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Title 

The analysis and application of a recombinant monooxygenase library as a biocatalyst for the Baeyer-Villiger reaction

 

Recombinant monooxygenase library의 분석 및 응용

Authors 

J ParkD KimSuJin KimJinhee KimK BaeC Lee

Publisher 

The Korean Society for Applied Microbiology

Issue Date 

2007

Citation 

Journal of Microbiology and Biotechnology, vol. 17, no. 7, pp. 1083-1089

Keywords 

baeyer-Villiger oxidationbiocatalysisGC-MSmonooxygenasesulfide oxidation2 oxabicyclo[3.3.0]oct 6 en 2 one3 oxabicyclo[3.3.0]oct 6 en 2 oneoxidoreductaserecombinant enzymethioanisole

Abstract 

Because of their selectivity and catalytic efficiency, BVMOs are highly valuable biocatalysts for the chemoenzymatic synthesis of a broad range of useful compounds. In this study, we investigated the microbial Baeyer-Villiger oxidation and sulfoxidation of thioanisole and bicyclo[3.2.0]hept-2-en-6-one using whole Escherichia coli cells that recombined with each of the Baeyer-Villiger monooxygenases originated from Pseudomonas aeruginosa PAO1 and two from Streptomyces coelicolor A3(2). The three BVMOs were identified in the microbial genome database by a recently described protein sequence motif; e.g., BVMO motif (FXGXXXHXXXW). The reaction products were identified as (R)-/ (S)-sulfoxide and 2-oxabicyclo/3-oxabicyclo[3.3.0]oct-6-en-2-one by GC-MS analysis. Consequently, this study demonstrated that the three enzymes can indeed catalyze the Baeyer-Villiger reaction as a biocatalyst, and effective annotation tools can be efficiently exploited as a source of novel BVMOs.

ISSN 

1017-7825

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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