Simple Purification and Characterization of an Extracellular Dextrin Dextranase from Acetobacter capsulatum ATCC 11894.
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- Suzuki Masayuki
- The Graduate School of Electronic Science and Technology, Shizuoka University
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- Unno Takehiro
- Research Institute , Nihon Shokuhin Kako Co., Ltd
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- Okadal Gentaro
- Department of Biology, Faculty of Education, Shizuoka University
Bibliographic Information
- Other Title
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- Acetobacter capsulatum ATCC11894株起源の菌体外デキストリンデキストラナーゼの簡易精製法と基本性質
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Abstract
Dextrin dextranase (DDase, EC2.4.1.2) was extracellularly secreted in a culture medium of Acetobacter capsulatum ATCC 11894 containing both glucose (5.45%) and an extremely small amount of dextrin (0.05%) as the essential carbon sources. The enzyme was simply purified by only one-step centrifugation at 4°C and 20, 000×g for 20 min, and immediately dialyzed against 50 mM acetate buffer (pH 4.5) at CC for 2-3 days. The purified DDase gave a single protein band on both Native- and SDS-PAGE. The molecular mass of the enzyme was estimated to be about 152 kDa by SDS-PAGE. The optimum pH and temperature of the enzyme were 5.2 and 38°C, respectively. The enzyme retained its original activity up to 45°C, and was stable in the range of pH 4.1-5.4 at 4°C for 24 h. The enzyme was completely inactivated by 1 mM of Hg2+ Pb2+ or KMn04. The purified enzyme effectively synthesized α-1, 6-glucan from maltooligosaccharides. The average molecular mass of the product dextran was estimated to be about 1270 kDa.
Journal
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- Journal of Applied Glycoscience
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Journal of Applied Glycoscience 46 (4), 469-473, 1999
The Japanese Society of Applied Glycoscience
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Details 詳細情報について
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- CRID
- 1390282681269607040
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- NII Article ID
- 10008259525
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- NII Book ID
- AN10453916
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- ISSN
- 13403494
- 18807291
- 13447882
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- NDL BIB ID
- 4976745
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- Text Lang
- en
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- Data Source
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- JaLC
- IRDB
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed