[Purification and physico-chemical properties of Eupenicillium erubescens alpha-L- rhamnosidase].

A scheme of isolation and purification of the enzyme with alpha-L-rhamnosidase activity 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 60 times with the yield of 0.5%. The enzyme preparation did not contain any glycosidase and proteolytic activity. Molecular mass of the alpha-L-rhamnosidase enzyme on the data of Sepharose 6B gel-filtration was 35 kDa. The enzyme preparation was stable during 48 hours at 20 degrees C, its pH- and thermal optimum were 5 and 60 degrees C, correspondingly.