[Screening of α-L-Rhamnosidases and Peptidases among Actinobacterium and Bacilli].

Purpose: To carry out screening of peptidases and α-L-rhamnosidases producers among actinobacterium and bacilli. Methods: The biochemical methods of α-L-rhamnosidase, elastase, caseinolytic, fibrinolytic and collagenase activity determination have been used. Results: Among 31 strains of actinobacterium and 24 strains of bacilli it was not exhibited any enzyme with elactolytic activity, while a number of actinobacterium strains displayed high collagenase activity. As to bacilli, elastolytic activity was observed only in five strains, however its level is not an interest for future investigations. Bacillus subtilis 121 and 108 exerted enough high activity (0.100 and 0.092 U/mg of protein respectively). Conclusion: The most effective producer of collagenase and α-L-rhamnosidase is actinobacterium strain 6/5 isolated from nettle zhisosphere,while peptidase with fibrinolytic activity - B. subtilis 121 and 108. We believe these strains may be perspective for further researches.

[Physico-Chemical Properties of Achromobacter SP. α-Amylase].

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, -ß-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).

[ABILITY OF MICROORGANISMS FROM DIFFERENT ECOLOGICAL NICHES TO HYDROLYZE THE INSOLUBLE PROTEINS].

Screening of protease producers with specificity to insoluble and hard soluble protein substrates of animal origin (collagen, fibrin, elastin and keratin) was carried out. It was studied the bacterial cultures (24 strains) isolated from water and periphyton of enclosures with dolphins, and also from exhalations, oral cavity and skin of dolphins. Some bacterial strains isolated from water and periphyton of enclosures hydrolyzed collagen (5-23 U/ml) and elastin (20-32 U/ml). Thus all tested cultures did not possess the property of extracellular keratinases synthesis. The streptomycetes (48 strains) were isolated from the soil of Black Sea coastal strip near Odessa and Saky, from parkland and the shores of freshwater lake in Saky and from the soil of Atlantic Ocean coastal strip near Albufena (Portugal). Several streptomycetes have been found to appeare the perspective producers of extracellular keratinase and collagenase. The strains isolated from the soil of the coastal strip area both sea and freshwater lake in Saky possessed the highest activity (up to 5 U/mg).