Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Hydrolysis of Arabinoxylo-oligosaccharides by α-ʟ-Arabinofuranosidases and β-ᴅ-Xylosidase from Bifidobacterium dentium

  • Lee, Min-Jae (Division of Animal, Horticultural and Food Sciences, Graduate School of Chungbuk National University) ;
  • Kang, Yewon (Division of Animal, Horticultural and Food Sciences, Graduate School of Chungbuk National University) ;
  • Son, Byung Sam (Division of Animal, Horticultural and Food Sciences, Graduate School of Chungbuk National University) ;
  • Kim, Min-Jeong (Division of Animal, Horticultural and Food Sciences, Graduate School of Chungbuk National University) ;
  • Park, Tae Hyeon (Division of Animal, Horticultural and Food Sciences, Graduate School of Chungbuk National University) ;
  • Park, Damee (Division of Animal, Horticultural and Food Sciences, Graduate School of Chungbuk National University) ;
  • Kim, Tae-Jip (Division of Animal, Horticultural and Food Sciences, Graduate School of Chungbuk National University)
  • Received : 2021.12.13
  • Accepted : 2021.12.22
  • Published : 2022.02.28
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Abstract

Two α-ʟ-arabinofuranosidases (BfdABF1 and BfdABF3) and a β-ᴅ-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 25℃. This exo-enzyme could hydrolyze p-nitrophenyl arabinofuranoside, arabino-oligosaccharides (AOS), arabinoxylo-oligosaccharides (AXOS) such as 32-α-ʟ-arabinofuranosyl-xylobiose (A3X), and 23-α-ʟ-arabinofuranosyl-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)-ʟ-arabinofuranosidic linkages compared to α-(1,3)-linkages. Especially, BfdABF1 could slowly hydrolyze 23,33-di-α-ʟ-arabinofuranosyl-xylotriose (A2+3XX). Meanwhile, BfdABF3 showed the highest activity in sodium acetate at pH 6.0 and 50℃, and it has the exclusively high activities on AXOS such as A3X and A2XX. BfdABF3 mainly catalyzes the removal of ʟ-arabinose side chains from various AXOS. BfdXYL2 exhibited the highest activity in sodium citrate at pH 5.0 and 55℃, and it specifically hydrolyzed p-nitrophenyl 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 hemiceullose-utilization system of Bf. dentium are proposed in the present study. These intracellular exo-hydrolases can synergistically produce ʟ-arabinose and ᴅ-xylose from various AOS, XOS, and AXOS.

Keywords

Acknowledgement

This work was supported by the National Research Foundation of Korea (NRF) grant funded by the Korea government (MSIT) [NRF-2017M3C1B5019292 and NRF-2020R1F1A1076947].

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