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2001 Fiscal Year Final Research Report Summary

Molecular directionality in polysaccharide synthesis by glucosyltransferase

Research Project

Project/Area Number 12660151
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field 林産学
Research InstitutionKYOTO UNIVERSITY

Principal Investigator

SUGIYAMA Junji  Kyoto University Wood Research Institute, Associate Professor, 木質科学研究所, 助教授 (40183842)

Project Period (FY) 2000 – 2001
Keywordsreducing end / cellulose / hemicellulose / reductive amination / biotin-streptaridin reaction / parallel packing / antiparallel packing
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.

  • Research Products

    (6 results)

All Other

All Publications (6 results)

  • [Publications] Imai: "Directional degradation of β-chitin by chitinase Al revealed by a novel reducing end labeling technique"FEBS Letters 510. 201. 201-205 (2002)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Uchiyama: "Roles of the Exposed Aromatic Residues in Crystalline Chitin Hydrolysis by Chitinase A from Serratia marcescens 2170^*"J. Biol. Chem.. 276. 41343-41349 (2001)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Watanabe: "Trp122 and Trp134 on the surface of the catalytic domain are essential for crystalline chitin hydrolysis by Bacillus circulans chitinase A1"FEBS Lett.. 494. 74-78 (2001)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Imai et al.: "Directional degradation of β-chitin by chitinase A1 revealed by a novel reducing end labelling technique"FEBS Lett.. 510. 201-205 (2002)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Uchiyama et al.: "Roles of the exposed aromatic residues in Crystalline chitin hydrolysis by chitinase A from Serratia Marcescens 2170"J. Biol. Chem.. 276. 41343-41349 (2001)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Watanabe et al.: "Trp 122 and Trp 134 on the surface of the catalytic domain are essential for crystalline chitin hydrolysis by Bacillno circulans chitinase A1"FEBS Lett.. 494. 74-78 (2001)

    • Description
      「研究成果報告書概要(欧文)」より

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Published: 2003-09-17  

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