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Information × Registration Number 0225U002434, (0123U102324) , R & D reports Title Secondary metabolites of microorganisms with antibiotic, proteolytic and glycolytic action: patterns of macromolecule organization, functional and biological activity, ways of modification and stabilization, aspects of practical use popup.stage_title Розробити підходи для виділення та очищення мікробних ензимів різного ступеня чистоти, дослідити їхні фізико-хімічні, кінетичні, каталітичні властивості, субстратну специфічність. Дослідити роль окремих амінокислотних залишків у каталітичній активності глікозидаз та протеаз різних мікроорганізмів. Ідентифікувати в геномах стрептоміцетів пучки споріднених генів біосинтезу вторинних метаболітів. Head Varbanets Liudmyla D., д.б.н. Registration Date 11-03-2025 Organization Institute of Microbiology and Virology named after D. K. Zabolotny of the National Academy of Sciences of Ukraine popup.description1 The aim of the work is to develop the fundamentals of obtaining microbial antibiotics, proteases, and glycosidases for the creation of technology for obtaining competitive drugs for medicine and the food industry. In order to realize this goal, the ways of production of secondary metabolites by microorganisms will be investigated, the catalytic properties of enzymes and their substrate specificity will be studied, the mechanisms of inactivation and stabilization by chemical modification will be established, the bundles of related genes for the biosynthesis of secondary metabolites in the genomes of streptomycetes will be studied. popup.description2 It was shown that the fibrin(ogen)ase of Bacillus subtilis 248, isolated from the bottom sediments of the Black Sea, is homogeneous, with a molecular weight of about 30 kDa. The enzyme retained its activity in a wide range of pH and temperatures with optimal values of 9.0 and 4° C. The activating effect on the fibrin(ogen)ase of B. subtilis 248 was shown by Mg2+, Mn2+, Fe2+, Fe3+, Al3+ ions (from 17.1 to 79.5%). The greatest inhibitory effect was shown by Ag3+ ions (55%) and somewhat less (from 9.8 to 25%) by Hg+, Zn2+, Pb+, Cu2+ ions. Studies of the functionally active groups of the active site indicate that the enzyme is a serine protease, its catalytic activity involves carboxyl groups of the C-terminal amino acid (aspartic or glutamic), sulfhydryl groups. Identification of the products of fibrinogen and fibrin hydrolysis by the B. subtilis 248 enzyme indicates that in both cases the cleavage of the Aα-chain of fibrin(ogen) is observed. Of the 20 cultures studied, 18 were able to break down chicken feathers, but only one, Priestia megaterium 035, exhibited the highest level of keratinase activity, and several cultures exhibited disulfide reductase activity: Bacillus pumilus A, Bacillus subtilis 248. These cultures may be promising for the processing of keratin waste generated as a result of the activities of large industrial poultry farms. Lipopolysaccharide was isolated from Escherichia coli K and it was shown that under its influence a high percentage of hemolysis is observed in erythrocytes of all donors. The presence of gene clusters of non-ribosomal peptide synthetases (NRPS) (9) and polyketide synthetases (PKS) (4) in the genome of Streptomyces globisporus and their homology with similar clusters of genes in other streptomycetes (82-94%) has been established. It has been shown that streptomycetes from different compositions consist of sets of different keratinases. Isolated from soil samples, pure cultures of streptomycetes are active producers of antibioti Product Description popup.authors Avdiiuk Kateryna V. Andrianova Tetiana V. Bambura Olha I. Borzova Nataliia V. Brovarska Oksana S. Bulyhina Tetiana V. Harmasheva Inna L. Hyrenko Olha D. Hudzenko Olena V. Dolbik Nadiia M. Zhytkevych Nataliia V. Zvinchuk Iryna O. Lakei Olha F. Lukianchuk Vitalii V. Matseliukh Bohdan P. Nasikovska Oksana P. Polishchuk Lyudmyla V. Postoliuk Tetiana H. Stepaniuk M. V. Yurieva Olena M. popup.nrat_date 2025-03-11 Close