Purification of an exo-1,3-beta-glucanase from Candida utilis.
An exo-1,3-beta-glucanase (EC 3.2.1.-) has been purified from the culture fluid of the yeast Candida utilis, and its biochemical properties have been studied. The amino acid analysis revealed a high content of acidic amino acids. The purified enzyme had 20% carbohydrate and a net negative charge showing higher affinity for laminarin than for p-nitrophenyl-beta-D-glucopyranoside and yeast cell-wall 1,3-beta-glucans. In addition, the enzyme hydrolyzed the substrates starting from the nonreducing ends, releasing glucose as the exclusive hydrolysis product. The enzyme activity was strongly inhibited by lactones and also by some heavy-metal ions.
D000596:Amino Acids / Q000032:analysis; D002175:Candida / Q000201:enzymology*; D002846:Chromatography, Affinity; D006026:Glycoside Hydrolases / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D008970:Molecular Weight
D000596:Amino Acids; D006026:Glycoside Hydrolases