Process of Thermal Denaturation of Xylanase (XynB) from Clostridium stercorarium F-9
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概要
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The thermal denaturation process of Clostridium stercorarium F-9 xylanase (XynB) was studied by monitoring remaining activity and recovered activity of the enzyme. At pH 5. 5, aggregation occurred rapidly after the thermal denaturation initiated. The aggregated protein could be dissolved in 8M urea solution, and the enzyme activity was recovered by diluting the urea. The extent of the recovered activity was gradually decreased with two phases as the reaction time of the thermal denaturation became longer. These results suggested the thermal denaturation process to be as follows : N→^^<k_1>D1⇆^^<k_2>__<k_<-2>>D2→^^<k_3>D3 where N is the native state of the enzyme ; D1 is the denatured state of the enzyme that is formed rapidly after the reaction started and can be renatured by the urea treatment, and D2 and D3 are the denatured states of the enzyme that cannot be renatured even by the urea treatment. The rate constants were k_1>9. 2, k_2=0. 33, and k_2=0. 57, and k_3=0.13 (in min^<-1> unit).
- 社団法人日本農芸化学会の論文
- 1995-01-23
著者
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Ohmiya Kunio
Faculty Of Bioresources Mie University
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Araki T
Faculty Of Bioresources Mie University
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Arai Takamitsu
Faculty Of Bioresources And Center For Molecular Biology And Genetics Mie University
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Tanaka A
Faculty Of Bioresources Mie University
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SAKKA Kazuo
Faculty of Bioresources, Mie University
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TANAKA Akiyoshi
Department of Food Science and Technology, Faculty of Agriculture, Kyoto University
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Sakka Kazuo
Faculty Of Bioresources Mie University
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Fukumura Masayuki
Department Of Bioscience Faculty Of Bioresources Mie University
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Fukumura Masayuki
Faculty of Bioresources, Faculty of Education, Mie University
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Tanaka Akiyoshi
Department Of Chemistry Faculty Of Education Mie University
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