Purification and Some Properties of Xylanase from Cryptococcus flavus

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概要

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• Extracellular xylanase produced by Cryptococcus flavus was conveniently purified to homogeneity by column chromatography on SP-Sephadex C-25. The purified enzyme showed a pH optimum of 4.5 and a was stable in the range of pH 3.0 to 8.0. This enzyme also showed a temperature optimum of 55℃ and was stable only up to 45℃. The molecular weight of the enzyme was estimated to be 25000 by SDS-polyacrylamide slab gel electrophoresis and 23000 by gel filtration on Bio-Gel P-100. Its isoelectric point (pI) was about 10.0. The number of amino acid residues per molecule was calculated to be 181 and a high content of glutamic acid was characteristic. The enzyme was especially active on various xylooligosaccharides (above xylotriose) and xylan and inactive on cellulose, starch, and arabinan. Its hydrolysis pattern on various xylooligosaccharides (from xylobiose to xylopentaose) and xylan demonstrated that this enzyme in an endotype xylanase and also has trans-xylosidase activity.

• 社団法人日本生物工学会の論文

著者

• YASUI Tsuneo

  Institute of Applied Biochemistry, University of Tsukuba

• NAKANISHI KOTOYOSHI

  Institute of Enology and Viticulture, Yamanashi University

• Yasui Tsuneo

  Institute Of Applied Biochemistry The University Of Tsukuba

• Nakanishi Kotoyoshi

  Institute Of Applied Biochemistry University Of Tsukuba

• ARAI HIDETO

  Institute of Applied Biochemistry, University of Tsukuba

• Arai Hideto

  Institute Of Applied Biochemistry University Of Tsukuba

• Nakanishi Kotoyoshi

  Institute Of Applied Biochemistry The University Of Tsukuba

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