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

Authors: Fedorov T.V.¹, Teymurazov M.G.¹, Surin A.K.¹, Tazina O.I.¹, Biketov S.F.¹
Affiliations:
1. “State Research Center for Applied Microbiology and Biotechnology” of the Federal Service for Supervision of Consumer Rights Protection and Human Welfare
Issue: Vol 59, No 5 (2023)
Pages: 457-464
Section: Articles
URL: https://journals.rcsi.science/0555-1099/article/view/138812
DOI: https://doi.org/10.31857/S0555109923050057
EDN: https://elibrary.ru/WTWAXK
ID: 138812

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Abstract
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Abstract

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.

Keywords

Staphylococcus hyicus, CHAP domain, Staphylolytic enzyme, MRSA

References

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