2003年11月
A thermostable non-xylanolytic alpha-glucuronidase of Thermotoga maritima MSB8
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
- ,
- ,
- 巻
- 67
- 号
- 11
- 開始ページ
- 2359
- 終了ページ
- 2364
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1271/bbb.67.2359
- 出版者・発行元
- TAYLOR & FRANCIS LTD
A putative alpha-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 alpha-D-glucuronopyranoside hydrolyzing alpha-glucuronidase, not alpha-glucosidase. It did not hydrolyze 4-O-methyl-D-glucuronoxylan or its fragment oligosaccharides. Agu4B was thermostable with an optimum temperature of 80degreesC. It strictly required Mn2+ 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 alpha-glucuronidase of T. maritima, 61%) than with AglA (alpha-glucosidase of T. maritima, 48%).
- リンク情報
- ID情報
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- DOI : 10.1271/bbb.67.2359
- ISSN : 0916-8451
- eISSN : 1347-6947
- PubMed ID : 14646194
- Web of Science ID : WOS:000186888100007