Cell aggregates of Escherichia coli with benzylpenicillin amidase activity.
Intact cells Escherichia coli CCM 2843, exhibiting substantial benzylpenicillin amidase activity, were bound mutually with supporting waste microbial cells, native or treated, to obtain an inexpensive biocatalyst for the production of 6-aminopenicillanic acid (6-APA). The bond was effected by glutaraldehyde (GA) and Sedipur CL-930 (PEI), without any carrier. The optimal concentration of GA was 2%, that of PEI 1%. The optimal biocatalyst was obtained by immobilization of productive cells with their fragments at a mass ratio of 4:1. The cell aggregates were used for hydrolysis of potassium benzyl-penicillin at a concentration of 5% to 6-APA. After 25 repeated batch conversions the degree of conversion did not decrease; its average value was 96.4%.
Zeman
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Research Institute of Antibiotics and Biotransformations, Roztoky near Prague, Czechoslovakia.
Vojtísek
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D001422:Bacterial Adhesion; D004926:Escherichia coli / Q000201:enzymology*; D010399:Penicillin Amidase / Q000378:metabolism*
D010399:Penicillin Amidase