Purification and Properties of Three Types of Xylanases Induced by Methyl β-Xyloside from Streptomyces sp.
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概要
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When mycelia of Streptomyces sp. No. 3137 were cultivated in a medium containing methyl β-xyloside, xylanases (EC 3.2.1.8) were inductively produced into the medium. Three types of enzyme from the culture nitrate have been purified by ultrafiltration with DIAFLO UM-10, chromatography on DEAE-Sephadex A-25, gel filtration on Bio Gel P-100, and isoelectric focusing with Servalyt 6-8 or 9-11. The three purified enzymes, tentatively named X-I, X-II-A, and X-II-B, were homogeneous by polyacrylamide gel electrophoresis at pH 4.3. The molecular weight of X-I was about 50, 000 by SDS-polyacrylamide gel electrophoresis or gel filtration on Bio Gel P-100. The molecular weight of X-II-A and X-II-B were both approximately 25, 000 by SDS-polyacrylamide gel electrophoresis and that of X-II-B was 25, 680 by the sedimentation-equilibrium method. X-I had an isoelectric point at 7.10, and X-II-A and X-II-B had different isoelectric points, 10.06 and 10.26, respectively. The three enzymes were optimally active at 60-65°C and stable to 55°C. The optimal pH of X-I, X-II-A, and X-II-B were pH 5.5-6.5, 5.0-6.0, and 5.0-6.0, respectively. The ranges of two X-IIs pH stability (pH 1.5-11.5) were wider than that of X-Is (pH 3.0-10.5). These purified preparations hydrolyzed xylotriose, xylotetraose, and xylan but not xylobiose, cellobiose, maltose, carboxymethyl cellulose, or soluble starch. Their actions were inhibited by Hg2+ and Fe3+ ions, sodium dodecyl sulfate, and N-bromosuccinimide.
- 社団法人 日本農芸化学会の論文
著者
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YASUI Tsuneo
Institute of Applied Biochemistry, University of Tsukuba
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Nakanishi K
Tokyo Univ. Agric. Tokyo Jpn
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NAKANISHI KOTOYOSHI
Institute of Enology and Viticulture, Yamanashi University
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MARUI Masaki
Institute of Applied Biochemistry, University of Tsukuba
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Yasui Tsuneo
Institute Of Applied Biochemistry The University Of Tsukuba
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Nakanishi Kotoyoshi
Institute Of Applied Biochemistry The University Of Tsukuba
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