Hydrolysis of Arabinoxylo-oligosaccharides by α-L-Arabinofuranosidases and β-DXylosidase from Bifidobacterium dentium
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Two α-L-arabinofuranosidases (BfdABF1 and BfdABF3) and a β-D-xylosidase (BfdXYL2) genes were cloned from Bifidobacterium dentium ATCC 27679, and functionally expressed in E. coli BL21(DE3). BfdABF1 showed the highest activity in 50 mM sodium acetate buffer at pH 5.0 and 25oC. This exoenzyme could hydrolyze p-nitrophenyl arabinofuranoside, arabino-oligosaccharides (AOS), arabinoxylo-oligosaccharides (AXOS) such as 32-α-L-arabinofuranosyl-xylobiose (A3X), and 23-α-Larabinofuranosyl- xylotriose (A2XX), whereas hardly hydrolyzed polymeric substrates such as debranched arabinan and arabinoxylans. BfdABF1 is a typical exo-ABF with the higher specific activity on the oligomeric substrates than the polymers. It prefers to α-(1,2)-L-arabinofuranosidic linkages compared to α-(1,3)-linkages. Especially, BfdABF1 could slowly hydrolyze 23,33-di-α-Larabinofuranosyl- xylotriose (A2+3XX). Meanwhile, BfdABF3 showed the highest activity in sodium acetate at pH 6.0 and 50oC, and it has the exclusively high activities on AXOS such as A3X and A2XX. BfdABF3 mainly catalyzes the removal of L-arabinose side chains from various AXOS. BfdXYL2 exhibited the highest activity in sodium citrate at pH 5.0 and 55oC, and it specifically hydrolyzed pnitrophenyl xylopyranoside and xylo-oligosaccharides (XOS). Also, BfdXYL2 could slowly hydrolyze AOS and AXOS such as A3X. Based on the detailed hydrolytic modes of action of three exo-hydrolases (BfdABF1, BfdABF3, and BfdXYL2) from Bf. dentium, their probable roles in the hemiceulloseutilization system of Bf. dentium are proposed in the present study. These intracellular exohydrolases can synergistically produce L-arabinose and D-xylose from various AOS, XOS, and AXOS.
Abstract
Two α-L-arabinofuranosidases (BfdABF1 and BfdABF3) and a β-D-xylosidase (BfdXYL2) genes were cloned from Bifidobacterium dentium ATCC 27679, and functionally expressed in E. coli BL21(DE3). BfdABF1 showed the highest activity in 50 mM sodium acetate buffer at pH 5.0 and 25oC. This exoenzyme could hydrolyze p-nitrophenyl arabinofuranoside, arabino-oligosaccharides (AOS), arabinoxylo-oligosaccharides (AXOS) such as 32-α-L-arabinofuranosyl-xylobiose (A3X), and 23-α-Larabinofuranosyl- xylotriose (A2XX), whereas hardly hydrolyzed polymeric substrates such as debranched arabinan and arabinoxylans. BfdABF1 is a typical exo-ABF with the higher specific activity on the oligomeric substrates than the polymers. It prefers to α-(1,2)-L-arabinofuranosidic linkages compared to α-(1,3)-linkages. Especially, BfdABF1 could slowly hydrolyze 23,33-di-α-Larabinofuranosyl- xylotriose (A2+3XX). Meanwhile, BfdABF3 showed the highest activity in sodium acetate at pH 6.0 and 50oC, and it has the exclusively high activities on AXOS such as A3X and A2XX. BfdABF3 mainly catalyzes the removal of L-arabinose side chains from various AXOS. BfdXYL2 exhibited the highest activity in sodium citrate at pH 5.0 and 55oC, and it specifically hydrolyzed pnitrophenyl xylopyranoside and xylo-oligosaccharides (XOS). Also, BfdXYL2 could slowly hydrolyze AOS and AXOS such as A3X. Based on the detailed hydrolytic modes of action of three exo-hydrolases (BfdABF1, BfdABF3, and BfdXYL2) from Bf. dentium, their probable roles in the hemiceulloseutilization system of Bf. dentium are proposed in the present study. These intracellular exohydrolases can synergistically produce L-arabinose and D-xylose from various AOS, XOS, and AXOS.
참고문헌 (28)
- Seri K, "L-arabinose selectively inhibits intestinal sucrase in an uncompetitive manner and suppresses glycemic response after sucrose ingestion in animals", Metabolism, 45, pp.1368~1374 (1996)
- Moon JS, "In vitro digestion and fermentation properties of linear sugar-beet arabinan and its oligosaccharides", Carbohydr. Polym, 131, pp.50~56 (2015)
- Falck P, "Xylooligosaccharides from hardwood and cereal xylans produced by a thermostable xylanase as carbon sources for Lactobacillus brevis and Bifidobacterium adolescentis", J. Agric. Food Chem, 61, pp.7333~7340 (2013)
- Pastell H, "In vitro fermentation of arabinoxylan-derived carbohydrates by bifidobacteria and mixed fecal microbiota", J. Agric. Food Chem, 57, pp.8598~8606 (2009)
- Jana UK, "Hemicellulose-derived oligosaccharides : Emerging prebiotics in disease alleviation", Front. Nutr, 8, pp.670817~ (2021)
- Biely P, "Towards enzymatic breakdown of complex plant xylan structures : State of the art", Biotechnol. Adv, 34, pp.1260~1274 (2016)
- Poria V, "Arabinofuranosidases : Characteristics, microbial production, and potential in waste valorization and industrial applications", Bioresour. Technol, 304, pp.123019~ (2020)
- Lagaert S, "β-xylosidases and α-L-arabinofuranosidases : Accessory enzymes for arabinoxylan degradation", Biotechnol. Adv, 32, pp.316~332 (2014)
- O'Callaghan A, "Bifidobacteria and their role as members of the human gut microbiota", Front. Microbiol, 7, pp.925~ (2016)
- Song AX, "Mechanistic insights into the structure-dependant and strain-specific utilization of wheat arabinoxylan by Bifidobacterium longum", Carbohydr. Polym, 249, pp.116886~ (2020)
- Pokusaeva K, "Carbohydrate metabolism in Bifidobacteria", Genes Nutr, 6, pp.285~306 (2011)
- Kelly SM, "Plant glycan metabolism by Bifidobacteria", Front. Microbiol, 12, pp.609418~ (2021)
- Yang J, "Combining of transcriptome and metabolome analyses for understanding the utilization and metabolic pathways of xylo-oligosaccharide in Bifidobacterium adolescentis ATCC 15703", Food Sci. Nutr, 7, pp.3480~3493 (2019)
- Saito Y, "Multiple transporters and glycoside hydrolases are involved in arabinoxylan-derived oligosaccharide utilization in Bifidobacterium pseudocatenulatum", Appl. Environ. Microbiol, 86, pp.01782~01720 (2020)
- van den Broek LA, "Cloning and characterization of arabinoxylan arabinofuranohydrolase-D3(AXHd3)from Bifidobacterium adolescentis DSM20083", Appl. Microbiol. Biotechnol, 67, pp.641~647 (2005)
- Lagaert S, "Substrate specificity of three recombinant α-Larabinofuranosidases from Bifidobacterium adolescentis and their divergent action on arabinoxylan and arabinoxylan oligosaccharides", Biochem. Biophys. Res. Commun, 402, pp.644~650 (2010)
- Margolles A, "Purification and functional characterization of a novel α-L-arabinofuranosidase from Bifidobacterium longum B667", Appl. Environ. Microbiol, 69, pp.5096~5103 (2003)
- Lee JH, "Cloning and characterization of α-L-arabinofuranosidase and bifunctional α-L-arabinopyranosidase", β-D-galactopyranosidase from Bifidobacterium longum H-1, 2011, pp.111, 1097~1107
- Masahiro Komeno, "Two novel α-L-arabinofuranosidases from Bifidobacterium longum subsp. longum belonging to glycoside hydrolase family 43 cooperatively degrade arabinan", Applied and Environmental Microbiology, 85(6) (2019), American Society for Microbiology[DOI]
- Shin HY, "Purification and characterization of α-L-arabinopyranosidase and α-Larabinofuranosidase from Bifidobacterium breve K-110, a human intestinal anaerobic bacterium metabolizing ginsenoside Rb2 and Rc", Appl. Environ. Microbiol, 69, pp.7116~7123 (2003)[DOI]
- Lagaert S, "Characterization of two β-xylosidases from Bifidobacterium adolescentis and their contribution to the hydrolysis of prebiotic xylooligosaccharides", Appl. Microbiol. Biotechnol, 92, pp.1179~1185 (2011)
- 현양진, "Cloning and Characterization of Ginsenoside Ra1-Hydrolyzing β-D-Xylosidase from Bifidobacterium breve K-110", Journal of Microbiology and Biotechnology, 22(4), pp.535~540 (2012), 한국미생물·생명공학회[DOI]
- Lugli GA, "Decoding the genomic variability among members of the Bifidobacterium dentium species", Microorganisms, 8, pp.1720~ (2020)
- Michlmayr H, "Heterologously expressed family 51 α-L-arabinofuranosidases from Oenococcus oeni and Lactobacillus brevis", Appl. Environ. Microbiol, 77, pp.1528~1531 (2011)
- Alexander Holm Viborg, "Biochemical and kinetic characterisation of a novel xylooligosaccharide-upregulated GH43 β-d-xylosidase", α-l-arabinofuranosidase (BXA43) from the probiotic Bifidobacterium animalis subsp. lactis BB-12, 2013, pp.3(1), ~[DOI]
- Michlmayr H, "Arabinoxylan oligosaccharide hydrolysis by family 43and 51 glycosidases from Lactobacillus brevis DSM 20054", Appl. Environ. Microbiol, 79, pp.6747~6754 (2013)
- Takuya Matsumoto, "Multi-functional glycoside hydrolase: Blon_0625 from Bifidobacterium longum subsp. infantis ATCC 15697", Enzyme and Microbial Technology, 68, pp.10~14 (2015), Elsevier BV[DOI]
- Su-Dan Jiang, "Chromophorylation of a Novel Cyanobacteriochrome GAF Domain from Spirulina and Its Response to Copper Ions", Journal of Microbiology and Biotechnology, 31(2), pp.233~239 (2021), 한국미생물·생명공학회[DOI]