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From Achromobacter sp. 7a, that was isolated with Black sea, aquatoria of island Zmi- inyi, was isolated enzyme with α-amylase activity, that able also to split the synthetic substrates: p-nitrophenyl-α-D-glucopyranoside and p-nitrophenyl-α, -β-D-xylopyranoside. Methods of isolation and purification of enzyme were selected which included: ammonium sulfate precipitation and affinity sorption on starch, that improved enzyme activity in 7 times in comparison with activity in the supernatant of cultural liquid. a-Amylase showed maximal activity at pH 7.0 and 11.0 and to the temperature 50 °C. Enzyme remained fully stable during 24 hours in the range of pH from 7.0 to 12.0, during 3 hours at a temperature 37 °C and 50 °C at pHopt 7.0, and also 87.5 % and 75 % of initial activity saved during 3 h of incubation at a temperature 37 °C and 50 °C at pHopt 11.0 respectively. It is shown that addition of antihunt agents (ions of calcium, chloride of natrium) did not protect an enzyme from thermoinactivation (60 °C, 70 °C).

Investigation of 15 different glycoside activities of 64 strains isolated from water and invertebra of the Black Sea has shown that 64% of the studied strains displayed the capacity to synthesize enzymes with alpha-L-ramnosidase activity which varied from 0.01 to 0.20 un/ml depending on the strain. The greatest number of the enzyme producers was found in representatives of Alteromonas macleodii. Other investigated glycosidase activities: alpha-amylase, beta-N-acetyl-D-glucosaminidase, beta-D-glucuronide, alpha-N-acetyl-D-galactosaminidase, beta-N-acetyl-D-galactosaminidase, beta-D-galactosidase, alpha-D-galactosidase, beta-D-glucosidase, KM-cellulase activities though have been found, but mainly with inconsiderable indices, alpha-D-glucosidase, alpha-D-mannosidase, alpha-L-fucosidase, beta-D-xylosidase and alpha-D-xylosidase activities were found in neither of the studied strains. Strains with rather high proteolytic activity were found among marine species of bacteria. It has been established that 18 strains (28%) of 64 marine isolates were characterized by rather high level of total proteolytic activity (from 0.1 to 05 un/ml), 43.75% of them displayed inconsiderable (up to 0.1 un/ml) or only trace (up to 0.01 un/ml), 18.75% did not display any hydrolytic activity in respect of casein. Investigation of substrate specificity to a number of fibrillar and globular proteins of 9 studied strains, which displayed considerable general (caseinolytic) activity has shown that 8 of them displayed fibrinolytic activity from 0.15 to 2.175 un/ml. All 9 strains were characterized by gelatin activity. Collagenase and keratinase activity was also revealed. Neither of 9 studied strains displayed elastase activity.