Project/Area Number |
11460032
|
Research Category |
Grant-in-Aid for Scientific Research (B)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
応用微生物学・応用生物化学
|
Research Institution | Hokkaido University |
Principal Investigator |
MATUI Hirokazu Hokkaido Univ., Grad. school of Agriculture. Prof., 大学院・農学研究科, 教授 (90109504)
|
Project Period (FY) |
1999 – 2001
|
Project Status |
Completed (Fiscal Year 2001)
|
Budget Amount *help |
¥4,300,000 (Direct Cost: ¥4,300,000)
Fiscal Year 2001: ¥1,300,000 (Direct Cost: ¥1,300,000)
Fiscal Year 2000: ¥3,000,000 (Direct Cost: ¥3,000,000)
|
Keywords | Glycosidase / Glucodextranase / Isomaltotrio-dextranase / Starch branching enzyme / Chimeric enzymes / Substnate Specificity / 枝作り酵素 / デキストラナーゼ / α-グルコシダーゼ / グランチングエンザイム / glucodextranase(グルコデキストラナーゼ) / isomaltotrio-dextranase(イソマルトトリオデキストラナーゼ) / glucoamylase(グルコアミラーゼ) |
Research Abstract |
I cloned the glucodextranase gene, and found that showed the similarity to some of glucoamylase, it is possible to determine the region for bind to α-1,4 orα-1,6 glucosidic linkages. Also the isomaltotrio-dextranase gene was isolated and expressed in E. coll. The expressed enzyme was analyzed. Starch branching enzyme (BE) is concern to biosynthesis of starch, which catalyze the hydrolysis ofα-1,4-glucosidic linkage and transferring it to make α-1,6 point. I cloned two types of this enzyme, and succcessed to express them in E, coll. Chimeric enzymes from these isozymes were analyzed. N-terminal was important to determine the affinity to amylose or amylopectin. And some chimeric enzymes which have different properties were made and analyzed.
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