Paenibacillus curdlanolyticus Strain B-6 Multienzyme Complex: A Novel System for Biomass Utilization

Waeonukul, Patthra Pason Rattiya; Tachaapaikoon, Chakrit; Kyu, Kazuo Sakka Khin Lay; Kosugi, Akihiko; Mori, Yutaka

doi:10.5772/51820

Cited by 20 publications

(25 citation statements)

References 78 publications

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“…Even though cellulose is the most copious material resource coming from plants, its employment is restricted due to its complex nature and rigid structure [7,10]. The majority of technological methodologies for the conversion of lignocellulosic stuff into chemicals and fuels are devoted to a pretreatment that allows obtaining cellulose from lignin and breaking down its rigid structure [7][8][9]. Afterward, by employing sulfuric acid as a catalyst, the cellulose material can be hydrolyzed into glucose monomers at high temperature [7].…”

Section: Furfural As Platform Molecule Coming From Biomassmentioning

confidence: 99%

“…The xylose monomer is the most abundant. Moreover, a polymeric xylan can be recovered from the hemicellulose fraction, and this polymer can be converted to a xylose monomer through diluted acid hydrolysis (for instance sulfuric acid) [7][8][9]. Finally, cellulose is a polymer made up of glucose units linked by β-glycosidic bonds [3,7].…”

Section: Furfural As Platform Molecule Coming From Biomassmentioning

confidence: 99%

“…Lignin is made up of methoxylatedphenylpropane and it has a three dimensional structure, which bestows structural stiffness to plants and that surrounds hemicellulose [3, [7][8][9]. Hemicellulose is a polymer and it is composed of C5 and C6 sugar monomers such as D-xylose, D-galactose, D-arabinose, D-glucose and D-manose [3, [7][8][9].…”

Section: Furfural As Platform Molecule Coming From Biomassmentioning

confidence: 99%

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Biomass Derived Chemicals: Furfural Oxidative Esterification to Methyl-2-furoate over Gold Catalysts

et al. 2016

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Abstract:The use of heterogeneous catalysis to upgrade biomass wastes coming from lignocellulose into higher value-added chemicals is one of the most explored subjects in the prospective vision of bio-refinery. In this frame, a lot of interest has been driven towards biomass-derived building block molecules, such as furfural. Gold supported catalysts have been successfully proven to be highly active and selective in the furfural oxidative esterification to methyl-2-furoate under mild conditions by employing oxygen as benign oxidant. Particular attention has been given to the studies in which the reaction occurs even without base as co-catalyst, which would lead to a more green and economically advantageous process. The Au catalysts are also stable and quite easily recovered and represent a feasible and promising route to efficiently convert furfural to methyl-2-furoate to be scaled up at industrial level.

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Section: Furfural As Platform Molecule Coming From Biomassmentioning

confidence: 99%

Section: Furfural As Platform Molecule Coming From Biomassmentioning

confidence: 99%

Section: Furfural As Platform Molecule Coming From Biomassmentioning

confidence: 99%

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Biomass Derived Chemicals: Furfural Oxidative Esterification to Methyl-2-furoate over Gold Catalysts

et al. 2016

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“…curdlanolyticus B-6, a facultatively anaerobic bacterium, has great potential in plant biomass degradation (21). Most of the enzymes characterized from the B-6 strain are endo-xylanases belonging to GH10 and GH11 (22), and a few other xylanolytic enzymes, such as a multifunctional GH43B6 exo-␤-xylosidase/ endo-xylanase/␣-L-arabinofuranosidase (19) and a GH67 ␣-glucuronidase (23), have been studied. In this work, we found a new gene, axy43A, from strain B-6, encoding an intracellular GH43 enzyme (PcAxy43A) with a high sequence similarity with enzymes of GH43 subfamily 35, including C. stercorarium XylA (13) and P. woosongensis XylC (14), which were reported to be bifunctional ␤-xylosidase/␣-L-arabinofuranosidases.…”

mentioning

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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“…1.). Paenibacillus genus contains some species such as P. campinasensis BL11 and P. curdlanolyticus B-6 that were reported to have the ability to degrade lignocellulosic materials [42,43], or P. polymyxa BEb-40 which was reported as a promising bacterial strain for the production of endoglucanases, with possibilities of application in the breakdown of lignocellulosic biomass [44]. However, P. illinoisensis has not been reported as having the ability to hydrolyze different lignocellulosic materials.…”

Section: Asian Journal Of Applied Sciences (Issn: 2321 -0893)mentioning

confidence: 99%

Saccharification of Lignocellulosic Materials by Cellulolytic and Xylanolytic <i>Paenibacillus illioisensis </i>CX11

Ahmed

McKay

2017

AJAS

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The utilization of lignocellulosic materials to produce a variety of building blocks (e.g. fermentable sugars) is an interesting alternative approach to meeting the growing demand for high value chemicals. Cellulose and hemicellulose can be hydrolyzed by cellulase and xylanase enzymes into their respective building blocks (hexoses and pentoses), which can later be converted into the targeted compounds. The aim of this study was to test the ability of Paenibacillus illinoisensis CX11 to saccharify different lignocellulosic materials, and to determine its ability to produce cellulolytic and xylanolytic enzymes for possible use in converting lignocellulosic materials into their respective fermentable sugars. The ability of P. illinoisensis CX11 to produce CMCase, xylanase, FPase, and avicelase was tested using SSF of corn stalk. Furthermore, the ability of P. illinoisensis CX11 to saccharify lignocellulosic materials was tested using corn stalk, wheat bran, sawdust, and corn cob. The amount of reducing sugars released from the saccharification of lignocellulosic materials was determined by the 3,5-dinitro-salicylic acid (DNS) method. Obtained results showed that P. illinoisensis CX11 can produce CMCase (400.12 Â± 1.23 U/L), xylanase (385.57 Â± 2.25 U/L), FPase (266.93 Â± 2.22 U/L), avicelase (187.85 Â± 2.22 U/L) and extracellular protein (4.56 Â± 0.14 mg/L). Moreover, P. illinoisensis CX11 showed an ability to saccharify lignocellulosic materials. These findings confirm that P. illinoisensis CX11 has the ability to produce cellulolytic and xylanolytic enzymes, and to hydrolyze different lignocellulosic materials into fermentable sugars. Therefore, this study concludes that P. illinoisensis CX11 can be considered a good source of cellulase and xylanase enzymes to saccharify different lignocellulosic materials.

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Paenibacillus curdlanolyticus Strain B-6 Multienzyme Complex: A Novel System for Biomass Utilization

Cited by 20 publications

References 78 publications

Biomass Derived Chemicals: Furfural Oxidative Esterification to Methyl-2-furoate over Gold Catalysts

Biomass Derived Chemicals: Furfural Oxidative Esterification to Methyl-2-furoate over Gold Catalysts

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

Saccharification of Lignocellulosic Materials by Cellulolytic and Xylanolytic <i>Paenibacillus illioisensis </i>CX11

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