Quantification of glycosidase activities in selected yeasts and lactic acid bacteria

Using a model system, the activities of alpha-L-arabinofuranosidase, beta-glucosidase, and alpha-L-rhamonopyranosidase were determined in 32 strains of yeasts belonging to the genera Aureobasidium, Candida, Cryptococcus, Hanseniaspora, Hansenula, Kloeckera, Metschnikowia, Pichia, Saccharomyces, Torulaspora 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 this enzyme. Aureobasidium pullulans hydrolyzed alpha-L-arabinofuranoside, beta-glucoside, and alpha-L-rhamnopyranoside. Eight Brettanomyces strains had beta-glucosidase activity. Location of enzyme activity was determined for those species with enzymatic activity. The majority of beta-glucosidase activity was located in the whole cell fraction, with smaller amounts found in permeabilized cells and released into the growth medium. Aureobasidium pullulans hydrolyzed glycosides found in grapes.