NEW BACTERIOLYTIC ENZYME PREPARATION N-ACETYL-D-GLUCOSAMINIDASE
Main Article Content
Authors
A.M. Rozhkova
Federal Research Centre ‘Fundamental Bases of Biotechnology’ of the Russian Academy of Sciences, Russian Federation, 119071, Moscow, 33 Leninsky Prospekt, building 2
A.M. Chulkin
Federal Research Centre ‘Fundamental Bases of Biotechnology’ of the Russian Academy of Sciences, Russian Federation, 119071, Moscow, 33 Leninsky Prospekt, building 2
I.G. Sinelnikov
Federal Research Centre ‘Fundamental Bases of Biotechnology’ of the Russian Academy of Sciences, Russian Federation, 119071, Moscow, 33 Leninsky Prospekt, building 2
O.A. Sinitsyna
Lomonosov Moscow State University, Department of Chemistry, Russian Federation, 119991, Moscow,1 Leninskie Gory, building 11
I.N. Zorov
Federal Research Centre ‘Fundamental Bases of Biotechnology’ of the Russian Academy of Sciences, Russian Federation, 119071, Moscow, 33 Leninsky Prospekt, building 2
Lomonosov Moscow State University, Department of Chemistry, Russian Federation, 119991, Moscow,1 Leninskie Gory, building 11
A.P. Sinitsyn
Lomonosov Moscow State University, Department of Chemistry, Russian Federation, 119991, Moscow,1 Leninskie Gory, building 11
Abstract
A new nag1 gene encoding N-acetyl-D-glucosaminidase from Streptomyces kursanovii was cloned. The soluble form of N-acetyl-D-glucosaminidase was obtained after improving its expression in E. coli ArcticExpressTM (DE3) cells. The homogeneous form of the enzyme was isolated by affinity chromatography, and its bacteriolytic ability against cells of the Gram-positive bacterium Micrococcus lysodeikticus was studied. It was demonstrated that the new enzyme's bacteriolytic capacity surpasses that of chicken lysozyme.
Keywords
gene, enzyme preparation, glucosaminidase, feed antibiotics, lysozyme, probiotic
Article Details
References
Moroz OV, Blagova E, Taylor E, Turkenburg JP, Skov LK, Gippert GP, Schnorr KM, Ming L, Ye L, Klausen M, Cohn MT, Schmidt EGW, Nymand-Grarup S, Davies GJ, Wilson KS. Fungal GH25 muramidases: New family members with applications in animal nutrition and a crystal structure at 0.78Å resolution // PLoS One. – 2021 Mar 12. – Vol. 16(3). – Р. e0248190. doi: 10.1371/journal.pone.0248190.
Lombard V, Ramulu HG, Drula E, Coutinho PM, Henrissat B. The carbohydrate-active enzymes data-base (CAZy) in 2013 // Nucleic Acids Res. – 2014. – Vol. 42(D1). – P.D490–D5. Crossref
Consortium CAZypedia. Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes // Glycobiology. – 2018. – Vol.28(1). – P. 3–8. Epub 2017/10/19. Crossref
Sais M., Barroeta A.C., López-Colom P., Nofrarías M., Majó N., Lopez-Ulibarri R., Pérez Calvo E., Martín-Orúe S M. Evaluation of dietary supplementation of a novel microbial muramidase on gastrointestinal unctionality and growth performance in broiler chickens // Poultry Science. – 2020. – Vol. 99 (1). – P.235-245, Crossref.
Hussain AM., Daniel RC., Frost AJ. The bactericidal effect of N-acetyl-beta-D-glucosaminidase on bacteria // Vet Microbiol. – 1992, Jul. – Vol.32(1). – P.75-80. doi: 10.1016/0378-1135(92)90008-h.
Rathee A., Panwar A., Kumari S., Chhibber S., Kumar A. Functional Characterization and Structural Modelling of Peptidoglycan Degrading β-N-acetyl-glucosaminidase from a Dental Isolate of Serratia marcescens // Comb Chem High Throughput Screen. – 2021. – Vol. 24(9). – P.1514-1526. doi: 10.2174/1386207323999201103204234.
Patent RU 206175C1, data publikacii 10.06.1996.
Aslanidis C., de Jong P.J. Ligation-independent cloning of PCR products (LIC-PCR) // Nucleic Acids Res. – 1990. – Vol. 18. – P. 6069–6074
James P. Proteome Research: Mass Spectrometry // Heidelberg: Springer Verlag. – 2001. – 274 p.
Sedov S.A., Belogurova N.G., Shipovskov S., Levashov A.V., Levashov P.A. Lysis of Escherichia coli cells by lysozyme: Discrimination between adsorption and enzyme action// Colloids and Surfaces B: Biointerfaces. – 2011. – Vol. 88 (1). – Р.131-133
Hell W, Meyer HG, Gatermann SG. Cloning of aas, a gene encoding a Staphylococcus saprophyticus surface protein with adhesive and autolytic properties // Mol Microbiol. – 1998, Aug. – Vol. 29(3). – P.871-81. doi: 10.1046/j.1365-2958.1998.00983.x. PMID: 9723925.
de Ruyter PGGA, Kuipers OP, Meijer WC, deVos WM. Food-grade controlled lysis of Lactococcus lactis for accelerated cheese ripening // Nat Biotechnol. – 1997. – Vol. 15(10). – P.976-9. Crossref