Purification and characterization of a (1,4)-?-d-arabinoxylan arabinofuranohydrolase from Aspergillus awamori

Kormelink, F.J.M.; Leeuwen, M.J.F. Searle-van; Wood, Thomas M.; Voragen, A.G.J.

doi:10.1007/bf00169890

Cited by 64 publications

(33 citation statements)

References 26 publications

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“…The A. niger arabinofuranosidase purified by Kaneko et al (174) was able to release only terminal ␣-1,3-linked arabinose residues, whereas arabinofuranosidase B from A. niger was able to release terminal ␣-1,2-, ␣-1,3-and ␣-1,5-linked arabinose residues (34). Unlike some of the arabinofuranosidases, the arabinoxylan arabinofuranohydrolase (AXH) from A. awamori was not able to release arabinose from pectin or pectin-derived oligosaccharides but is highly specific for arabinose residues linked to xylan (209). Wood and McCrae (403) reported the ability of an A. awamori arabinofuranosidase to release feruloylated arabinose residues from wheat straw arabinoxylan.…”

Section: Accessory Enzymes Involved In the Degradation Of Plant Cell mentioning

confidence: 99%

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AspergillusEnzymes Involved in Degradation of Plant Cell Wall Polysaccharides

Vries

Visser

2001

Microbiol Mol Biol Rev

886

585

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SUMMARY Degradation of plant cell wall polysaccharides is of major importance in the food and feed, beverage, textile, and paper and pulp industries, as well as in several other industrial production processes. Enzymatic degradation of these polymers has received attention for many years and is becoming a more and more attractive alternative to chemical and mechanical processes. Over the past 15 years, much progress has been made in elucidating the structural characteristics of these polysaccharides and in characterizing the enzymes involved in their degradation and the genes of biotechnologically relevant microorganisms encoding these enzymes. The members of the fungal genus Aspergillus are commonly used for the production of polysaccharide-degrading enzymes. This genus produces a wide spectrum of cell wall-degrading enzymes, allowing not only complete degradation of the polysaccharides but also tailored modifications by using specific enzymes purified from these fungi. This review summarizes our current knowledge of the cell wall polysaccharide-degrading enzymes from aspergilli and the genes by which they are encoded.

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Section: Accessory Enzymes Involved In the Degradation Of Plant Cell mentioning

confidence: 99%

“…Arabinoxylan arabinofuranohydrolases were produced when Aspergillus was grown on oat straw (209) and birchwood xylan (126). The induction of these enzymes is discussed in more detail below (see "Expression of specific genes responding to different inducers").…”

Section: Accessory Enzymes Involved In the Degradation Of Plant Cell mentioning

confidence: 99%

AspergillusEnzymes Involved in Degradation of Plant Cell Wall Polysaccharides

Vries

Visser

2001

Microbiol Mol Biol Rev

886

585

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“…In addition to these substrates, the type B enzymes can also hydrolyze polymeric substrates such as branched arabinan and arabinoxylan (45). Arabinoxylan arabinofuranohydrolases (AXHs) are members of type B enzymes; however, they are specific for arabinoxylan hydrolysis (7,28,30,31,54,64,66,67). Therefore, based on this nomenclature, we designated FSU2269, which showed activity only on arabinoxylan, as Fibrobacter succinogenes arabinoxylan arabinofuranohydrolase, or FSUAXH1.…”

Section: Characterization Of the Catalytic Activities Of Fsu2269mentioning

confidence: 99%

Domain Analysis of a Modular α- l -Arabinofuranosidase with a Unique Carbohydrate Binding Strategy from the Fiber-Degrading Bacterium Fibrobacter succinogenes S85

et al. 2010

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Family 43 glycoside hydrolases (GH43s) are known to exhibit various activities involved in hemicellulose hydrolysis. Thus, these enzymes contribute to efficient plant cell wall degradation, a topic of much interest for biofuel production. In this study, we characterized a unique GH43 protein from Fibrobacter succinogenes S85. The recombinant protein showed ␣-L-arabinofuranosidase activity, specifically with arabinoxylan. The enzyme is, therefore, an arabinoxylan arabinofuranohydrolase (AXH). The F. succinogenes AXH (FSUAXH1) is a modular protein that is composed of a signal peptide, a GH43 catalytic module, a unique ␤-sandwich module (XX domain), a family 6 carbohydrate-binding module (CBM6), and F. succinogenes-specific paralogous module 1 (FPm-1). Truncational analysis and site-directed mutagenesis of the protein revealed that the GH43 domain/XX domain constitute a new form of carbohydrate-binding module and that residue Y484 in the XX domain is essential for binding to arabinoxylan, although protein structural analyses may be required to confirm some of the observations. Kinetic studies demonstrated that the Y484A mutation leads to a higher k cat for a truncated derivative of FSUAXH1 composed of only the GH43 catalytic module and the XX domain. However, an increase in the K m for arabinoxylan led to a 3-fold decrease in catalytic efficiency. Based on the knowledge that most XX domains are found only in GH43 proteins, the evolutionary relationships within the GH43 family were investigated. These analyses showed that in GH43 members with a XX domain, the two modules have coevolved and that the length of a loop within the XX domain may serve as an important determinant of substrate specificity.

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“…Linkage preference (see above) may intervene (17, (18), and only one enzyme known to be able to release arabinosyl residues from disubstituted xylose has been isolated to date (31). Finally, it is important to note that the progressive loss of arabinose substituents increases the insolubility of the substrate, which may also contribute to a decreased hydrolysis rate (19). Concluding remarks.…”

mentioning

confidence: 99%

“…Despite the obvious potential role for ␣-L-arabinofuranosidases in the industrial bioconversion of plant material, most of the known enzymes would be unsuitable. Indeed, in addition to their lack of robustness (thermostability and pH tolerance), most ␣-L-arabinofuranosidases exhibit a narrow substrate specificity range (2,10), which limits their action towards either oligomeric substrates (13,16,19,21) or polymeric substrates (11,12). Our work on a novel thermophilic bacterium, Thermobacillus xylanilyticus, has led to the identification of several hemicellulase-encoding genes (3, 4, 7), including one for an ␣-L-arabinofuranosidase, the products of which may be suitable as biological catalysts for industrial processes (24,25).…”

mentioning

confidence: 99%

Genetic and Biochemical Characterization of a Highly Thermostable α- l -Arabinofuranosidase from Thermobacillus xylanilyticus

Debeche¹,

Cummings

Connerton

et al. 2000

Appl Environ Microbiol

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The gene encoding an ␣-L-arabinofuranosidase from Thermobacillus xylanilyticus D3, AbfD3, was isolated. Characterization of the purified recombinant ␣-L-arabinofuranosidase produced in Escherichia coli revealed that it is highly stable with respect to both temperature (up to 90°C) and pH (stable in the pH range 4 to 12). On the basis of amino acid sequence similarities, this 56,071-Da enzyme could be assigned to family 51 of the glycosyl hydrolase classification system. However, substrate specificity analysis revealed that AbfD3, unlike the majority of F51 members, displays high activity in the presence of polysaccharides.Microorganisms employ a wide variety of enzymes to degrade hemicellulosic material. Backbone-degrading endoxylanases and ␤-xylosidases are the principal enzymes, but numerous side chain-cleaving enzymes, such as ␣-L-arabinofuranosidases (8, 12, 33), ␣-glucuronidases, acetylxylan esterases, and phenolic acid esterases, are also important. One substituent of xylan, L-arabinose, is present in significant amounts in wheat bran and straw in the form of arabinoxylans. Hydrolysis of such important agricultural by-products using a endo-␤(1,4)-xylanase has identified substituting L-arabinose as a potential barrier for xylanase action (20), and indeed, a synergistic effect between the activities of an ␣-L-arabinofuranosidase and a xylanase has been previously reported (1). Despite the obvious potential role for ␣-L-arabinofuranosidases in the industrial bioconversion of plant material, most of the known enzymes would be unsuitable. Indeed, in addition to their lack of robustness (thermostability and pH tolerance), most ␣-L-arabinofuranosidases exhibit a narrow substrate specificity range (2, 10), which limits their action towards either oligomeric substrates (13,16,19,21) or polymeric substrates (11,12). Our work on a novel thermophilic bacterium, Thermobacillus xylanilyticus, has led to the identification of several hemicellulase-encoding genes (3, 4, 7), including one for an ␣-L-arabinofuranosidase, the products of which may be suitable as biological catalysts for industrial processes (24,25).Isolation and characterization of the ␣-L-arabinofuranosidase-encoding gene, abfD3. Genetic analysis of ϳ9-kb genomic DNA segment revealed the presence of three open reading frames in the same strand (EMBL database accession number Y16849). Of these, one (1,488 bp) encodes a 56-kDa (496-amino-acid) protein which was identified by a database enquiry as a putative family 51 ␣-L-arabinofuranosidase. Comparison of the sequence of this protein, AbfD3, with members of family 51 (F-51) of the glycosyl hydrolase classification system (9) and the creation of a phylogenetic tree revealed that this enzyme is localized within a distinct phylogenetic cluster which contains three other ␣-L-arabinofuranosidases from taxonomically related bacterial sources (Bacillus subtilis [14], Clostridium stercorarium [28], and Bacillus stearothermophilus [6]) (Fig. 1).Expression and purification of recombinant AbfD3. The insertion of the abf...

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Purification and characterization of a (1,4)-?-d-arabinoxylan arabinofuranohydrolase from Aspergillus awamori

Cited by 64 publications

References 26 publications

AspergillusEnzymes Involved in Degradation of Plant Cell Wall Polysaccharides

AspergillusEnzymes Involved in Degradation of Plant Cell Wall Polysaccharides

Domain Analysis of a Modular α- l -Arabinofuranosidase with a Unique Carbohydrate Binding Strategy from the Fiber-Degrading Bacterium Fibrobacter succinogenes S85

Genetic and Biochemical Characterization of a Highly Thermostable α- l -Arabinofuranosidase from Thermobacillus xylanilyticus

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