Purification and Characterization of β-Xylosidase from Thermoascus sp.

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概要

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• A β-xylosidase was purified from the culture filtrate of the thermophilic fungus Thermoascus sp. by ultrafiltration, ethanol precipitation, and chromatography with DEAE-Toyopearl 650M, Mono Q HR5/5, and Phenyl Superose HR5/5. The purified β-xylosidase was found to be homogeneous on sodium dodecyl sulphate-polyacrylamide gel electrophoresis(SDS-PAGE). Its molecular weight was estimated to be 107 kDa by gel filtration chromatography(Superdex 200 HR)and 100 kDa by SDS-PAGE. The optimum activity of the enzyme was observed at pH 4.5 and 55℃. The enzyme was stable up to 60℃ at pH 4.5 for 1 h. The enzyme exhibited hydrolytic activity on phenyl β-_D-xyloside and xylan(birch wood). Fifteen of the amino acid residues in the amino terminal region of the Thermoascus sp. β-xylosidase were homologous with residues in the equivalent region of the maturation protein β-glucosidase from Aspergillus aculeatus.

• 社団法人日本生物工学会の論文
• 1998-10-25

著者

• MATSUO Masaru

  Institute of Applied Biochemistry, Uriiversity of Tsukuba

• Okada Takahiro

  Institute Of Applied Biochemistry Tsukuba University

• Matsuo Masaru

  Institute Of Applied Biochemistry Tsukuba University

• ENDOU AKIO

  Institute of Applied Biochemistry, Tsukuba University

• YAMAOKA YUUICHI

  Institute of Agriculture and Forestry, Tsukuba University

• Endou Akio

  Institute Of Applied Biochemistry Tsukuba University

• Yamaoka Yuuichi

  Institute Of Agriculture And Forestry Tsukuba University

• MATSUO MASARU

  Institute of Applied Biochemistry, Tsukuba University

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