書誌事項
- タイトル別名
-
- Comparison of cell-bound and extracellular isopullulanase from Aspergillus niger.
抄録
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).
収録刊行物
-
- 澱粉科学
-
澱粉科学 37 (1), 39-41, 1990
日本応用糖質科学会
- Tweet
詳細情報 詳細情報について
-
- CRID
- 1390001206293150336
-
- NII論文ID
- 130003866726
-
- COI
- 1:CAS:528:DyaK3cXltFWgs7c%3D
-
- ISSN
- 1884488X
- 00215406
-
- 本文言語コード
- ja
-
- データソース種別
-
- JaLC
- Crossref
- CiNii Articles
-
- 抄録ライセンスフラグ
- 使用不可