Quantification of glycosidase activities in selected yeasts and lactic acid bacteria

Using a model system, the activities of alpha-L-arabinofuranosidase, beta-g lucosidase, and alpha-L-rhamonopyranosidase were determined in 32 strains o f yeasts belonging to the genera Aureobasidium, Candida, Cryptococcus, Hans eniaspora, Hansenula, Kloeckera, Metschnikowia, Pichia, Saccharomyces, Toru laspora and Brettanomyces (10 strains); and seven strains of the bacterium Leuconostoc oenos. Only one Saccharomyces strain exhibited beta-glucosidase activity, but several non-Saccharomyces yeast species showed activity of t his enzyme. Aureobasidium pullulans hydrolyzed alpha-L-arabinofuranoside, b eta-glucoside, and alpha-L-rhamnopyranoside. Eight Brettanomyces strains ha d beta-glucosidase activity. Location of enzyme activity was determined for those species with enzymatic activity. The majority of beta-glucosidase ac tivity was located in the whole cell fraction, with smaller amounts found i n permeabilized cells and released into the growth medium. Aureobasidium pu llulans hydrolyzed glycosides found in grapes.