[Purification and physico-chemical properties of Cryptococcus albidus 1001 alpha-L-rhamnosidase].

A scheme of isolation and purification of the enzyme with alpha-L-rhamnosidase activity from culture liquid Cryptococcus albidus 1001 has been developed. It included fractionation by ammonium sulfate and chromatography on TSK-gels Toyopearl HW-60, Fractogel TSK DEAE-650-s and Sepharose 6B. The enzyme was purified 42 times with the yield of 0.7 %. The enzyme preparation did not contain any glycosidase (except of beta-D-glucosidase) and proteolytic activity. Molecular mass of the alpha-L-rhamnosidase preparation by the data of Sepharose 6B gel-filtration was 50 kDa. The enzyme preparation was stable during 48 hours at 20 degrees C, its pH and thermal optimum were 4.0-5.0 and 60 degrees C, correspondingly.