Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Arabinoxylo- and Arabino-Oligosaccharides-Specific α-ʟ-Arabinofuranosidase GH51 Isozymes from the Amylolytic Yeast Saccharomycopsis fibuligera

  • Park, Tae Hyeon (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) ;
  • Kim, Hyeon Jin (Department of Life Science, Chung-Ang University) ;
  • Song, Jeong-Rok (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) ;
  • Kang, Hyun Ah (Department of Life Science, Chung-Ang University) ;
  • Kim, Tae-Jip (Division of Animal, Horticultural and Food Sciences, Graduate School of Chungbuk National University)
  • Received : 2020.12.20
  • Accepted : 2020.12.30
  • Published : 2021.02.28
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Abstract

Two genes encoding probable α-ʟ-arabinofuranosidase (E.C. 3.2.1.55) isozymes (ABFs) with 92.3% amino acid sequence identity, ABF51A and ABF51B, were found from chromosomes 3 and 5 of Saccharomycopsis fibuligera KJJ81, an amylolytic yeast isolated from Korean wheat-based nuruk, respectively. Each open reading frame consists of 1,551 nucleotides and encodes a protein of 517 amino acids with the molecular mass of approximately 59 kDa. These isozymes share approximately 49% amino acid sequence identity with eukaryotic ABFs from filamentous fungi. The corresponding genes were cloned, functionally expressed, and purified from Escherichia coli. SfABF51A and SfABF51B showed the highest activities on p-nitrophenyl arabinofuranoside at 40~45℃ and pH 7.0 in sodium phosphate buffer and at 50℃ and pH 6.0 in sodium acetate buffer, respectively. These exoacting enzymes belonging to the glycoside hydrolase (GH) family 51 could hydrolyze arabinoxylo-oligosaccharides (AXOS) and arabino-oligosaccharides (AOS) to produce only ʟ-arabinose, whereas they could hardly degrade any polymeric substrates including arabinans and arabinoxylans. The detailed product analyses revealed that both SfABF51 isozymes can catalyze the versatile hydrolysis of α-(1,2)- and α-(1,3)-ʟ-arabinofuranosidic linkages of AXOS, and α-(1,2)-, α-(1,3)-, and α-(1,5)-linkages of linear and branched AOS. On the contrary, they have much lower activity against the α-(1,2)- and α-(1,3)-double-substituted substrates than the single-substituted ones. These hydrolases could potentially play important roles in the degradation and utilization of hemicellulosic biomass by S. fibuligera.

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