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

Feruloyl esterase from Alternaria tenuissima that hydrolyses lignocellulosic material to release... 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 (K M) and catalytic efficiencies (k cat/K M) were determined for typical substrates of feruloyl esterase, and the lowest K M of 50.6 μM (i.e., the highest affinity) and the highest k cat/K M (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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Applied Biochemistry and Microbiology Springer Journals

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

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References (2)

Publisher
Springer Journals
Copyright
Copyright © 2017 by Pleiades Publishing, Inc.
Subject
Life Sciences; Biochemistry, general; Microbiology; Medical Microbiology
ISSN
0003-6838
eISSN
1608-3024
DOI
10.1134/S0003683817060047
Publisher site
See Article on Publisher Site

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 (K M) and catalytic efficiencies (k cat/K M) were determined for typical substrates of feruloyl esterase, and the lowest K M of 50.6 μM (i.e., the highest affinity) and the highest k cat/K M (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.

Journal

Applied Biochemistry and Microbiology – Springer Journals

Published: Nov 23, 2017

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