Screening of Biocatalysts for Synthesis of the Wieland–Miescher Ketone

Catalysts

KimberlyA. Kew¹  NathanealT. Green²  MitulP. Patel²  RobertM. Hughes²  JacobK. Burch² 

[1] Department of Biochemistry and Molecular Biology, Brody School of Medicine, East Carolina University, Greenville, NC 27834, USA;Department of Chemistry, East Carolina University, Greenville, NC 27858, USA;

关键词: lipase;    biocatalysis;    Wieland-Miescher ketone;    biocatalyst screening;    amylase;    peptidase;   

DOI  :  10.3390/catal10091063

来源: DOAJ

【 摘 要 】

Lipases, a versatile class of biocatalysts, have been shown to function in non-aqueous media/organic solvents and to possess “promiscuous” catalytic activity for a wide range of organic transformations. In this study, we explored the biocatalytic properties of a library of commercially available lipases by screening them for catalysis of a one-pot synthesis of Wieland–Miescher ketone, an important intermediate in the synthesis of biologically active compounds such as steroids and terpenoids, from methyl vinyl ketone and 2-methyl-1,3-cyclohexanedione. As a direct outgrowth of this screen, we created an optimized procedure for Wieland–Miescher ketone (WMK) synthesis using crude lipase preparations, characterizing both reaction yield and enantiomeric excess. We also identified principal components of the crude lipase mixture through proteomics and present evidence for a non-lipolytic origin of the observed catalysis. Finally, using the optimized conditions developed in this study, we propose a general absorbance-based screening methodology for assessing biocatalytic potential of crude enzyme preparations for synthesis of WMK.

【 授权许可】

Unknown