Degradation of different [(glucurono)arabino]xylans by a combination of purified xylan-degrading enzymes

Kormelink, F.J.M.; Voragen, A.G.J.

doi:10.1007/bf00182811

Cited by 115 publications

(61 citation statements)

References 31 publications

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“…Synergistic action has been observed between endoxylanase, ␤-xylosidase, arabinoxylan arabinofuranohydrolase, and acetylxylan esterase in the degradation of different (glucuronoarabino)xylans (211). Synergy has also been observed between these enzymes and some of the other xylanolytic enzymes.…”

Section: Synergy Between Polysaccharide-degrading Enzymesmentioning

confidence: 91%

AspergillusEnzymes Involved in Degradation of Plant Cell Wall Polysaccharides

Vries

Visser

2001

Microbiol Mol Biol Rev

877

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: Synergy Between Polysaccharide-degrading Enzymesmentioning

confidence: 91%

AspergillusEnzymes Involved in Degradation of Plant Cell Wall Polysaccharides

Vries

Visser

2001

Microbiol Mol Biol Rev

877

585

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“…However, an explanation for the difference in the initial reaction rates for larchwood xylan and oat spelt xylan, in which there is a similar degree of arabino-monosubstitution anddisubstitution, might be the linkage preference of AbfD3. Indeed, in larchwood xylan, arabinose is mainly O-2 linked to xylose, whereas in oat spelt xylan, it is O-3 linked (17). Interestingly, the yield of arabinose from wheat arabinoxylan hydrolysis could not be improved by increasing enzyme concentrations, indicating that the remaining arabinose was not available to hydrolysis.…”

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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“…The low contents of arabinose in birchwood, beechwood (Ͻ1%) (34), and oat spelt xylans (Յ10%) (35) might be the reason why no arabinose released by Abf43A or Abf43B was detected. On the other hand, significant arabinose (0.65 mg ml Ϫ1 ) was detected in water-soluble wheat arabinoxylan, which contains 37% arabinose (35).…”

Section: Discussionmentioning

confidence: 98%

Distinct Actions by Paenibacillus sp. Strain E18 α- l -Arabinofuranosidases and Xylanase in Xylan Degradation

Shi

Xiao-yan

Meng

et al. 2013

Appl Environ Microbiol

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We cloned a Paenibacillus sp. strain E18 5.3-kb xylanolytic gene cluster that contains three open reading frames encoding two family 43 ␣-L-arabinofuranosidases (Abf43A and Abf43B) and one family 10 xylanase (XynBE18). The deduced amino acid sequences of Abf43A and Abf43B were at most 68% and 63% identical to those of two putative family 43 proteins from Clostridium sp. strain DL-VIII (EHI98634.1 and EHI98635.1), respectively, but were only 11% identical to each other. Recombinant Abf43A and Abf43B had similar activities at 45°C and pH 6.0 but varied in thermostabilities and substrate specificities. Abf43B was active against only 4-nitrophenyl ␣-L-arabinofuranoside, whereas Abf43A acted on 4-nitrophenyl ␣-L-arabinofuranoside, wheat arabinoxylan, 4-nitrophenyl ␣-D-xylopyranoside, and sugar beet arabinan. The sequential and combined effects on xylan degradation by XynBE18, Abf43A, and Abf43B were characterized. For beechwood, birchwood, and oat spelt xylans as the substrates, synergistic effects were found when XynBE18 and Abf43A or Abf43B were incubated together and when the substrates were first incubated with Abf43A or Abf43B and then with XynBE18. Further high-performance liquid chromatography (HPLC) analysis showed that the amounts of xylobiose and xylose increased sharply in the aforementioned reactions. For water-soluble wheat arabinoxylan as the substrate, Abf43A not only released arabinose but also had a synergistic effect with XynBE18. Synergy may arise as the result of removal of arabinose residues from xylans by ␣-L-arabinofuranosidases, which eliminates steric hindrance caused by the arabinose side chains and which allows xylanases to then degrade the xylan backbone, producing short xylooligosaccharides.

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Degradation of different [(glucurono)arabino]xylans by a combination of purified xylan-degrading enzymes

Abstract: The degradation of [({4-O-methyl-}glucu-rono)arabino]xylans from rice bran, oat spelts, wheat flour, larchwood, and birchwood with two. types of endo-(

Cited by 115 publications

References 31 publications

AspergillusEnzymes Involved in Degradation of Plant Cell Wall Polysaccharides

AspergillusEnzymes Involved in Degradation of Plant Cell Wall Polysaccharides

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

Distinct Actions by Paenibacillus sp. Strain E18 α- l -Arabinofuranosidases and Xylanase in Xylan Degradation

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