industry as an alternative to PGA from Escherichia coli (EcPGA) for the hydrolysis of penicillin G to produce 6-aminopenicillanic acid (6-APA), a penam nucleus for semisynthetic penicillins. Despite the significant differences in amino-acid sequence between PGAs from Gram-positive and Gram-negative bac...

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Optimization of Enzymatic Synthesis of Ampicillin Using Cross-Linked Aggregates of Penicillin G Acylase

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...

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Optimization of Enzymatic Synthesis of Ampicillin Using Cross-Linked Aggregates of Penicillin G Acylase

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...

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Isolation of a Penicillin Acylase Producing E.coli and Kinetic Characterization of the Whole Cell Enzyme Activity

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...

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ژورنال

عنوان ژورنال: Brazilian Journal of Chemical Engineering

سال: 2007

ISSN: 0104-6632

DOI: 10.1590/s0104-66322007000300001