title: Paenibacillus curdlanolyticus B-6 xylanase Xyn10C capable of producing a doubly arabinose-substituted xylose, α-L-Araf-(1→2)-[α-L-Araf-(1→3)]-D-Xylp, from rye arabinoxylan.
abstract: Paenibacillus curdlanolyticus B-6 Xyn10C is a single module xylanase consisting of a glycoside hydrolase family-10 catalytic module. The recombinant enzyme, rXyn10C, was produced by Escherichia coli and characterized. rXyn10C was highly active toward soluble xylans derived from rye, birchwood, and oat spelt, and slightly active toward insoluble wheat arabinoxylan. It hydrolyzed xylooligosaccharides larger than xylotetraose to produce xylotriose, xylobiose, and xylose. When rye arabinoxylan and oat spelt xylan were treated with the enzyme and the hydrolysis products were analyzed by thin layer chromatography (TLC), two unknown hydrolysis products, U1 and U2, were detected in the upper position of xylose on a TLC plate. Electrospray ionization mass spectrometry and enzymatic analysis using Bacillus licheniformis α-L-arabinofuranosidase Axh43A indicated that U1 was α-L-Araf-(1→2)-[α-L-Araf-(1→3)]-D-Xylp and U2 was α-L-Araf-(1→2)-D-Xylp, suggesting that rXyn10C had strong activity toward a xylosidic linkage before and after a doubly arabinose-substituted xylose residue and was able to accommodate an α-1,2- and α-1,3-linked arabinose-substituted xylose unit in both the -1 and +1 subsites. A molecular docking study suggested that rXyn10C could accommodate a doubly arabinose-substituted xylose residue in its catalytic site, at subsite -1. This is the first report of a xylanase capable of producing α-L-Araf-(1→2)-[α-L-Araf-(1→3)]-D-Xylp from highly arabinosylated xylan.
authors.affiliation: School of Bioresources and Technology, King Mongkut's University of Technology Thonburi, Bangkuntien, Bangkok 10150, Thailand.
authors.forename: Siriluck
authors.initials: S
authors.lastname: Imjongjairak
authors.affiliation: Faculty of Science, Chandrakasem Rajabhat University, 39/1 Ratchadaphisek Road, Bangkok 10900, Thailand.
authors.forename: Pattaporn
authors.initials: P
authors.lastname: Jommuengbout
authors.affiliation: Department of Agro-Industrial Technology, King Mongkut's University of Technology North Bangkok, 1518 Pibulsongkram Road, Bangsue, Bangkok 10800, Thailand.
authors.forename: Pirin
authors.initials: P
authors.lastname: Karpilanondh
authors.affiliation: Graduated School of Bioresources, Mie University, 1577 Kurimamachiya-cho, Tsu 514-8507, Japan.
authors.forename: Hirotaka
authors.initials: H
authors.lastname: Katsuzaki
authors.affiliation: Graduated School of Bioresources, Mie University, 1577 Kurimamachiya-cho, Tsu 514-8507, Japan.
authors.forename: Makiko
authors.initials: M
authors.lastname: Sakka
authors.affiliation: Graduated School of Bioresources, Mie University, 1577 Kurimamachiya-cho, Tsu 514-8507, Japan.
authors.forename: Tetsuya
authors.initials: T
authors.lastname: Kimura
authors.affiliation: School of Bioresources and Technology, King Mongkut's University of Technology Thonburi, Bangkuntien, Bangkok 10150, Thailand.
authors.forename: Patthra
authors.initials: P
authors.lastname: Pason
authors.affiliation: Pilot Plant Development and Training Institute, King Mongkut's University of Technology, Thonburi, Bangkok 10150, Thailand.
authors.forename: Chakrit
authors.initials: C
authors.lastname: Tachaapaikoon
authors.affiliation: Department of Chemistry, Ramkhamhaeng University, Bangkok 10241, Thailand.
authors.forename: Jariya
authors.initials: J
authors.lastname: Romsaiyud
authors.affiliation: School of Bioresources and Technology, King Mongkut's University of Technology Thonburi, Bangkuntien, Bangkok 10150, Thailand. Electronic address: khanok.rat@kmutt.ac.th.
authors.forename: Khanok
authors.initials: K
authors.lastname: Ratanakhanokchai
authors.affiliation: Graduated School of Bioresources, Mie University, 1577 Kurimamachiya-cho, Tsu 514-8507, Japan. Electronic address: sakka@bio.mie-u.ac.jp.
authors.forename: Kazuo
authors.initials: K
authors.lastname: Sakka
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D001709:Biotechnology; D020134:Catalytic Domain; D043364:Endo-1,4-beta Xylanases / Q000235:genetics / Q000378:metabolism*; D005798:Genes, Bacterial; D005965:Glucuronates / Q000096:biosynthesis / Q000737:chemistry; D006868:Hydrolysis; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000096:biosynthesis / Q000737:chemistry; D056507:Paenibacillus / Q000201:enzymology* / Q000235:genetics; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D012434:Secale / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D014990:Xylans / Q000378:metabolism; D014994:Xylose / Q000031:analogs & derivatives* / Q000096:biosynthesis / Q000737:chemistry
chemical_list: D001426:Bacterial Proteins; D005965:Glucuronates; D009844:Oligosaccharides; D011994:Recombinant Proteins; D014990:Xylans; C570991:xylooligosaccharide; C085118:arabinoxylan; D014994:Xylose; D043364:Endo-1,4-beta Xylanases
keywords: Arabinoxylan; Arabinoxylooligosaccharides; Carbohydrate-binding module; Molecular docking; Paenibacillus curdlanolyticus; Xylanase