scholarly journals A non-modular type B feruloyl esterase from Neurospora crassa exhibits concentration-dependent substrate inhibition

2003 ◽  
Vol 370 (2) ◽  
pp. 417-427 ◽  
Author(s):  
Valerie F. CREPIN ◽  
Craig B. FAULDS ◽  
Ian F. CONNERTON

Feruloyl esterases, a subclass of the carboxylic acid esterases (EC 3.1.1.1), are able to hydrolyse the ester bond between the hydroxycinnamic acids and sugars present in the plant cell wall. The enzymes have been classified as type A or type B, based on their substrate specificity for aromatic moieties. We show that Neurospora crassa has the ability to produce multiple ferulic acid esterase activities depending upon the length of fermentation with either sugar beet pulp or wheat bran substrates. A gene identified on the basis of its expression on sugar beet pulp has been cloned and overexpressed in Pichia pastoris. The gene encodes a single-domain ferulic acid esterase, which represents the first report of a non-modular type B enzyme (fae-1 gene; GenBank accession no. AJ293029). The purified recombinant protein has been shown to exhibit concentration-dependent substrate inhibition (Km 0.048mM, Ki 2.5mM and Vmax 8.2units/mg against methyl 3,4-dihydroxycinnamate). The kinetic behaviour of the non-modular enzyme is discussed in terms of the diversity in the roles of the feruloyl esterases in the mobilization of plant cell wall materials and their respective modes of action.

2006 ◽  
Vol 52 (9) ◽  
pp. 886-892 ◽  
Author(s):  
Ourdia Bouzid ◽  
Eric Record ◽  
Michèle Asther ◽  
Mireille Haon ◽  
David Navarro ◽  
...  

The ability of members of Aspergillus sections Nigri, Flavi, and Terrei to produce feruloyl esterases was studied according to their substrate specificity against synthetic methyl esters of hydroxycinnamic acids. Type A feruloyl esterases (FAEA), induced during growth on cereal-derived products, show a preference for the phenolic moiety of substrates that contain methoxy substitutions, as found in methyl sinapinate, whereas type B feruloyl esterases (FAEB) show a preference for the phenolic moiety of substrates that contain hydroxyl substitutions, as occurs in methyl caffeate. All the strains of Aspergillus section Nigri (e.g., A. niger and A. foetidus) were able to produce feruloyl esterases with activity profiles similar to those reported for FAEA and FAEB of A. niger when grown on oat–spelt xylan and sugar beet pulp, respectively. The two genes encoding these proteins, faeA and faeB, were identified by Southern blot analysis. The strains of Aspergillus sections Flavi (e.g., A. flavus, A. flavo-furcatus, and A. tamarii) and Terrei (e.g., A. terreus) were able to produce type A and type B enzymes. faeA was revealed in genomic DNA of these strains, and FAEA was determined by immunodetection in cultures grown in oat–spelt xylan. In addition, type B enzymes, not related to faeB, were efficiently induced by oat–spelt xylan and exhibited very original activity profiles on sugar beet pulp. This work confirms that the members of the genus Aspergillus are good feruloyl esterase producers.Key words: Aspergillus, Nigri, Flavi, Terrei, feruloyl esterase.


Author(s):  
A. G. Low ◽  
J. C. Carruthers ◽  
A. C. Longland ◽  
J.I. Harland

In several recent studies it has been shown that growing pigs and sows can digest substantial amounts of plant cell wall polysaccharides (non-starch polysaccharides (NSP)) by microbial activity in the intestines (for example, see Longland and Low, 1988). Furthermore, it is clear that the principal products of the fermentation, acetic, propionic and butryic acids, are absorbed and used as energy substrate for growth (Bulman et al, 1989). Of the sources of NSP that have been examined, sugar beet pulp is particularly well digested, and it was used in the present study. The objective of the work was to measure the development of the capacity of the intestinal microflora of piglets, after weaning at 21 d, to digest sugar beet pulp. At the same time the performance of the piglets from 21 to 56 d was assessed.


2005 ◽  
Vol 85 (3) ◽  
pp. 255-267 ◽  
Author(s):  
P. Yu ◽  
J. J. McKinnon ◽  
D. A. Christensen

Ferulic acid (3-methoxy-4-hydroxycinnamic acid), present in complex plant cell walls, is covalently cross-linked to polysaccharides by ester bonds and to components of lignin mainly by ether bonds. Ferulic acid has also been shown to occur in dimer- and trimerized forms through oxidative coupling between esterified and/or etherified ferulic acid residues. These cross-links are among the factors most inhibitory to digestion of complex plant cell walls in ruminants. Recently obtained information on ferulic acid and ferulic acid esterases in relation to complex plant cell wall biodegradation is reviewed. A focus of the review is on structural characteristics of plant cell walls associated with ferulic acid, physicochemical properties of ferulic acid esterase and synergistic interaction between ferulic acid esterase and other accessary cell wall degrading enzymes on the release of ferulic acid and plant cell wall biodegradation. Key words: Ferulic acid, hydroxycinnamic acid, feruloyl esterase, interaction effects, polysaccharide, feruloyl-polysaccharides, plant cell walls, biodegradation


1996 ◽  
Vol 24 (3) ◽  
pp. 384S-384S ◽  
Author(s):  
PAUL A KROON ◽  
CRAIG B FAULDS ◽  
PETER RYDEN ◽  
GARY WILLIAMSON

1999 ◽  
Vol 65 (12) ◽  
pp. 5500-5503 ◽  
Author(s):  
Ronald P. de Vries ◽  
Jaap Visser

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.


2009 ◽  
Vol 55 (6) ◽  
pp. 729-738 ◽  
Author(s):  
Fadi Kheder ◽  
Stéphane Delaunay ◽  
Ghassan Abo-Chameh ◽  
Cédric Paris ◽  
Lionel Muniglia ◽  
...  

For the first time, the presence of a ferulic acid esterase (FAE) was demonstrated in Streptomyces ambofaciens . This extracellular enzyme was produced on a range of lignocellulosic substrates. The maximal level of activity was detected in the presence of either destarched wheat bran or oat spelt xylan as the sole carbon source. We found that 1% (m/v) of destarched wheat bran was the optimal concentration to induce its production. With this inducer, no ferulic acid dimers were released from the cell wall by the produced FAE. Interestingly, rape cattle cake ( Brassica napus ), which does not contain esterified ferulic acid, was also shown to induce the production of the FAE from S. ambofaciens. The FAE was partially purified from the culture supernatant. The purified enzyme was optimally active at pH 7 and 40 °C. The substrate specificity of the FAE from S. ambofaciens was investigated: the highest activity was determined with methyl p-coumarate, methyl ferulate, and methyl cinnamate. Furthermore, the FAE required a certain distance between the benzene ring and the ester bond to be active. According to these biochemical characteristics, the FAE from S. ambofaciens has been classified as a type B FAE.


1996 ◽  
Vol 288 ◽  
pp. 143-153 ◽  
Author(s):  
Alexander Oosterveld ◽  
Gerrit Beldman ◽  
Henk A. Schols ◽  
Alfons G.J. Voragen

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