Modification of Bacillus sp. IMV B-7883 Elastase Activity by the Hetero-Metallic Carboxylatogermanates/Stannates
DOI:
https://doi.org/10.15407/microbiolj86.04.033Keywords:
Bacillus sp. IMV B-7883, elastase activity, hetero-metallic carboxylatogermanates/stannates complexesAbstract
In recent years, some researchers have found that although many Gram-negative and Gram-positive bacteria secrete elastase, the bacterial forms of elastase have either a low activity or harmful effects. Therefore, further research is needed in isolating and screening microorganisms that produce a high level of elastase activity. Previously we selected strain Bacillus sp. IMV B-7883, which exhibits fairly high elastase activity. To increase its activity, we chose one of the well-known approaches, in particular, the use of a number of coordination compounds capable to influence elastase activity. In this regard, the purpose of this work was to study the effect of such coordination compounds as hetero-metallic carboxylatogermanates/stannates on the elastase activity of Bacillus sp. IMV B-7883. Methods. The object of the investigation was the strain of Bacillus sp., deposited in the Ukrainian Collection of Microorganisms under the number IMV B-7883, isolated from soil. The culture was grown under conditions of submerged cultivation at 28 °С, with a mixing speed of the nutrient medium of 244 rpm for three to six days (72–144 hours). We used an enzyme purified from the supernatant of the culture liquid by precipitation with 90% ammonium sulfate, with further fractionation on neutral and charged carriers. Elastase activity was determined colorimetrically by the intensity of the color of the solution upon enzymatic hydrolysis of elastin stained with Congo red. As modifiers of enzyme activity, hetero-metallic carboxylatogermanates/stannates were used. Results. Of the 15 studied in this work coordination compounds presented by hetero-metallic carboxylatogermanates/stannates, only 1 [Ba(H2O)6][Ge2(OH)2(C6H8O7)2]·nH2O, n=2 and 3 [Ni (H2O)6][Ge2(OH)2(C6H8O7)2]·nH2O, n=4, depending on the concentration used and incubation time, increase the elastase activity by only 3–5%. All other compounds have an inhibitory effect. Conclusions. Obtained data on the inhibitory effect of hetero-metallic carboxylatogermanates/stannates on the elastase activity of Bacillus sp. IMV B-7883 provide new information which may help in solving the issue of the mechanism of interaction between enzymes and complex chemical molecules.
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Afanasenko, E., Seifullina, I., Martsinko, E., Dyakonenko, V., Shishkina, S., Gudzenko, O., & Varbanets, L. (2023). Supramolecular organization and enzyme-effector properties of double coordination salts with malatostannate/germanate(IV) anions and Fe(II), Co(II), Ni(II), Cu(II) 1,10-phenanthroline cations. Journal of Molecular Structure, 1271, 133996. https://doi.org/10.1016/j.molstruc.2022.133996
Atanasov, A. G., Zotchev, S. B., Dirsch, V. M., International Natural Product Sciences Taskforce, & Supuran, C. T. (2021). Natural products in drug discovery: advances and opportunities. Nature reviews. Drug discovery, 20(3), 200–216. https://doi.org/10.1038/s41573-020-00114-z
Chen, Q., Ruan, H., Zhang, H., Ni, H., & He, G. (2007). Enhanced production of elastase by Bacillus licheniformis ZJUEL31410: optimization of cultivation conditions using response surface methodology. Journal of Zhejiang University SCIENCE B, 8(11), 845–852. https://doi.org/10.1631/jzus.2007.B0845
Gudzenko, О. V., Varbanets, L. D., & Seifullina, І. I. (2020). The influence of coordinative tartrate and malatogermanate compounds on the activity of ?-L-rhamnosidase preparations from Penicillium tardum, Eupenicillium erubescens and Cryptococcus albidus. The Ukrainian Biochemical Journal, 92(4), 85–95. https://doi.org/10.15407/ubj92.04.085
Gudzenko, O. V., Borzova, N. V., Varbanets, L. D., Seifullina, I. I., Martsinko, E. E., Buchko, O. V., & Pesaroglo, А. G. (2023a). Influence of New Types of Biscitratogermanates on Penicillium restrictum α-L-Rhamnosidase. Mikrobiolohichnyi Zhurnal, 85(3), 3–11. https://doi.org/10.15407/microbiolj85.03.003
Gudzenko, O. V., Borzova, N. V., Varbanets, L. D., Seifullina, I. I., Martsinko, О. E., & Chebanenko, О. A. (2023b). Germanium (IV) Complexes with Gluconic Acid as Effectors of Penicillium tardum and Eupenicillium erubescens α-L-Rhamnosidases. Mikrobiolohichnyi Zhurnal, 85(4), 58–65. https://doi.org/10.15407/microbiolj85.04.058
Gudzenko, O. V., Borzova, N. V., Varbanets, L. D., Seifullina, I. I., Martsinko, O. E., & Afanasenko, E. V. (2023c). The influence of coordination compounds with malatogermanate/stannate anions and 1,10-phenanthroline cations of 3d metals on α-L-rhamnosidase activity of Penicillium tardum, Penicillium restrictum and Eupenicillium erubescens. The Ukrainian Biochemical Journal, 95(4), 46–54. https://doi.org/10.15407/ubj95.04.046
Gudzenko, O. V., Varbanets, L. D. (2023). Characterization of Bacillus sp. IMV B-7883 proteases. The Ukrainian Biochemical Journal, 95(6), 46–54. https://doi.org/10.15407/ubj95.05.098
Insuasty, D., Castillo, J., Becerra, D., Rojas, H., & Abonia, R. (2020). Synthesis of Biologically Active Molecules through Multicomponent Reactions. Molecules (Basel, Switzerland), 25(3), 505. https://doi.org/10.3390/molecules25030505
Kaul, P., & Asano, Y. (2012). Strategies for discovery and improvement of enzyme function: state of the art and opportunities. Microbial biotechnology, 5(1), 18–33. https://doi.org/10.1111/j.1751-7915.2011.00280.x
Korkmaz, B., Horwitz, M. S., Jenne, D. E., & Gauthier, F. (2010). Neutrophil elastase, proteinase 3, and cathepsin G as therapeutic targets in human diseases. Pharmacological reviews, 62(4), 726–759. https://doi.org/10.1124/pr.110.002733
Kotb, E., Alabdalall, A. H., Alsayed, M. A., Alghamdi, A. I., Alkhaldi, E., AbdulAzeez, S., & Borgio, J. F. (2023). Isolation, Screening, and Identification of Alkaline Protease-Producing Bacteria and Application of the Most Potent Enzyme from Bacillus sp. Mar64. Fermentation, 9(7), 637. https://doi.org/10.3390/fermentation9070637
Kunder, M., Lakshmaiah, V., & Moideen Kutty, A. V. (2022). Selective decrease in alpha1-antitrypsin levels in diabetic retinopathy: Could the levels of it be playing a role in the pathophysiology of diabetic retinopathy? The Indian journal of medical research, 156(1), 104–110. https://doi.org/10.4103/ijmr.IJMR_1293_19
López-Otín, C., & Bond, J. S. (2008). Proteases: multifunctional enzymes in life and disease. The Journal of biological chemistry, 283(45), 30433–30437. https://doi.org/10.1074/jbc.R800035200
Mechri, S., Bouacem, K., Amziane, M., Dab, A., Nateche, F., & Jaouadi, B. (2019). Identification of a New Serine Alkaline Peptidase from the Moderately Halophilic Virgibacillus natechei sp. nov., Strain FarDT and its Application as Bioadditive for Peptide Synthesis and Laundry Detergent Formulations. BioMed research international, 6470897. https://doi.org/10.1155/2019/6470897
Mótyán, J. A., Tóth, F., & Tőzsér, J. (2013). Research applications of proteolytic enzymes in molecular biology. Biomolecules, 3(4), 923–942. https://doi.org/10.3390/biom3040923
Seifullina, I., Martsinko, E., Chebanenko, E., Pirozhok, O., Dyakonenko, V., & Shishkina, S. (2016). Synthesis and Structural Characteristics of Bis(Citrate)Germanates(IV) (Hbipy)2[Ge(HCit)2]·2H2 and [CuCl(bipy)2]2[Ge(HCit)2]·8H2O. Chemistry Journal of Moldova, 11(2), 52–57. https://doi.org/10.19261/cjm.2016.11(2).11
Seifullina, I., Martsinko, E., Chebanenko, E., Afanasenko, E., Dyakonenko, V., & Shishkina, S. (2017a). Synthesis, Structure and Investigation of Germanium(IV) and Copper(II) Complexes with Malic Acid and 1,10ʹ-phenanthroline. Chemistry Journal of Moldova, 12(2), 28–33. https://doi.org/10.19261/cjm.2016.369
Seifullina, I. I., Martsinko, E. E., Chebanenko, E. A., Pirozhok, O. V., Dyakonenko, V. V., & Shishkina, S. V. (2017b). Structure of bis(citrato)germanates with different types of cations: (Hphen)2[Ge(HCit)2·3H2O], [CuCl(phen)2]2[Ge(HCit)2·6H2O], where H4Cit is citric acid, phen IS 1,10-phenanthroline. Journal of Structural Chemistry, 58(3), 532–538. https://doi.org/10.1134/S0022476617030143
Su, Y., Liu, C., Fang, H., & Zhang, D. (2020). Bacillus subtilis: a universal cell factory for industry, agriculture, biomaterials and medicine. Microbial cell factories, 19(1), 173. https://doi.org/10.1186/s12934-020-01436-8
Trowbridge, J. O., & Moon, H. D. (1972). Purification of human Society for Experimental Biology and Medicine (New York, N.Y.), 141(3), 928–931. https://doi.org/10.3181/00379727-141-36903
Wen, G., An, W., Chen, J., Maguire, E. M., Chen, Q., Yang, F., Pearce, S. W. A., Kyriakides, M., Zhang, L., Ye, S., Nourshargh, S., & Xiao, Q. (2018). Genetic and Pharmacologic Inhibition of the Neutrophil Elastase Inhibits Experimental Atherosclerosis. Journal of the American Heart Association, 7(4), e008187. https://doi.org/10.1161/JAHA.117.008187
Wiltschi, B., Cernava, T., Dennig, A., Galindo Casas, M., Geier, M., Gruber, S., Haberbauer, M., Heidinger, P., Herrero Acero, E., Kratzer, R., Luley-Goedl, C., Müller, C. A., Pitzer, J., Ribitsch, D., Sauer, M., Schmölzer, K., Schnitzhofer, W., Sensen, C. W., Soh, J., Steiner, K., & Wriessnegger, T. (2020). Enzymes revolutionize the bioproduction of value-added compounds: From enzyme discovery to special applications. Biotechnology advances, 40, 107520. https://doi.org/10.1016/j.biotechadv.2020.107520
Yang, Z., Huang, Z., Wu, Q., Tang, X., & Huang, Z. (2023). Cold-Adapted Proteases: An Efficient and Energy-Saving Biocatalyst. International Journal of Molecular Sciences, 24(10), 8532. https://doi.org/10.3390/ijms24108532
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