Purification and Some Properties of Aspergillus aculeatus β-Xylosidase
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- OOI Toshihiko
- Department of Applied Biological Chemistry, College of Agriculture, University of Osaka Prefecture
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- FUJIMOTO Hiroaki
- Department of Applied Biological Chemistry, College of Agriculture, University of Osaka Prefecture
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- WANG Sang-lang
- Department of Applied Biological Chemistry, College of Agriculture, University of Osaka Prefecture
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- TAKIZAWA Toshio
- Bioscience Laboratory, Meiji Seika Kaisha Ltd.
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- HIDAKA Hidemasa
- Bioscience Laboratory, Meiji Seika Kaisha Ltd.
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- OGURA Sei
- Department of Applied Biological Chemistry, College of Agriculture, University of Osaka Prefecture
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- MURAO Sawao
- Department of Applied Biological Chemistry, College of Agriculture, University of Osaka Prefecture
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- ARAI Motoo
- Department of Applied Biological Chemistry, College of Agriculture, University of Osaka Prefecture
Bibliographic Information
- Other Title
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- Aspeygillus aculeatus由来β-キシロシダーゼの精製と諸性質
- Aspergillus aculeatus ユライ ベータ キシロシダーゼ ノ
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Abstract
Extracellular β-xylosidase ([EC 3.2.1.37]: xylan 1, 4-β-xylosidase) was purified from a culture filtrate of Aspergillus aculeatus No. F-50 by column chromatography using DEAE-Sephadex A-50, Sephacry 5-200, and DEAE-Toyopearl 650M columns, and preparative isoelectric focusing. The purified enzyme was homogeneous on SDS-polyacrylamide gel electrophoresis . The molecular weight was about 105, 000 by SDS-PAGE and its p1 value was 4.3. The optimum pH and temperature for the /3 -xylosidase activities were 2.0 and 70°C, respectively. The β-xylosidase was stable for 30 min at 50°C and stable between pH 3 and 7. The enzyme activity was strongly inhibited by Cu2+, Mn2+, and Hg2+. The enzyme hydrolyzed xylooligosaccharides, xylobiose through xylopentaose, to form xylose. The β-xylosidase showed potent activity towards larchwood xylan .
Journal
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- Journal of Applied Glycoscience
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Journal of Applied Glycoscience 42 (1), 45-48, 1995
The Japanese Society of Applied Glycoscience
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Details 詳細情報について
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- CRID
- 1390282680148776704
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- NII Article ID
- 10008253971
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- NII Book ID
- AN10453916
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- COI
- 1:CAS:528:DyaK2MXltlyitbw%3D
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- ISSN
- 18844898
- 13403494
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- NDL BIB ID
- 3616893
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- Data Source
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- JaLC
- NDL
- CiNii Articles
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- Abstract License Flag
- Disallowed