PURIFICATION AND PROPERTIES OF THE BETA-GLUCOSIDASE OF A NEW STRAIN OF CANDIDA-MOLISCHIANA ABLE TO WORK AT LOW PH VALUES - POSSIBLE USE IN THE LIBERATION OF BOUND TERPENOLS

A yeast strain isolated in the laboratory was studied and classified as a Candida molischiana. The beta-glucosidase of this yeast strain was then purified. Its molecular weight, estimated by gel filtration, was 100,000. The enzyme consisted of only one subunit, identified after treatment with sodium dodecyl sulfate. Maximum activity was obtained at 55-degrees-C and pH 4 but the enzyme still possessed activity at pH 2.5. Active against different glucosides with beta(1-2), beta(1-3), beta(1-4), beta(1-6), and alpha(1-4) configurations it presented an alpha(1-6)-arabinofuranosidase acitivity. The enzyme was competitively inhibited by glucose (Ki 9.5 mm). A glucosyltransferase activity appeared in the presence of ethanol. The enzyme was constitutive but its synthesis was repressed by glucose.