Substrate specificity of three recombinant α-l-arabinofuranosidases from Bifidobacterium adolescentis and their divergent action on arabinoxylan and arabinoxylan oligosaccharides

Lagaert, Stijn; Pollet, Annick; Delcour, Jan A.; Lavigne, Rob; Courtin, Christophe M.; Volckaert, Guido

doi:10.1016/j.bbrc.2010.10.075

Cited by 70 publications

(51 citation statements)

References 41 publications

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“…Although putative orthologs to the GH 43 AXHd3 from B. adolescentis are so far not discernible in LAB genomes, AXHd3 activity was recently reported for a GH 51 arabinofuranosidase as well (8). Consequently, the ability to utilize AXOS could be restricted to only a few LAB species, as was indicated by the particularly low level of occurrence of GH 51 arabinosidases (see Fig.…”

Section: Discussionmentioning

confidence: 95%

“…The bifidogenic effect of dietary (A)XOS was thoroughly studied and confirmed (1,7). Furthermore, several bifidobacterial ␣-L-arabinofuranosidases (both AXHm and AXHd3) (3,6,(8)(9)(10), as well as ␤-D-xylosidases (11,12) required for complete (A)XOS degradation, have been identified and characterized, whereas all of the enzymes reported so far (both AXH and ␤-xylosidases) are members of glycoside hydrolase (GH) family 43 or 51 (13).…”

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confidence: 93%

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Arabinoxylan Oligosaccharide Hydrolysis by Family 43 and 51 Glycosidases from Lactobacillus brevis DSM 20054

Michlmayr

Hell

Lorenz

et al. 2013

Appl Environ Microbiol

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Due to their potential prebiotic properties, arabinoxylan-derived oligosaccharides [(A)XOS] are of great interest as functional food and feed ingredients. While the (A)XOS metabolism of Bifidobacteriaceae has been extensively studied, information regarding lactic acid bacteria (LAB) is still limited in this context. The aim of the present study was to fill this important gap by characterizing candidate (A)XOS hydrolyzing glycoside hydrolases (GHs) identified in the genome of Lactobacillus brevis DSM 20054. Two putative GH family 43 xylosidases (XynB1 and XynB2) and a GH family 43 arabinofuranosidase (Abf3) were heterologously expressed and characterized. While the function of XynB1 remains unclear, XynB2 could efficiently hydrolyze xylooligosaccharides. Abf3 displayed high specific activity for arabinobiose but could not release arabinose from an (A)XOS preparation. However, two previously reported GH 51 arabinofuranosidases from Lb. brevis were able to specifically remove ␣-1,3-linked arabinofuranosyl residues from arabino-xylooligosaccharides (AXHm3 specificity). These results imply that Lb. brevis is at least genetically equipped with functional enzymes in order to hydrolyze the depolymerization products of (arabino)xylans and arabinans. The distribution of related genes in Lactobacillales genomes indicates that GH 43 and, especially, GH 51 glycosidase genes are rare among LAB and mainly occur in obligately heterofermentative Lactobacillus spp., Pediococcus spp., members of the Leuconostoc/Weissella branch, and Enterococcus spp. Apart from the prebiotic viewpoint, this information also adds new perspectives on the carbohydrate (i.e., pentose-oligomer) metabolism of LAB species involved in the fermentation of hemicellulose-containing substrates.

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Section: Discussionmentioning

confidence: 95%

mentioning

confidence: 93%

Arabinoxylan Oligosaccharide Hydrolysis by Family 43 and 51 Glycosidases from Lactobacillus brevis DSM 20054

Michlmayr

Hell

Lorenz

et al. 2013

Appl Environ Microbiol

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“…The first AXH group seems to be more widespread among GH43, GH51, GH54, and GH62 enzymes. In contrast, a few AXHs have been reported to cleave arabinose at the C(O)-3 position of disubstituted xylose residues, including two GH43 enzymes from Bifidobacterium adolescentis DSM 20083 (44) and Humicola insolens (45), and a GH51 enzyme from B. adolescentis BAF40305 (46). However, the mode of action of PcAxy43A as an AXH appears to be similar to that of AXH Ara I from barley malt; that is, Ara I was able to act on linkages at nonreducing terminal ␤-D-Xylp with one or two ␣-L-Araf substituents but shows no activity toward doubly substituted internal ␤-D-Xylp (47).…”

Section: Resultsmentioning

confidence: 99%

Novel Trifunctional Xylanolytic Enzyme Axy43A from Paenibacillus curdlanolyticus Strain B-6 Exhibiting Endo-Xylanase, β- d -Xylosidase, and Arabinoxylan Arabinofuranohydrolase Activities

Teeravivattanakit

Baramee

Phitsuwan

et al. 2016

Appl Environ Microbiol

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The axy43A gene encoding the intracellular trifunctional xylanolytic enzyme from Paenibacillus curdlanolyticus B-6 was cloned and expressed in Escherichia coli. Recombinant PcAxy43A consisting of a glycoside hydrolase family 43 and a family 6 carbohydrate-binding module exhibited endo-xylanase, ␤-xylosidase, and arabinoxylan arabinofuranohydrolase activities. PcAxy43A hydrolyzed xylohexaose and birch wood xylan to release a series of xylooligosaccharides, indicating that PcAxy43A contained endo-xylanase activity. PcAxy43A exhibited ␤-xylosidase activity toward a chromogenic substrate, p-nitrophenyl-␤-D-xylopyranoside, and xylobiose, while it preferred to hydrolyze long-chain xylooligosaccharides rather than xylobiose. In addition, surprisingly, PcAxy43A showed arabinoxylan arabinofuranohydrolase activity; that is, it released arabinose from both singly and doubly arabinosylated xylose,Moreover, the combination of PcAxy43A and P. curdlanolyticus B-6 endo-xylanase Xyn10C greatly improved the efficiency of xylose and arabinose production from the highly substituted rye arabinoxylan, suggesting that these two enzymes function synergistically to depolymerize arabinoxylan. Therefore, PcAxy43A has the potential for the saccharification of arabinoxylan into simple sugars for many applications. IMPORTANCEIn this study, the glycoside hydrolase 43 (GH43) intracellular multifunctional endo-xylanase, ␤-xylosidase, and arabinoxylan arabinofuranohydrolase (AXH) from P. curdlanolyticus B-6 were characterized. Interestingly, PcAxy43A AXH showed a new property that acted on both the C(O)-2 and C(O)-3 positions of xylose residues doubly substituted with arabinosyl, which usually obstruct the action of xylanolytic enzymes. Furthermore, the studies here show interesting properties for the processing of xylans from cereal grains, particularly rye arabinoxylan, and show a novel relationship between PcAxy43A and endo-xylanase Xyn10C from strain B-6, providing novel metabolic potential for processing arabinoxylans into xylose and arabinose.

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“…However, the specificity of the arabinosyl position on AX was not examined. Arabinofuranosidases are categorised by the specificity of the arabinosyl positions, which are specific on α-1,2 and 1,3 monosubstitution (Bourgois et al 2007;Lagaert et al 2010), and only on α-1,3 of diarabinosyl substitution (van den Broek et al 2005, Sørensen et al 2007.…”

Section: Gh43b6 Gsthklvyamsknpegpfvfkgtiltp---------------vigwtthhsivmentioning

confidence: 99%

Multifunctional Properties of Glycoside Hydrolase Family 43 from Paenibacillus curdlanolyticus Strain B-6 Including Exo-β-xylosidase, Endo-xylanase, and α-L-Arabinofuranosidase Activities

Wongratpanya¹,

Imjongjairak²,

Waeonukul³

et al. 2015

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Substrate specificity of three recombinant α-l-arabinofuranosidases from Bifidobacterium adolescentis and their divergent action on arabinoxylan and arabinoxylan oligosaccharides

Cited by 70 publications

References 41 publications

Arabinoxylan Oligosaccharide Hydrolysis by Family 43 and 51 Glycosidases from Lactobacillus brevis DSM 20054

Arabinoxylan Oligosaccharide Hydrolysis by Family 43 and 51 Glycosidases from Lactobacillus brevis DSM 20054

Novel Trifunctional Xylanolytic Enzyme Axy43A from Paenibacillus curdlanolyticus Strain B-6 Exhibiting Endo-Xylanase, β- d -Xylosidase, and Arabinoxylan Arabinofuranohydrolase Activities

Multifunctional Properties of Glycoside Hydrolase Family 43 from Paenibacillus curdlanolyticus Strain B-6 Including Exo-β-xylosidase, Endo-xylanase, and α-L-Arabinofuranosidase Activities

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