Enzymatic synthesis of cephalexin and cefaclor with the use of immobilized aminocephalosporin synthetase from Xanthomonas sp. as a biocatalyst was studied. The employment of a mathematical model based on the acyl-enzyme mechanism of the biocatalyst action was shown possible for the quantitative description of the antibiotic syntheses. A relationship providing determination of the complex of the physico-chemical investigations required for the enzymatic synthesis design was suggested. Kinetic and thermodynamic parameters of the processes were evaluated and the ratios of the maximum conversion of the key amino acids and the initial concentrations of the substrate and nucleophile were calculated. The regions of the model fit to the experimental data within a wide range of the substrate and nucleophile concentrations were defined. The technology for the enzymatic synthesis of aminocephalosporins exemplified by cephalexin and cefaclor was designed.

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