NDLI: Expression and bioconversion of recombinant m- and p-hydroxybenzoate hydroxylases from a novel moderate halophile, Chromohalobacter sp.

Content Provider	Springer Nature Link
Author	Kim, Wonduck Park, Yu Ri Im, Seonghun Kim, Dockyu Kim, Si Wouk
Copyright Year	2012
Abstract	p-Hydroxybenzoate hydroxylase (pobA) and m-hydroxybenzoate hydroxylase (mobA) genes, from the moderate halophile Chromohalobacter sp. HS-2, were expressed and characterized. Solubilities of overexpressed recombinant MobA and PobA were enhanced by the induction of the heat-shock proteins DnaJ and DnaK. Each MobA and PobA maintained stable activity under high NaCl concentrations. V max and K m values for MobA with m-hydroxybenzoate were 70 μmol min−1 mg−1 protein and 81 μM, respectively. Similarly, those of PobA with p-hydroxybenzoate as substrate were 5 μmol min−1 mg−1 protein and 129 μM, respectively. The Escherichia coli expression system, including induction of heat shock proteins, was used to convert hydroxybenzoates into protocatechuate (3,4-dihydroxybenzoate) and revealed that resting cells harboring mobA converted 15 mM m-hydroxybenzoate to 15 mM protocatechuate while those harboring pobA converted 50 mM p-hydroxybenzoate to 35 mM protocatechuate at 30 °C, respectively.
Starting Page	1687
Ending Page	1692
Page Count	6
File Format	PDF
ISSN	01415492
Journal	Biotechnology Letters
Volume Number	34
Issue Number	9
e-ISSN	15736776
Language	English
Publisher	Springer Netherlands
Publisher Date	2012-05-22
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Bioconversion Chromohalobacter sp. HS-2 m-Hydroxybenzoate hydroxylase p-Hydroxybenzoate hydroxylase Protocatechuate Biotechnology Applied Microbiology Biochemistry Microbiology
Content Type	Text
Resource Type	Article
Subject	Medicine Bioengineering Applied Microbiology and Biotechnology Biotechnology

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