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  • Title: Hydrolytic properties of a thermostable α-L-arabinofuranosidase from Caldicellulosiruptor saccharolyticus.
    Author: Lim YR, Yoon RY, Seo ES, Kim YS, Park CS, Oh DK.
    Journal: J Appl Microbiol; 2010 Oct; 109(4):1188-97. PubMed ID: 20477891.
    Abstract:
    AIMS: To characterize of a thermostable recombinant α-L-arabinofuranosidase from Caldicellulosiruptor saccharolyticus for the hydrolysis of arabino-oligosaccharides to l-arabinose. METHODS AND RESULTS: A recombinant α-L-arabinofuranosidase from C. saccharolyticus was purified by heat treatment and Hi-Trap anion exchange chromatography with a specific activity of 28.2 U mg(-1). The native enzyme was a 58-kDa octamer with a molecular mass of 460 kDa, as measured by gel filtration. The catalytic residues and consensus sequences of the glycoside hydrolase 51 family of α-L-arabinofuranosidases were completely conserved in α-L-arabinofuranosidase from C. saccharolyticus. The maximum enzyme activity was observed at pH 5.5 and 80°C with a half-life of 49 h at 75°C. Among aryl-glycoside substrates, the enzyme displayed activity only for p-nitrophenyl-α-L-arabinofuranoside [maximum k(cat)/K(m) of 220 m(mol l(-1))(-1) s(-1)] and p-nitrophenyl-α-L-arabinopyranoside. This substrate specificity differs from those of other α-L-arabinofuranosidases. In a 1 mmol l(-1) solution of each sugar, arabino-oligosaccharides with 2-5 monomer units were completely hydrolysed to L-arabinose within 13 h in the presence of 30 U ml(-1) of enzyme at 75°C. CONCLUSIONS: The novel substrate specificity and hydrolytic properties for arabino-oligosaccharides of α-L-arabinofuranosidase from C. saccharolyticus demonstrate the potential in the commercial production of L-arabinose in concert with endoarabinanase and/or xylanase. SIGNIFICANCE AND IMPACT OF THE STUDY: The findings of this work contribute to the knowledge of hydrolytic properties for arabino-oligosaccharides performed by thermostable α-L-arabinofuranosidase.
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