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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Antimicrobial compounds produced by Lactobacillus sakei subsp sakei 2a, a bacteriocinogenic strain isolated from a Brazilian meat product

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Author(s):
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de Carvalho, Katia G. [1, 2] ; Bambirra, Felipe H. S. [3] ; Kruger, Monika F. [1] ; Barbosa, Matheus S. [1] ; Oliveira, Jamil S. [4] ; Santos, Alexandre M. C. [4, 5] ; Nicoli, Jacques R. [3] ; Bemquerer, Marcelo P. [4, 6] ; de Miranda, Antonio [7] ; Salvucci, Emiliano J. [2] ; Sesma, Fernando J. M. [2] ; Franco, Bernadette D. G. M. [1]
Total Authors: 12
Affiliation:
[1] Univ Sao Paulo, Fac Ciencias Farmaceut, Dept Alimentos & Nutr Expt, Sao Paulo - Brazil
[2] Ctr Referencia Lactobacilos CERELA, San Miguel De Tucuman - Argentina
[3] Univ Fed Minas Gerais, Inst Ciencias Biol, Dept Microbiol, Belo Horizonte, MG - Brazil
[4] Univ Fed Minas Gerais, Inst Ciencias Biol, Dept Bioquim & Imunol, Belo Horizonte, MG - Brazil
[5] Univ Fed Espirito Santo, Dept Ciencias Fisiol, Vitoria, ES - Brazil
[6] Embrapa Recursos Genet & Biotecnol Parque Estacao, Brasilia, DF - Brazil
[7] Univ Fed Sao Paulo, Dept Biofis, Sao Paulo - Brazil
Total Affiliations: 7
Document type: Journal article
Source: Journal of Industrial Microbiology & Biotechnology; v. 37, n. 4, p. 381-390, APR 2010.
Web of Science Citations: 20
Abstract

Bacteriocins produced by lactic acid bacteria are gaining increased importance due to their activity against undesirable microorganisms in foods. In this study, a concentrated acid extract of a culture of Lactobacillus sakei subsp. sakei 2a, a bacteriocinogenic strain isolated from a Brazilian pork product, was purified by cation exchange and reversed-phase chromatographic methods. The amino acid sequences of the active antimicrobial compounds determined by Edman degradation were compared to known protein sequences using the BLAST-P software. Three different antimicrobial compounds were obtained, P1, P2 and P3, and mass spectrometry indicated molecular masses of 4.4, 6.8 and 9.5 kDa, respectively. P1 corresponds to classical sakacin P, P2 is identical to the 30S ribosomal protein S21 of L. sakei subsp. sakei 23 K, and P3 is identical to a histone-like DNA-binding protein HV produced by L. sakei subsp. sakei 23 K. Total genomic DNA was extracted and used as target DNA for PCR amplification of the genes sak, lis and his involved in the synthesis of P1, P2 and P3. The fragments were cloned in pET28b expression vector and the resulting plasmids transformed in E. coli KRX competent cells. The transformants were active against Listeria monocytogenes, indicating that the activity of the classical sakacin P produced by L. sakei 2a can be complemented by other antimicrobial proteins. (AU)