Abstract:
:We isolated a eugenol-degrading bacterium, Pseudomonas fluorescens E118. This strain produced a novel enzyme, eugenol dehydrogenase, which catalyzes the conversion of eugenol into coniferyl alcohol. The enzyme was purified from the eugenol-induced cells of P. fluorescens E118. The purified enzyme appeared to be homogeneous, judging from the analysis of polyacrylamide gel electrophoresis. The enzyme was a 68-kDa protein composed of two different subunits (alpha subunit, 10 kDa; and beta subunit, 58 kDa). The enzyme exhibited a cytochrome c-like absorption spectrum. The alpha subunit corresponded to cytochrome c. The enzyme catalyzed the dehydrogenation of 4-alkylphenol into the corresponding alkyl 1-(4-hydroxyphenyl)-alcohol derivatives. The reaction products were isolated and identified physicochemically. The enzyme catalyzed the enantioselective hydroxylation of p-alkylphenols. p-Ethylphenol and p-propylphenol were converted to S-(-)-p-(1-hydroxyphenyl)ethanol and S-(-)-p(1-hydroxyphenyl)propanol, respectively.
journal_name
Ann N Y Acad Scijournal_title
Annals of the New York Academy of Sciencesauthors
Furukawa H,Nagasawa Tdoi
10.1111/j.1749-6632.1998.tb10290.xsubject
Has Abstractpub_date
1998-12-13 00:00:00pages
81-6eissn
0077-8923issn
1749-6632journal_volume
864pub_type
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