Abstract
Recombinant, as well as native alpha-amino acid ester hydrolase from Xanthomonas rubrilineans VKPM B-9915 (XrAEH, EC 3.1.1.43), was tested for synthesis of amino-beta-lactam antibiotic cephalexin. It was shown that the recombinant enzyme r-XrAEH produced by Escherichia coli VKPM B-11246 is more efficient in comparison with the native enzyme wt-XrAEH prepared from mutant strain Xanthomonas rubrilineans VKPM B-9915. When r-XrAEH was used as a biocatalyst, addition of ethylene glycol (33 vol %) to the reaction medium improved the yield from 70 to 95%. During synthesis of cephalexin under optimal conditions in the case of the native enzyme wt-XrAEH the cephalexin yield was 85%, in contrast to r-XrAEH where it was 95%. Furthermore, unlike native wt-XrAEH enzymes, preparations of recombinant r-XrAEH do not possess beta-lactamase side activity.
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Original Russian Text © A.V. Sklyarenko, O.V. Berezina, D.E. Satarova, V.V. Fedorchuk, E.A. Fedorchuk, S.S. Savin, S.V. Yarotsky, V.I. Tishkov, 2014, published in Vestnik Moskovskogo Universiteta. Khimiya, 2014, No. 2, pp. 86–92.
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Sklyarenko, A.V., Berezina, O.V., Satarova, D.E. et al. Recombinant alpha-amino ester acid hydrolase from Xanthomonas rubrilineans VKPM B-9915 is a highly efficient biocatalyst of cephalexin synthesis. Moscow Univ. Chem. Bull. 69, 62–67 (2014). https://doi.org/10.3103/S0027131414020084
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DOI: https://doi.org/10.3103/S0027131414020084