Isolation, Purification and some Properties of Staphylolytic Enzyme from  Staphylococcus hyicus

T. V. Fedorov; Федоров Т. В.; M. G. Teymurazov; Теймуразов М. Г.; A. K. Surin; Сурин А. К.; O. I. Tazina; Тазина О. И.; S. F. Biketov; Бикетов С. Ф.

doi:10.31857/S0555109923050057

Isolation, Purification and some Properties of Staphylolytic Enzyme from Staphylococcus hyicus

Autores: Fedorov T.V.¹, Teymurazov M.G.¹, Surin A.K.¹, Tazina O.I.¹, Biketov S.F.¹
Afiliações:
1. “State Research Center for Applied Microbiology and Biotechnology” of the Federal Service for Supervision of Consumer Rights Protection and Human Welfare
Edição: Volume 59, Nº 5 (2023)
Páginas: 457-464
Seção: Articles
URL: https://cardiosomatics.ru/0555-1099/article/view/674598
DOI: https://doi.org/10.31857/S0555109923050057
EDN: https://elibrary.ru/WTWAXK
ID: 674598

Citar

Texto integral

Acesso aberto
Acesso é fechado

Acesso está concedido
Acesso é fechado

Somente assinantes

Resumo
Sobre autores
Bibliografia
Arquivos suplementares
Estatísticas

Resumo

The paper presents data on the identification of a new staphylolytic enzyme from the cultural liquid of Staphylococcus hyicus B-8870. The primary sequence of the enzyme has the maximum similarity to the CHAP domain of N-acetylmuramoyl-L-alanine amidase from Staphylococcus sciuri DD 4747. The enzyme is active against a wide range of microorganisms of the Staphylococcus genus, including MRSA strains. The molecular weight of the enzyme is 13993 Da, the absorption coefficient at 280 nm is \(\varepsilon \frac{{{\text{mg}}}}{{{\text{ml}}}}\) 3.94, the value of the isoelectric point pI 10.35. The specific activity of the enzyme in relation to the cell suspension of S.aureus FDA 209P is 1518 U/mg with an optimum pH of 7.7 and a temperature of 40°C.

Palavras-chave

Staphylococcus hyicus, CHAP domain, Staphylolytic enzyme, MRSA

Bibliografia

Karam G., Chastre J., Wilcox M., Vincent J.-L. // Critical Care. 2016. V. 20. P. 136–145.
Vermassen A., Leroy S., Talon R., Provot C., Popowska M., Desvaux M. // Front. Microbiol. 2019. V. 10. P. 331–358.
Son B., Kong M., Ryu S. // Viruses. 2018. V. 10. P. 284–296.
Fujiki J., Nakamura T., Furusawa T., Ohno H., Takahashi H., Kitana J., Usui M., Higuchi H., Tanji Y., Tamura Y., Iwano H. // Pharmaceuticals. 2018. V. 11. P. 25–44.
Bateman A., Rawlings N.D. // Trends Biochem. Sci. 2003. V. 28. P. 234–237.
Rigden D.J., Jedrzejas M.J., Galperin M.Y. // Trends Biochem. Sci. 2003. V. 28. P. 230–234.
Llull D., Lopez R., Garcia E. // FEBS Lett. 2006. V. 580. P. 1959–1964.
Becker S.C., Dong S., Baker J.R., Foster-Frey J., Pritchard D.G., Donovan D. M. // FEMS Microbiol. Lett. 2009. V. 294. P. 52–60.
Frankel M.B., Schneewind O. // J. Biol. Chem. 2012. № 287. P. 10460–10471.
Zou Y., Hou C. // Comput. Biol. Chem. 2010. V. 34. P. 251–257.
Li X., Wang S., Nyaruaba R., Liu H., Yang H., Wei H.A. // Antibiotics. 2021. V. 10. P. 461–474.
Ennahar S., Sashihara T., Sonomoto K., Ishizaki A. // FEMS Microbiol. Rev. 2000. V. 24. P. 85–106.
Alispahic M., Hummel K., Jandreski-Cvetkovic D. et al. // J. Med. Microbiol. 2010. V. 59. P. 295–301.
Laemmli U.K. // Nature. 1970. V. 227 № 5259. P. 680–685.
Heath L.S., Gargis S.R., Smithberg S.R., Johnson H.P., Heath H.E., LeBlanc P.A., Sloan G.L. // FEMS Microbiol. Lett. 2005. V. 249. P. 227–231.
J., Yang R., Yu S., Zhao W. // J Dairy Sci. 2021. V. 104. P. 2641–2653.