Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Detailed Mode of Action of Arabinan-Debranching α-ʟ-Arabinofuranosidase GH51 from Bacillus velezensis

  • Oh, Gyo Won (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) ;
  • Choi, Chang-Yun (Division of Animal, Horticultural and Food Sciences, Graduate School of Chungbuk National University) ;
  • Kang, So-Yeong (Division of Animal, Horticultural and Food Sciences, Graduate School of Chungbuk National University) ;
  • Kang, Jung-Hyun (Division of Animal, Horticultural and Food Sciences, Graduate School of Chungbuk National University) ;
  • Lee, Min-Jae (Division of Animal, Horticultural and Food Sciences, Graduate School of Chungbuk National University) ;
  • Han, Nam Soo (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 : 2018.11.20
  • Accepted : 2018.12.03
  • Published : 2019.01.28
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Abstract

The gene encoding an ${\alpha}-{\text\tiny{L}}-arabinofuranosidase$ (BvAF) GH51 from Bacillus velezensis FZB42 was cloned and expressed in Escherichia coli. The corresponding open reading frame consists of 1,491 nucleotides which encode 496 amino acids with the molecular mass of 56.9 kDa. BvAF showed the highest activity against sugar beet (branched) arabinan in 50 mM sodium acetate buffer (pH 6.0) at $45^{\circ}C$. However, it could hardly hydrolyze debranched arabinan and arabinoxylans. The time-course hydrolyses of branched arabinan and arabinooligosaccharides (AOS) revealed that BvAF is a unique exo-hydrolase producing exclusively ${\text\tiny{L}}-arabinose$. BvAF could cleave ${\alpha}-(1,2)-$ and/or ${\alpha}-(1,3)-{\text\tiny{L}}-arabinofuranosidic$ linkages of the branched substrates to produce the debranched forms of arabinan and AOS. Although the excessive amount of BvAF could liberate ${\text\tiny{L}}-arabinose$ from linear AOS, it was extremely lower than that on branched AOS. In conclusion, BvAF is the arabinan-specific exo-acting ${\alpha}-{\text\tiny{L}}-arabinofuranosidase$ possessing high debranching activity towards ${\alpha}-(1,2)-$ and/or ${\alpha}-(1,3)-linked$ branches of arabinan, which can facilitate the successive degradation of arabinan by $endo-{\alpha}-(1,5)-{\text\tiny{L}}-arabinanase$.

Keywords

Acknowledgement

Supported by : National Research Foundation

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