[PURIFICATION AND PHYSICO-CHEMICAL PROPERTIES OF PENICILLIUM TARDUM a-L- RHAMNOSIDASE].

By ammonium sulfate fractionation and chromatography on TSK-gels Toyopearl HW- 60 and Fractogel TSK DEAE-650-s from supernantant of cultural liquid of Penicillium tardum 1MB F-100074 was isolated and purified in 23 times preparation of enzyme with α-L-rhamnosidase activity with yield of 3.12 %. The specific activity was 27.7 U/mg of protein, molecular mass 67 kDa, thermo- and pH optimum - 60 °C and pH 5.0 respec- tively. It was shown high pH- and thermostability of purified P tardum a-L-rhamnosidase which may be dued to presence of 12 % of carbohydrate component.