The aim of this work was to study α-L-rhamnosidase [КФ 3.2.1.40] - enzyme, which hydrolyse the terminal non-reduced α-1,2-, α-1,4- and α-1,6-linked L-rhamnose. As a result of screening conducted among 30 strains of micromycetes ability to synthesize α-L-rhamnosidase revealed in Penicillium tardum 60, 39, 2929, 2962, 2963, 2964, 2965, 2966, P. rugulosum 2778, 1652, 2766, P. restrictum 425, 2756, P. aculeatum 202, 217, 329, 2973, 2974, 2975, 2976, 2977, 2979 activity, which ranged from 0.07 to 0.53 OD/mg protein. The most active is brought out P. amleatum 202. From culture supernatant of this micromycete by fractionation with ammonium sulfate (90 % saturation) complex enzyme preparation was obtained and its physico-chemical properties were studied. It was shown that enzyme has pH optimum 3.0, thermooptimum - 60 °C and displayed stability in pH values from 2.0 to 4.0 during 90 min. At pH 5.0 the activity of complex enzyme preparation insignificantly decreased and appears to be up 40 % from initial one. At optimal pH value 3.0 and temperature 15 °C α-L-rhamnosidase tested was stable during 3 days. In addition to α-L-rhamnosidase enzyme preparation of P. arnleatum 202 exerted also β-D-glucosidase activity.
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