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Three chitinases (EC 3.2.1.14) were purified from yam, Dioscorea opposita Thumb, by fractionation with ammonium sulfate, chromatographies on DEAE-Cellulose and DEAE-Sephadex A-50, chromatofocusing and gel filtration on Bio-Gel P-60. The purified enzymes (E-l, E-2 and E-3) showed single bands on sodium dodecylsulfate polyacrylamide gel electrophoresis, and the molecular weights were estimated to be 33,500. The pis were 4.05 (E-l), 4.0 (E-2) and 3.8 (E-3). All enzymes were glycoproteins and the neutral sugar contents were 3.6% (E-l), 3.6 (E-2) and 0.9% (E-3). The N-terminal amino acids ofE-l and E-3 were the same and determined to be histidine. All enzymes hydrolyzed glycolchitin, but not /?-nitrophenyl-2-acetamido-2-deoxy-/?-D-glucopyranoside or Micrococcus lysodeikticus cell walls. E-l and E-3 were stable in the pH range of 5~ll, and below 60°C. These enzymes showed two optimum pHs around 3.5 and 8.0 or 8.5 with glycolchitin as substrate. Chitinase (EC 3.2.1.14) is widely distributed in nature, and plays important roles in degradation of chitin. Chitin is a component of

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A new fucose-containing glycosaminoglycan was investigated as the chiral additive for the separation of basic drug enantiomers by capillary electrophoresis. Tolperisone and eperisone enantiomers were not separated with α- or β-cyclodextrin, or heparin as the chiral additive, but were separated with the new fucose-containing glycosaminoglycan. A variety of basic drug enantiomers were resolved using 2-5%(w/w) solution of the glycosaminoglycan in 10 mM phosphate buffer (final pH 5.0).