scholarly journals A Two-Step Bioconversion Process for Canolol Production from Rapeseed Meal Combining an Aspergillus niger Feruloyl Esterase and the Fungus Neolentinus lepideus

2017 ◽  
Vol 5 (4) ◽  
pp. 67 ◽  
Author(s):  
Elise Odinot ◽  
Frédéric Fine ◽  
Jean-Claude Sigoillot ◽  
David Navarro ◽  
Oscar Laguna ◽  
...  
Keyword(s):  
Aspergillus Niger ◽  
Rapeseed Meal ◽  
Feruloyl Esterase ◽  
Neolentinus Lepideus

Probing the determinants of substrate specificity of a feruloyl esterase, AnFaeA, from Aspergillus niger

FEBS Journal ◽  
2005 ◽  
Vol 272 (17) ◽  
pp. 4362-4371 ◽  
Author(s):  
Craig B. Faulds ◽  
Rafael Molina ◽  
Ramon Gonzalez ◽  
Fiona Husband ◽  
Nathalie Juge ◽  
...  
Keyword(s):  
Aspergillus Niger ◽  
Substrate Specificity ◽  
Feruloyl Esterase

scholarly journals Regulation of the Feruloyl Esterase (faeA) Gene from Aspergillus niger

1999 ◽  
Vol 65 (12) ◽  
pp. 5500-5503 ◽  
Author(s):  
Ronald P. de Vries ◽  
Jaap Visser
Keyword(s):  
Cell Wall ◽  
Aspergillus Niger ◽  
Ferulic Acid ◽  
Methoxy Group ◽  
Plant Cell Wall ◽  
Ring Structure ◽  
Feruloyl Esterase ◽  
Cell Wall Polysaccharides ◽  
Aromatic Residues ◽  
Encoding Gene

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.

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

2006 ◽  
Vol 73 (4) ◽  
pp. 872-880 ◽  
Author(s):  
Anthony Levasseur ◽  
Markku Saloheimo ◽  
David Navarro ◽  
Martina Andberg ◽  
Frédéric Monot ◽  
...  
Keyword(s):  
Aspergillus Niger ◽  
Ferulic Acid ◽  
Trichoderma Reesei ◽  
Feruloyl Esterase ◽  
Chimeric Enzyme

Amino acid, phosphorus, and energy digestibility of Aspergillus niger fermented rapeseed meal fed to growing pigs1

2015 ◽  
Vol 93 (6) ◽  
pp. 2916-2925 ◽  
Author(s):  
C. Shi ◽  
J. He ◽  
J. Yu ◽  
B. Yu ◽  
X. Mao ◽  
...  
Keyword(s):  
Amino Acid ◽  
Aspergillus Niger ◽  
Rapeseed Meal

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

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.

Feruloyl esterase from Aspergillus niger

2002 ◽  
Vol 38 (5) ◽  
pp. 685-691 ◽  
Author(s):  
Michèle Asther ◽  
Mireille Haon ◽  
Sevastianos Roussos ◽  
Eric Record ◽  
Michel Delattre ◽  
...  
Keyword(s):  
Aspergillus Niger ◽  
Feruloyl Esterase

Synthesis of highly water-soluble feruloyl diglycerols by esterification of an Aspergillus niger feruloyl esterase

2012 ◽  
Vol 95 (3) ◽  
pp. 615-622 ◽  
Author(s):  
Masaki Kikugawa ◽  
Moriyasu Tsuchiyama ◽  
Kenji Kai ◽  
Tatsuji Sakamoto
Keyword(s):  
Aspergillus Niger ◽  
Water Soluble ◽  
Feruloyl Esterase

Carrier-bound and carrier-free immobilization of type A feruloyl esterase from Aspergillus niger: Searching for an operationally stable heterogeneous biocatalyst for the synthesis of butyl hydroxycinnamates

2020 ◽  
Vol 316 ◽  
pp. 6-16 ◽  
Author(s):  
Daniel A. Grajales-Hernández ◽  
Susana Velasco-Lozano ◽  
Mariana A. Armendáriz-Ruiz ◽  
Jorge A. Rodríguez-González ◽  
Rosa María Camacho-Ruíz ◽  
...  
Keyword(s):  
Aspergillus Niger ◽  
Type A ◽  
Feruloyl Esterase ◽  
Carrier Free ◽  
Heterogeneous Biocatalyst
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