Feruloyl esterase from Alternaria tenuissima that hydrolyses lignocellulosic material to release hydroxycinnamic acids

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ID: 260962
2017
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Abstract
An extracellular feruloyl esterase from the culture filtrates of the isolated fungus Alternaria tenuissima was successfully purified to apparent homogeneity by anion-exchange and size-exclusion chromatography. Peptide fragments of purified enzyme (designated as AltFAE; molecular weight of 30.3 kDa determined by SDS-PAGE) were identified by mass spectrometry using a NanoLC-ESI-MS/MS system. Michaelis-Menten constants (KM) and catalytic efficiencies (kcat/KM) were determined for typical substrates of feruloyl esterase, and the lowest KM of 50.6 μM (i.e., the highest affinity) and the highest kcat/KM (3.1 × 105 s—1 M–1) were observed for methyl p-coumarate and methyl ferulate, respectively. Not least, AltFAE catalyzed conversion of lignocellulosic material (e.g. wood meal) to release hydroxycinnamic products, i.e. ferulic- and p-coumaric acids.
Reference Key
chi2017appliedferuloyl Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors D. H. Chi;V. D. Giap;L. P. H. Anh;D. H. Nghi;D. H. Chi;V. D. Giap;L. P. H. Anh;D. H. Nghi;
Journal applied biochemistry and microbiology
Year 2017
DOI
doi:10.1134/S0003683817060047
URL
https://link.springer.com/article/10.1134/S0003683817060047
Keywords
Microbiology biochemistry medical microbiology general

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