Chrysosporium lucknowense arabinohydrolases effectively degrade sugar beet arabinan

Kühnel, Stefan; Hinz, S.W.A.; Pouvreau, Laurice; Wery, Jan; Schols, Henk A.; Gruppen, Harry

doi:10.1016/j.biortech.2010.05.070

Cited by 50 publications

(28 citation statements)

References 27 publications

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“…This observation is manifested in the large number of microbes reported to harbor enzymes for its hydrolysis (29)(30)(31)(32)(33)(34)(35), including Bacteroides spp., Bacillus subtilis, and Bacillus stearothermophilus. In addition, arabinan is an important product for the food and biotechnology industries (4,5). This polysaccharide is composed of a backbone of ␣-1,5-linked arabinose units and is further branched with side chains of arabinose units at position O-3 or O-2 or at both positions (5).…”

Section: Discussionmentioning

confidence: 99%

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Enzymatic Mechanism for Arabinan Degradation and Transport in the Thermophilic Bacterium Caldanaerobius polysaccharolyticus

Wefers

Dong

Abdelhamid

et al. 2017

Appl Environ Microbiol

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The plant cell wall polysaccharide arabinan provides an important supply of arabinose, and unraveling arabinan-degrading strategies by microbes is important for understanding its use as a source of energy. Here, we explored the arabinan-degrading enzymes in the thermophilic bacterium Caldanaerobius polysaccharolyticus and identified a gene cluster encoding two glycoside hydrolase (GH) family 51 ␣-L-arabinofuranosidases (CpAbf51A, CpAbf51B), a GH43 endoarabinanase (CpAbn43A), a GH27 ␤-L-arabinopyranosidase (CpAbp27A), and two GH127 ␤-Larabinofuranosidases (CpAbf127A, CpAbf127B). The genes were expressed as recombinant proteins, and the functions of the purified proteins were determined with para-nitrophenyl (pNP)-linked sugars and naturally occurring pectin structural elements as the substrates. The results demonstrated that CpAbn43A is an endoarabinanase while CpAbf51A and CpAbf51B are ␣-L-arabinofuranosidases that exhibit diverse substrate specificities, cleaving ␣-1,2, ␣-1,3, and ␣-1,5 linkages of purified arabinan-oligosaccharides. Furthermore, both CpAbf127A and CpAbf127B cleaved ␤-arabinofuranose residues in complex arabinan side chains, thus providing evidence of the function of this family of enzymes on such polysaccharides. The optimal temperatures of the enzymes ranged between 60°C and 75°C, and CpAbf43A and CpAbf51A worked synergistically to release arabinose from branched and debranched arabinan. Furthermore, the hydrolytic activity on branched arabinan oligosaccharides and degradation of pectic substrates by the endoarabinanase and L-arabinofuranosidases suggested a microbe equipped with diverse activities to degrade complex arabinan in the environment. Based on our functional analyses of the genes in the arabinan degradation cluster and the substrate-binding studies on a component of the cognate transporter system, we propose a model for arabinan degradation and transport by C. polysaccharolyticus. IMPORTANCE Genomic DNA sequencing and bioinformatic analysis allowed the identification of a gene cluster encoding several proteins predicted to function in arabinan degradation and transport in C. polysaccharolyticus. The analysis of the recombinant proteins yielded detailed insights into the putative arabinan metabolism of this thermophilic bacterium. The use of various branched arabinan oligosaccharides provided a detailed understanding of the substrate specificities of the enzymes and allowed assignment of two new GH127 polypeptides as ␤-L-arabinofuranosidases able to degrade pectic substrates, thus expanding our knowledge of this rare group of glycoside hydrolases. In addition, the enzymes showed synergistic effects for the degradation of arabinans at elevated temperatures. The enzymes characterized from the gene cluster are, therefore, of utility for arabinose production in both the biofuel and food industries.

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Section: Discussionmentioning

confidence: 99%

“…A rabinose is the second most abundant pentose sugar found in nature and is of considerable importance in both microbial metabolism and the biotechnology industry (1)(2)(3)(4). Arabinose can be found in various plant cell wall polysaccharides, with arabinans being the most important polymers.…”

Section: Abstract Pectic Enzymes Thermophilesmentioning

confidence: 99%

Enzymatic Mechanism for Arabinan Degradation and Transport in the Thermophilic Bacterium Caldanaerobius polysaccharolyticus

Wefers

Dong

Abdelhamid

et al. 2017

Appl Environ Microbiol

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“…Physic-chemical properties of wine could be affected by the branching degree. It has been reported that branched arabino-oligosaccharides are more difficult to degrade than linear arabinan-oligomers in sugar beet (Kühnel et al, 2010). Additional in-depth characterization would be required to confirm the branching configuration, e.g.…”

Section: Glycosyl-linkage Determination: Structure Of Oligosaccharidementioning

confidence: 99%

Oligosaccharides of Cabernet Sauvignon, Syrah and Monastrell red wines

et al. 2015

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“…As found by sugar analysis, neutral arabino-oligosaccharides contained an α-(1,5)-linked backbone of l-arabinosyl residues and carried single substituted α-(1,3)-linked l-arabinosyl residues or consisted of a double substituted α-(1,2,3,5)-linked arabinan structure within the molecule (Westphal et al, 2010). Enzyme Abn4 belongs to GH43 family and is more active toward branched polymeric arabinan substrate that releases arabinose monomers from single substituted arabinose residues, while Abn1 and Abn2 are active toward linear arabinan (Kühnel et al, 2010). Abn2 is a member of GH93 family that consists of exoarabinases acting on linear arabinan, hydrolyzing the α-1,5-linkages of arabinan polysaccharides presented as side chains of pectin.…”

Section: Hemicellulolytic Systemmentioning

confidence: 99%

Genomic insights into the fungal lignocellulolytic system of Myceliophthora thermophila

et al. 2014

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The microbial conversion of solid cellulosic biomass to liquid biofuels may provide a renewable energy source for transportation fuels. Cellulolytic fungi represent a promising group of organisms, as they have evolved complex systems for adaptation to their natural habitat. The filamentous fungus Myceliophthora thermophila constitutes an exceptionally powerful cellulolytic microorganism that synthesizes a complete set of enzymes necessary for the breakdown of plant cell wall. The genome of this fungus has been recently sequenced and annotated, allowing systematic examination and identification of enzymes required for the degradation of lignocellulosic biomass. The genomic analysis revealed the existence of an expanded enzymatic repertoire including numerous cellulases, hemicellulases, and enzymes with auxiliary activities, covering the most of the recognized CAZy families. Most of them were predicted to possess a secretion signal and undergo through post-translational glycosylation modifications. These data offer a better understanding of activities embedded in fungal lignocellulose decomposition mechanisms and suggest that M. thermophila could be made usable as an industrial production host for cellulolytic and hemicellulolytic enzymes.

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Chrysosporium lucknowense arabinohydrolases effectively degrade sugar beet arabinan

Cited by 50 publications

References 27 publications

Enzymatic Mechanism for Arabinan Degradation and Transport in the Thermophilic Bacterium Caldanaerobius polysaccharolyticus

Enzymatic Mechanism for Arabinan Degradation and Transport in the Thermophilic Bacterium Caldanaerobius polysaccharolyticus

Oligosaccharides of Cabernet Sauvignon, Syrah and Monastrell red wines

Genomic insights into the fungal lignocellulolytic system of Myceliophthora thermophila

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