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Carbohydrate Bioengineering, Vol 10. Progress in Biotechnology

  • ID: 1757912
  • Book
  • 368 Pages
  • Elsevier Science and Technology
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The Carbohydrate Bioengineering Meeting held in Elsinore, Denmark, April 23-26, 1995, gathered 230 scientists, mostly from Europe, with interest in carbohydrate analysis and structure; carbohydrates in medicine and glycopathology; structure, function, application, and protein engineering of carbohydrate active enzymes; oligo- and polysaccharides of industrial interest; and production of carbohydrate containing new materials.

The first chapters address glycoconjugates as modulatory and recognition molecules, structure determination using NMR and mass spectrometry, and microdialysis-chip enzyme-based sensors. Active site mutations coupled with crystal structures and synthetic substrate analogue interactions as well as new three-dimensional structures and binding domains for biotechnological applications are included in the chapters. Carbohydrate active enzymes turned out to be a predominant topic.

The rapid development in glycobiology and glycotechnology has resulted in an enormous increase in our knowledge on the structure conversion, and application of carbohydrates in industry and medicine.

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Glycans of glycoconjugates as modulatory and recognition molecules (N. Sharon). NMR studies of the structure and dynamics of carbohydrates in aqueous solution (H. van Halbeek and S. Sheng). Linkage analysis by mass spectrometry of chemically modified oligo-saccharides from glycosphingolipids and glycoproteins (B. Nilsson). Development of a novel enzyme based glucose sensor (F. Spener et al). Carbohydrate binding at the active site of Escherichia coli maltodextrin phosphorylase (P. Drueckes et al.). The chitinolytic system of Streptomyces olivaceoviridis (H. Schrempf). Properties and production of the ß-glycosidase from the thermophilic Archaeon Sulfolobus solfataricus expressed in mesophilic hosts (M. Moracci et al.). Contribution of subsites to catalysis and specificity in the extended binding cleft of Bacillus 1,3-1,4-&bgr;-D-glucan 4-glucanohydrolases (A. Planas and C. Malet). Probing of glycosidase active sites through labeling, mutagenesis and kinetic studies (S.G. Withers). Thiooligosaccharides: toys or tools for the studies of glycanases (H. Driguez). Mutational analysis of catalytic mechanism and specificity in amylolytic enzymes (B. Svensson et al.). The structure and function relationship of Schizophyllum commune xylanase A (M.R. Bray and A.J. Clarke). Protein engineering of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 (L. Dijkhuzien et al.). Oxidation stable amylases for detergents (T.V. Borchert et al.). Electrostatic studies of carbohydrate active enzymes (A. Baptista et al.). Effects of glycosylation on protein folding, stability and solubility. Studies of chemically modified or engineered plant and fungal peroxidases (K.G. Welinder and J.W. Tams). Modes of action of two Trichoderma reesei cellobiohydrolases (T.T. Teeri et al.). Structural studies on fungal endoglucanases from Humicola insolens (G.J. Davies and M. Schülein). The catalytic domain of endoglucanase A from Clostridium cellulolyticum belonging to family 5: an &agr;/&bgr;-barrel enzyme (V. Ducros et al.). Celluosome domains for novel biotechnological application (E.A. Bayer et al.). Interactions of cellulases from Cellulomonas fimi with cellulose (N. Din et al.). Transgenic plants as a tool to understand starch biosynthesis (J. Ko&bgr;mann et al.). Targeted expression of microbial cellulases in transgenic animals (S. Ali et al.). Mechanism and action of glucansucrases (J.F. Robyt). Studies of recombinant amylosucrase (M. Remaud-Simeon et al.). Application of cloned monocomponent carbohydrates for modification of plant materials (L.V. Kofod et al.). Fatty acid esters of ethyl glucoside, a unique class of surfactants (O. Andresen and O. Kirk). A wide range of carbohydrate modifications by a single microorganism: leuconostoc mesenteroides (W. Soetaert et al.).
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Petersen, S.B.
Svensson, B.
Pedersen, S.
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