Purification of an exo-1,3-β-glucanase from Candida utilis

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Abstract
An exo-1,3-.beta.-glucanase (EC 3.2.1.-) was purified from the culture fluid of the yeast C. utilis, and its biochemical properties were 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. 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.