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Purification and N‐terminal amino acid sequence of Enterocin CRL 35, a ‘pediocin‐like’ bacteriocin produced by Enterococcus faecium CRL 35
Author(s) -
Farías M.E.,
Farías R.N.,
Holgado A.P. de Ruiz,
Sesma F.
Publication year - 1996
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1111/j.1472-765x.1996.tb01193.x
Subject(s) - bacteriocin , enterococcus faecium , biology , peptide sequence , size exclusion chromatography , amino acid , microbiology and biotechnology , ion chromatography , peptide , biochemistry , gene , enzyme , antimicrobial , antibiotics
M.E. FARÍAS, R.N. FARÍAS, A.P. DE RUIZ HOLGADO AND F. SESMA. 1996. Enterocin CRL 35, a bacteriocin produced by Enterococcus faecium CRL 35 that inhibits food‐borne pathogens, was purified by precipitation with (NH 4 ) 2 SO 4 , gel filtration, ion exchange and reverse phase chromatography. The partial N‐terminal amino acid sequence indicated a strong homology with other ‘pediocin‐like bacteriocins’ previously described.