ESCHERICHIA-COLI JM109 PHBP461, A RECOMBINANT BIOCATALYST FOR THE REGIOSELECTIVE MONOHYDROXYLATION OF ORTHO-SUBSTITUTED PHENOLS TO THEIR CORRESPONDING 3-SUBSTITUTED CATECHOLS

Authors
SCHMID A KOHLER HPE ENGESSER KH
Citation
A. Schmid et al., ESCHERICHIA-COLI JM109 PHBP461, A RECOMBINANT BIOCATALYST FOR THE REGIOSELECTIVE MONOHYDROXYLATION OF ORTHO-SUBSTITUTED PHENOLS TO THEIR CORRESPONDING 3-SUBSTITUTED CATECHOLS, Journal of molecular catalysis. B, Enzymatic, 5(1-4), 1998, pp. 311-316
Citations number
9
Categorie Soggetti
Chemistry Physical
Journal title
Journal of molecular catalysis. B, Enzymatic → ACNP
ISSN journal
13811177
Volume
5
Issue
1-4
Year of publication
1998
Pages
311 - 316
Database
ISI
SICI code
1381-1177(1998)5:1-4<311:EJPARB>2.0.ZU;2-G
Abstract
An expression system for the 2-hydroxybiphenyl-3-monooxygenase gene ( hbpA) from Pseudomonas azelaica HBP1 was developed based on E. coli JM 109 and the high copy vector pUCBM20. The system was used for the conv ersion of 2,2'-dihydroxybiphenyl to 2,2',3-trihydroxybiphenyl on a pre parative scale with a productivity of 0.06 g h(-1) l(-1). This system also allows the biocatalytic production of various 3-aryl-, 3-alkyl-, and 3-halo-substituted catechols. (C) 1998 Elsevier Science B.V. All r ights reserved.