MULTIPLE FORMS OF GLYCOSIDASES IN AN ENZYME PREPARATION FROM ASPERGILLUS-NIGER - PARTIAL CHARACTERIZATION OF A BETA-APIOSIDASE

Chromatofocusing on PBE 94 of a crude enzyme preparation from Aspergil lus niger showed the presence of multiple forms of beta-apiosidase, be ta-glucosidase, alpha-rhamnosidase, and alpha-arabinofuranosidase. A b eta-apiofuranosidase from the enzyme preparation was purified 27-fold by gel filtration and ion-exchange chromatography. The molecular mass of the enzyme and the K-m value for p-nitrophenyl-beta-D-apiofuranosid e were 84,000 and 3.3 mW, respectively. The optimum pH and temperature for the enzyme activity were between pH 5.0-6.0 and 50-60 degrees C, respectively. The enzyme was stable up to 50 degrees C and between pH 4.0-7.0. Geranyl, linalyl apiosylglucosides, aroma precursors in grape , and flavone apiosylglucoside were the substrates for the beta-apiosi dase. by (C) 1997 by Elsevier Science Inc.