Recombinant alpha-amino ester acid hydrolase from Xanthomonas rubrilineans VKPM B-9915 is a highly efficient biocatalyst of cephalexin synthesis
| Autor: | O. V. Berezina, S. V. Yarotsky, E. A. Fedorchuk, Vladimir I. Tishkov, A. V. Sklyarenko, V. V. Fedorchuk, S. S. Savin, D. E. Satarova |
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| Rok vydání: | 2014 |
| Předmět: |
chemistry.chemical_classification
biology medicine.drug_class Antibiotics General Chemistry medicine.disease_cause law.invention chemistry.chemical_compound Enzyme chemistry Biochemistry Biocatalysis law Yield (chemistry) Recombinant DNA medicine biology.protein Ethylene glycol Escherichia coli Acid hydrolase |
| Zdroj: | Moscow University Chemistry Bulletin. 69:62-67 |
| ISSN: | 1935-0260 0027-1314 |
| DOI: | 10.3103/s0027131414020084 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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