The Ethaline Effect on Feruloyl Esterase Activity

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Feruloyl esterase

Feruloyl esterase forms a part of the enzyme complex that acts collectively and synergistically to completely hydrolyze xylan to its monomers. The enzyme has found potential uses in a wide variety of applications of interest to the agrifood and pharmaceutical industries. This review describes the enzymology of feruloyl esterases involved in xylan degradation. The occurrence of feruloyl esterase...

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Expanding the feruloyl esterase gene family of Aspergillus niger by characterization of a feruloyl esterase, FaeC.

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Regulation of the feruloyl esterase (faeA) gene from Aspergillus niger.

Feruloyl esterases can remove aromatic residues (e.g., ferulic acid) from plant cell wall polysaccharides (xylan, pectin) and are essential for complete degradation of these polysaccharides. Expression of the feruloyl esterase-encoding gene (faeA) from Aspergillus niger depends on D-xylose (expression is mediated by XlnR, the xylanolytic transcriptional activator) and on a second system that re...

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Structure of a feruloyl esterase from Aspergillus niger.

The crystallographic structure of feruloyl esterase from Aspergillus niger has been determined to a resolution of 1.5 A by molecular replacement. The protein has an alpha/beta-hydrolase structure with a Ser-His-Asp catalytic triad; the overall fold of the protein is very similar to that of the fungal lipases. The structure of the enzyme-product complex was determined to a resolution of 1.08 A a...

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Characterization of a feruloyl esterase from Lactobacillus plantarum.

Lactobacillus plantarum is frequently found in the fermentation of plant-derived food products, where hydroxycinnamoyl esters are abundant. L. plantarum WCFS1 cultures were unable to hydrolyze hydroxycinnamoyl esters; however, cell extracts from the strain partially hydrolyze methyl ferulate and methyl p-coumarate. In order to discover whether the protein Lp_0796 is the enzyme responsible for t...

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ژورنال

عنوان ژورنال: Proceedings

سال: 2019

ISSN: 2504-3900

DOI: 10.3390/proceedings2019029107