Purification and Characterization of Laccase from White Rot Fungus Trametes sanguinea M85-2
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概要
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Laccase produced by the white rot fungus Trametes sanguinea M85-2 was purified and crystallized. Purification of the enzyme was performed by chromatographies on DEAE- and phenyl-Toyopearl at room temperature. The enzyme was purified to an almost homogeneous state about 6-fold with a yield of 73% from the culture filtrate. The molecular mass of the enzyme was determined to be 62 kDa by SDS-PAGE and the enzyme to be a monomeric glycoprotein containing 9.1% carbohydrate. The purified laccase had 3.3 atoms of copper per enzyme molecule and an isoelectric point of 3.5. The optimum pH and temperature for maximum enzyme activity were 5.0 and 60℃, respectively. The enzyme was stable in a pH range from 5 to 10 and at pH 6.0 for 2 weeks at 25℃. The substrate specificity was broad and the enzyme activity was potently inhibited by compounds such as azide and cyanide.
- 公益社団法人日本生物工学会の論文
- 1995-07-25
著者
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SHINAGAWA Emiko
Department of Chemical and biological Engineering, Ube National College of Technology
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Nishizawa Yoshinori
Department Of Applied Chemistry And Chemical Engineering Faculty Of Engineering Yamaguchi University
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Shinagawa Emiko
Department Of Chemical And Biological Engineering Ube National College Of Technology
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NAKABAYASHI KAZUKI
Department of Applied Chemistry and Chemical Engineering, Faculty of Engineering, Yamaguchi Universi
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Nakabayashi Kazuki
Department Of Applied Chemistry And Chemical Engineering Faculty Of Engineering Yamaguchi University
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Shinagawa Emiko
Department of Agricultural Chemistry, Faculty of Agriculture, Yamaguchi University
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