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Optimized Enzymatic Synthesis of Feruloyl Derivatives Catalyzed by Three Novel Feruloyl Esterases from Talaromyces wortmannii in Detergentless Microemulsions.


ABSTRACT: Three novel feruloyl esterases (Fae125, Fae7262 and Fae68) from Talaromyces wortmannii overexpressed in the C1 platform were evaluated for the transesterification of vinyl ferulate with two acceptors of different size and lipophilicity (prenol and L-arabinose) in detergentless microemulsions. The effect of reaction conditions such as the microemulsion composition, the substrate concentration, the enzyme load, the pH, the temperature and the agitation were investigated. The type A Fae125 belonging to the subfamily 5 (SF5) of phylogenetic classification showed highest yields for the synthesis of both products after optimization of reaction conditions: 81.8% for prenyl ferulate and 33.0% for L-arabinose ferulate. After optimization, an 8-fold increase in the yield and a 12-fold increase in selectivity were achieved for the synthesis of prenyl ferulate.

SUBMITTER: Antonopoulou I 

PROVIDER: S-EPMC6197793 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature

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Optimized Enzymatic Synthesis of Feruloyl Derivatives Catalyzed by Three Novel Feruloyl Esterases from <i>Talaromyces wortmannii</i> in Detergentless Microemulsions.

Antonopoulou Io I   Iancu Laura L   Jütten Peter P   Piechot Alexander A   Rova Ulrika U   Christakopoulos Paul P  

Computational and structural biotechnology journal 20181005


Three novel feruloyl esterases (Fae125, Fae7262 and Fae68) from <i>Talaromyces wortmannii</i> overexpressed in the C1 platform were evaluated for the transesterification of vinyl ferulate with two acceptors of different size and lipophilicity (prenol and L-arabinose) in detergentless microemulsions. The effect of reaction conditions such as the microemulsion composition, the substrate concentration, the enzyme load, the pH, the temperature and the agitation were investigated. The type A Fae125 b  ...[more]

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