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Purification and characterization of a bacteriocin produced by Lactobacillus acidophilus IBB 801
Author(s) -
Zamfir M.,
Callewaert R.,
Cornea P. C.,
Savu L.,
Vatafu I.,
De Vuyst L.
Publication year - 1999
Publication title -
journal of applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 1364-5072
DOI - 10.1046/j.1365-2672.1999.00950.x
Subject(s) - bacteriocin , lactobacillus acidophilus , microbiology and biotechnology , lactobacillaceae , biology , bacteria , lactobacillus , probiotic , antimicrobial , genetics
M. ZAMFIR, R. CALLEWAERT, P.C. CORNEA, L. SAVU, I. VATAFU and L. DE VUYST.1999. Lactobacillus acidophilus IBB 801 produces a small bacteriocin, designated acidophilin 801, with an estimated molecular mass of less than 6·5 kDa. It displays a narrow inhibitory spectrum (only related lactobacilli but including the Gram‐negative pathogenic bacteria Escherichia coli Row and Salmonella panama 1467) with a bactericidal activity. The antimicrobial activity of cell‐free culture supernatant fluid was insensitive to catalase but sensitive to proteolytic enzymes such as trypsin, proteinase K and pronase, heat‐stable (30 min at 121 °C), and maintained in a wide pH range. The proteinaceous compound was isolated from cell‐free culture supernatant fluid and purified. Crude bacteriocin was isolated as a floating pellicle after ammonium sulphate precipitation (40% saturation) and partially purified by extraction/precipitation with chloroform/methanol (2/1, v/v). Further purification to homogeneity was performed by reversed phase Fast Performance Liquid Chromatography. The amino acid composition was determined. Amino acid sequencing revealed that the N‐terminal end was blocked.