Cell aggregates ofEscherichia coli with benzylpenicillin amidase activity |
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Authors: | R Zeman V Vojtí?ek |
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Institution: | (1) Research Institute of Antibiotics and Biotransformations, 252 63 Roztoky near Prague, Czechoslovakia;(2) Institute of Microbiology, Czechoslovak Academy of Sciences, 142 20 Prague 4 |
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Abstract: | Intact cellsEscherichia 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%. |
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