Molecular directionality in polysaccharide synthesis by glucosyltransferase
| Project/Area Number |
12660151
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
林産学
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| Research Institution | KYOTO UNIVERSITY |
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Principal Investigator |
SUGIYAMA Junji Kyoto University Wood Research Institute, Associate Professor, 木質科学研究所, 助教授 (40183842)
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| Project Period (FY) |
2000 – 2001
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| Project Status |
Completed (Fiscal Year 2001)
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| Budget Amount *help |
¥4,100,000 (Direct Cost: ¥4,100,000)
Fiscal Year 2001: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 2000: ¥3,500,000 (Direct Cost: ¥3,500,000)
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| Keywords | reducing end / cellulose / hemicellulose / reductive amination / biotin-streptaridin reaction / parallel packing / antiparallel packing / キチン |
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| Research Abstract |
We have developed a recipe for labeling reducing end of polysaccharide chains by reductive amination for microscopic visualization by TEM. This method was applied to investigate the following topics,
1. Structure of native microfibrils and their directionality of synthesis.
2. Chain packing in cellulose and chitin polymorphs
3. Molecular directionality of enzymatic degradation
4. Preference in binding modules of some cellobiohydrolases.
1. The "parallel-up" structure was confirmed both for cellulose I and β-chitin. The polymerization of those chains was found to occur at non-reducing ends.
2. Cellulose III was parallel while II was anti-parallel, which are in good accord with the previous studies on these polymorphs. However, the reducing end labeling of α-chitin was not in good accord with anti-parallel structure.
3. Chitinase A and B from Serratia was found to digest b-chitin microfibrils from their reducing ends and non-reducing ends, respectively.
4. Binding modules from some cellobiohydrolases showed preferential adsorption to the hydrophobic surface of cellulose : i.e. (100) surface of cellulose crystals.
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Report
(3 results)
Research Products
(11 results)
