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- SAKANO Yoshiyuki
- Laboratory of Biochemistry, Department of Agricultural Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology
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- TAGUCHI Ayako
- Laboratory of Biochemistry, Department of Agricultural Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology
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- HISAMATSU Reiko
- National Food Research Institute
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- KOBAYASHI Shoichi
- National Food Research Institute
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- FUJIMOTO Daisaburo
- Laboratory of Biochemistry, Department of Agricultural Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology
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- KOBAYASHI Tsuneo
- Laboratory of Biochemistry, Department of Agricultural Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology
Bibliographic Information
- Other Title
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- Aspergillus niger菌体結合型と細胞外イソプルラナーゼの比較
Description
Cell-bound isopullulanase of Aspergillus niger was purified from the mycelia in a sub-merged culture through 1) solubilization of the enzyme with Novozyme 234, 2) P-cellulose (pH 3.8) and DEAF-cellulose (pH 5.5) chromatography, 3) displacement chromatography (changing pH from 6.2 to 4.0) and gel filtration on Bio-Gel P-100 (pH 5.5). Purified enzyme showed a single glycoprotein band, stained with Coomassie Brilliant blue and Na104-Schiff's reagent, on PAGE and a single peak on HPLC using TSK-gel G-3000 Swxz. Substrate specificity of cell-bound and extracellular isopullulanase was the same on pullulan, panose (GlcP(α1→6)Glcp(α1→4)Glc), and 62-a-maltosylmaltose (GlcP (α1→44) Glcp (α1→6) GlcP (α1→4) Glc) . Their optimum pH and temperature were almost similar, but pH and thermal stability of extracellular enzyme were better than those of cell-bound enzyme. Their molecular weight and isoelectric point were different, i, e., 62, 000 and 4.8 (cell-bound enzyme), and 74, 000 and 4.65 (extracellular enzyme).
Journal
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- Journal of the Japanese Society of Starch Science
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Journal of the Japanese Society of Starch Science 37 (1), 39-41, 1990
The Japanese Society of Applied Glycoscience
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Details 詳細情報について
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- CRID
- 1390001206293150336
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- NII Article ID
- 130003866726
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- COI
- 1:CAS:528:DyaK3cXltFWgs7c%3D
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- ISSN
- 1884488X
- 00215406
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- Text Lang
- ja
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- Data Source
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- JaLC
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed