The feruloyl esterase system of Talaromyces stipitatus: determining the hydrolytic and synthetic specificity of TsFaeC.

@article{Vafiadi2006TheFE,
  title={The feruloyl esterase system of Talaromyces stipitatus: determining the hydrolytic and synthetic specificity of TsFaeC.},
  author={Christina Vafiadi and Evangelos Topakas and Paul Christakopoulos and Craig B Faulds},
  journal={Journal of biotechnology},
  year={2006},
  volume={125 2},
  pages={
          210-21
        }
}
The active site of the recombinant Talaromyces stipitatus type-C feruloyl esterase (TsFaeC) was probed using a series of C1-C4 alkyl ferulates and methyl esters of phenylalkanoic and cinnamic acids. The enzyme was active on 23 of the 34 substrates tested. Lengthening or shortening the aliphatic side chain while maintaining the same aromatic substitutions completely abolished the enzyme activity. Maintaining the phenylpropenoate structure but altering the substitutions of the aromatic ring… CONTINUE READING

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