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March 7, 2026Applied Microbiology and BiotechnologyOpen Access

Unveiling a catalytically promiscuous feruloyl esterase from Clostridium acetobutylicum

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Authors

SLShang LiXHXiaowang HuXCXinyu Che

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Overview

Functional characterization reveals a promiscuous enzyme for biomass conversion, indicating significant potential for renewable fuel production.

Key Points

  • The study aims to characterize the biochemical and structural properties of a novel feruloyl esterase from Clostridium acetobutylicum.
  • Functional and crystallographic analysis of CaFaeA enzyme
  • Evaluation of enzyme activity with various substrates including hydroxycinnamate esters
  • Mutagenesis to identify residues influencing substrate access and activity
  • Assessment of enzyme performance in organic solvents
  • CaFaeA shows broad catalytic activity toward multiple substrates, unlike typical carboxyl esterases.
  • The crystal structure reveals a unique lid architecture and a canonical α/β-hydrolase fold.
  • Significant ferulic acid release from insoluble wheat arabinoxylan at a rate of 5.39 mg·μmol<sup>-1</sup>·h<sup>-1</sup>.
  • CaFaeA maintains or enhances activity in the presence of 25% dimethyl sulfoxide and n-hexane.

Cite This Study

Li et al. (2026) studied this question.

synapsesocial.com/papers/69abc0925af8044f7a4e9507https://doi.org/10.1007/s00253-026-13756-7
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