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Functional characterization of CYP52G3 from Aspergillus oryzae and its application for bioconversion and synthesis of hydroxyl flavanone and steroids
Author(s) -
Uno Tomohide,
Yanase Takeshi,
Imaishi Hiromasa
Publication year - 2016
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1002/bab.1496
Subject(s) - flavanone , bioconversion , aspergillus oryzae , biochemistry , chemistry , enzyme , escherichia coli , biotransformation , cytochrome p450 , fermentation , recombinant dna , flavonoid , gene , antioxidant
Abstract Aspergillus oryzae is a fungus widely used in traditional Japanese fermentation industries. Cytochrome P450 (CYP) proteins are ubiquitously distributed in nature and display a broad range of enzymatic activities. A novel CYP52 (CYP52G3) gene was found in A. oryzae . In this study, we report the functional characterization of CYP52G3. The recombinant protein was expressed heterologously in Escherichia coli , and its membrane fraction isolated. CYP52G3 showed activities for 7‐ethoxycoumarin and α‐naphtoflavone. Furthermore, CYP52G3 hydroxylated flavanone at the 4′ and 6 position and metabolized some hydroxyl‐flavanones and steroids. Bioconversion experiments indicated that CYP52G3 could convert flavanone and testosterone in a synthetic medium. The conversion rates of flavanone and testosterone at 24 H were 50% and 70%, respectively. These results support that CYP52G3 could prove a useful enzyme for the efficient production of new compounds from flavonoids and steroids.