Abstract
A novel thermostable extracellular β-galactosidase of Paecilomyces varioti was purified 47-fold by precipitation with iso-propanol followed by ion-exchange chromatography with carboxymethyl-cellulose and ultrafiltration. An interesting feature of this enzyme was the high activity on cellobiose combined with a remarkably low activity on o-nitrophenyl-β-d-galactoside. The enzyme, a glycoprotein, had a molecular weight of 94,000, an isoelectric point of 4.1, a pH optimum of 3.5 and a temperature optimum at 50° C. It was 95% stable for 3 h at 60° C. Enzyme activity was inhibited by mercury, nickel, barium, iron, copper and p-hydroxymercuribenzoate. A Km of 64 mM for lactose was observed. Glucono-δ-lactone and glucosamine both effected mixed inhibition. The enzyme displayed transferase activity.
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