A Thermostable Non-xylanolytic α-Glucuronidase of Thermotoga maritima MSB8(Biochemistry & Molecular Biology)
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概要
- 論文の詳細を見る
A putative α-glucosidase belonging to glycosyl hydrolase family 4 of Thermotoga maritima (TM0752) was expressed in Escherichia coli and it was found that the recombinant protein (Agu4B) was a p-nitrophenyl α-D-glucuronopyranoside hydrolyzing α-glucuronidase, not α-glucosidase. It did not hydrolyze 4-O-methyl-D-glucuronoxylan or its fragment oligosaccharides. Agu4B was thermostable with an optimum temperature of 80℃. It strictly required Mn^<2+> and thiol compounds for its activity. The presence of NAD^+ slightly activated the enzyme. The amino acid sequence of Agu4B showed higher identity with Agu4A (another α-glucuronidase of T.maritima, 61%) than with AglA (α-glucosidase of T.maritima, 48%).
- 社団法人日本農芸化学会の論文
- 2003-11-23
著者
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KITAOKA Motomitsu
Enzyme Laboratory, National Food Research Institute, National Agriculture and Food Research Organiza
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HAYASHI Kiyoshi
Enzyme Applications Laboratory, National Food Research Institute
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Kitaoka Motomitsu
Enzyme Laboratory National Food Research Institute
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SURESH Cuddapah
Enzyme Laboratory, National Food Research Institute
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Suresh Cuddapah
Enzyme Laboratory National Food Research Institute
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Hayashi Kiyoshi
Enzyme Laboratory National Food Research Institute
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