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Cloning, expression and characterization of an aryl-alcohol... » Isaúde
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BMC microbiology [electronic resource]
2012-06-29 03:29:27

Cloning, expression and characterization of an aryl-alcohol dehydrogenase from the white-rot fungus Phanerochaete chrysosporium strain BKM-F-1767

Descrição: Background:The white-rot fungus Phanerochaete chrysosporium is among the small group of fungi thatcan degrade lignin to carbon dioxide while leaving the crystalline cellulose untouched. Theefficient lignin oxidation system of this fungus requires cyclic redox reactions involving thereduction of aryl-aldehydes to the corresponding alcohols by aryl-alcohol dehydrogenase.However, the biochemical properties of this enzyme have not been extensively studied. Theseare of most interest for the design of metabolic engineering/synthetic biology strategies in thefield of biotechnological applications of this enzyme.Results:We report here the cloning of an aryl-alcohol dehydrogenase cDNA from the white-rotfungus Phanerochaete chrysosporium, its expression in Escherichia coli and the biochemicalcharacterization of the encoded GST and His6 tagged protein. The purified recombinantenzyme showed optimal activity at 37 degreesC and at pH 6.4 for the reduction of aryl- and linearaldehydes with NADPH as coenzyme. NADH could also be the electron donor, while havinga higher Km (220 muM) compared to that of NADPH (39 muM). The purified recombinantenzyme was found to be active in the reduction of more than 20 different aryl- and linearaldehydes showing highest specificity for mono- and dimethoxylated Benzaldehyde at positions 3, 4, 3,4 and 3,5. The enzyme was also capable of oxidizing aryl-alcohols withNADP + at 30degreesC and an optimum pH of 10.3 but with 15 to 100-fold lower catalyticefficiency than for the reduction reaction.Conclusions:In this work, we have characterized the biochemical properties of an aryl-alcoholdehydrogenase from the white-rot fungus Phanerochaete chrysosporium. We show that thisenzyme functions in the reductive sense under physiological conditions and that it displaysrelatively large substrate

Identificador: doi:10.1186/1471-2180-12-126
Volume: 0
Página: 1 a

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