Property of Taka-amylase A with Glu or Asp of the Catalytic Residue Replaced by the Corresponding Amine
スポンサーリンク
概要
- 論文の詳細を見る
Compared with the enzyme activity of a recombinant Taka-amylase A (wild TAA) at 25℃ and pH 5.3, those of two mutants (E230Q and D297N) were 1/10,000 and 1/16,000 for amylase activity, and 1/920 and less than 1/20,000 for maltosidase activity, respectively. This indicates that all residual activities of E230Q are not due to contamination by wild-type TAA. The results from difference spectroscopy suggested that E230Q retains amylose binding ability.
- 社団法人日本農芸化学会の論文
- 1996-08-23
著者
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Kitamoto Katsuhiko
Department of Biotechnology, The University of Tokyo
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Kitamoto Katsuhiko
Department Of Biotechnology The University Of Tokyo
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Nagashima Tadashi
Shin Nihon Chemical Co., Ltd.
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Nagashima Tadashi
Shin Nihon Chemical Co. Ltd
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Oyama Takuji
Laboratory Of Enzyme Chemistry Graduate School Of Agriculture And Biological Science
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Oyama Takuji
Laboratory Of Biophysical Chemistry College Of Agriculture Osaka Prefecture University
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Kitamoto Katsuhiko
Department Of Applied Biological Chemistry And Department Of Applied Biological Engineering Graduate
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MYOJIN Miho
Laboratory of Biophysical Chemistry, College of Agriculture, Osaka Prefecture University
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NITTA Yasunori
Laboratory of Biophysical Chemistry, College of Agriculture, Osaka Prefecture University
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TODA Hiroko
Institute for Protein Research, Osaka University
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Toda H
Institute For Protein Research Osaka University
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Myojin Miho
Laboratory Of Biophysical Chemistry College Of Agriculture Osaka Prefecture University
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Toda Hiroko
Institute For Protein Research Osaka University
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Nitta Yasunori
Laboratory Of Biophysical Chemistry College Of Agriculture Osaka Prefecture University
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