Chromatofocusing on PBE 94 of a crude enzyme preparation from Aspergillus niger showed the presence of multiple forms of beta-apiosidase, beta-glucosidase, alpha-rhamnosidase, and alpha-arabinofuranosidase. A beta-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-apiofuranoside 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-apiosidase. by