The Crystal Structure of Feruloyl Esterase A from Aspergillus niger Suggests Evolutive Functional Convergence in Feruloyl Esterase Family

ABSTRACT 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) fromAspergillus niger depends on d-xylose (expression is mediated by XlnR, the xylanolytic transcriptional activator) and on a second system that responds to aromatic compounds with a defined ring structure, such as ferulic acid and vanillic acid. Several compounds were tested, and all of the inducing compounds contained a benzene ring which had a methoxy group at C-3 and a hydroxy group at C-4 but was not substituted at C-5. Various aliphatic groups occurred at C-1. faeA expression in the presence of xylose or ferulic acid was repressed by glucose. faeA expression in the presence of ferulic acid and xylose was greater thanfaeA expression in the presence of either compound alone. The various inducing systems allow A. niger to produce feruloyl esterase not only during growth on xylan but also during growth on other ferulic acid-containing cell wall polysaccharides, such as pectin.

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Production of a chimeric enzyme tool associating the Trichoderma reesei swollenin with the Aspergillus niger feruloyl esterase A for release of ferulic acid

Applied Microbiology and Biotechnology ◽

10.1007/s00253-006-0546-8 ◽

2006 ◽

Vol 73 (4) ◽

pp. 872-880 ◽

Cited By ~ 34

Author(s):

Anthony Levasseur ◽

Markku Saloheimo ◽

David Navarro ◽

Martina Andberg ◽

Frédéric Monot ◽

...

Keyword(s):

Aspergillus Niger ◽

Ferulic Acid ◽

Trichoderma Reesei ◽

Feruloyl Esterase ◽

Chimeric Enzyme

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Multiple amino acid substitutions significantly improve the thermostability of feruloyl esterase A from Aspergillus niger

Bioresource Technology ◽

10.1016/j.biortech.2012.04.042 ◽

2012 ◽

Vol 117 ◽

pp. 140-147 ◽

Cited By ~ 30

Author(s):

Shuai-Bing Zhang ◽

Xiao-Qiong Pei ◽

Zhong-Liu Wu

Keyword(s):

Amino Acid ◽

Aspergillus Niger ◽

Feruloyl Esterase ◽

Amino Acid Substitutions ◽

Multiple Amino Acid

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Regioselective chemo-enzymatic syntheses of ferulate conjugates as chromogenic substrates for feruloyl esterases

10.3762/bxiv.2020.107.v1 ◽

2020 ◽

Author(s):

Olga Gherbovet ◽

Fernando Ferreira ◽

Apolline Clément ◽

Mélanie Ragon ◽

Julien Durand ◽

...

Keyword(s):

Aspergillus Niger ◽

Feruloyl Esterase ◽

Thermomyces Lanuginosus ◽

Hydroxyl Group ◽

Chromogenic Substrates ◽

Carbohydrate Active Enzymes ◽

Experimental Application ◽

Synthetic Routes ◽

Feruloyl Esterases ◽

Regioselective Functionalization

Generally, carbohydrate-active enzymes are studied using chromogenic substrates that provide quick and easy color-based detection of enzyme-mediated hydrolysis. In the case of feruloyl esterases, commercially available chromogenic ferulate derivatives are both costly and limited in terms of their experimental application. In this study, we describe solutions for these two issues, using a chemoenzymatic approach to synthesize different ferulate compounds. The overall synthetic routes towards commercially available 5-bromo-4-chloro-3-indolyl and 4-nitrophenyl O-5-feruloyl-α-l-arabinofuranosides 1a and 1b were significantly shortened (7-8 steps reduced to 4-6) and transesterification yields enhanced (from 46 to 73% for 1a and 47 to 86 % for 1b). This was achieved using enzymatic (immobilized Lipolase 100T from Thermomyces lanuginosus) transesterification of unprotected vinyl ferulate to the primary hydroxyl group of α‐l‐arabinofuranosides. Moreover, a novel feruloylated-butanetriol 4-nitrocatechol-1-yl analog 12, containing a cleavable hydroxylated linker was also synthesized in 29% overall yield in 3 steps (convergent synthesis). The latter route combined regioselective functionalization of 4-nitrocatechol and enzymatic transferuloylation. The use of 12 as a substrate to characterize type A feruloyl esterase from Aspergillus niger reveals the advantages of this substrate for the characterizations of feruloyl esterases.

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