Cloning, Sequencing, and Expression of the Gene Encoding the Clostridium stercorarium Xylanase C in Escherichia coli
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概要
- 論文の詳細を見る
The nucleotide sequence of the Clostridium stercorarium F-9 xynC gene, encoding a xylanase XynC, consists of 3,093 bp and encodes a 1,031-amino acids with a molecular weight of 115,322. XynC is a multidomain enzyme composed of an N-terminal signal peptide and six domains in the following order : two thermostabilizing domains, a family 10 xylanase domain, a family IX cellulose-binding domain, and two S-layer homologous domains. Immunological analysis indicated the presence of XynC in the culture supernatant of C. stercorarium F-9 and in the cells, most likely on the cell surface. XynC purified from a recombinant E. coli was highly active toward xylan and slightly active toward p-nitrophenyl-β-D-xylopyranoside, p-nitrophenyl-β-D-cellobioside, p-nitrophenyl-β-D-glucopyrano-side, and carboxymethylcellulose. XynC hydrolyzed xylan and xylooligosaccharides larger than xylotriose to produce xylose and xylobiose. This enzyme was optimally active at 85℃ and was stable up to 75℃ at pH 5.0 and over the pH range of 4 to 7 at 25℃.
- 社団法人日本農芸化学会の論文
- 1999-09-23
著者
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Kajino T
Special Research Laboratory Ii Toyota Central R&d Laboratories Inc.
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KARITA Shuichi
Center for Molecular Biology and Genetics Mie University
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Kimura Tetsuya
Department Of Clinical Retrovirology And Infectious Diseases Center For Aids Research Kumamoto Unive
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Sakka Kazuo
Department Of Bioscience Faculty Of Bioresources Mie University
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Ohmiya Kunio
Department Of Bioresources School Of Bioresources Mie University
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Fukumura Masayuki
Department Of Bioscience Faculty Of Bioresources Mie University
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Ali Murshedak.
Faculty Of Bioresources:mie University
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ALI MurshedaK.
Department of Bioscience, Faculty of Bioresources Mie University
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SAKANO Katsushi
Department of Bioscience, Faculty of Bioresources Mie University
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Ali Mursheda
Department of Bioscience, Faculty of Bioresources Mie University
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