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

—This 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 maximum similarity to the CHAP domain of N-acetylmuramoyl-L-alanine amidase from Staphylococcus sciuri DD 4747. The enzyme is...

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Bibliographic Details
Published in:Applied biochemistry and microbiology 2023-10, Vol.59 (5), p.622-629
Main Authors: Fedorov, T. V., Teymurazov, M. G., Surin, A. K., Tazina, O. I., Biketov, S. F.
Format: Article
Language:English
Subjects:
Absorptivity
Alanine
Amidase
Biochemistry
Biomedical and Life Sciences
Drug resistance
L-Alanine
Life Sciences
Medical Microbiology
Microbiology
Microorganisms
Molecular weight
N-Acetylmuramoyl-L-alanine amidase
Staphylococcus
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Summary:—This 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 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 13 993 Da, the absorption coefficient at 280 nm is 3.94 , and the isoelectric point is 10.35. The specific activity of the enzyme in relation to S. aureus FDA 209P cell suspension is 1518 U/mg with pH optimum of 7.7 and a temperature of 40°C.
ISSN:0003-6838
1608-3024
DOI:10.1134/S0003683823050058