title: Easy and rapid purification of highly active nisin.
abstract: Nisin is an antimicrobial peptide produced and secreted by several L. lactis strains and is specifically active against Gram-positive bacteria. In previous studies, nisin was purified via cation exchange chromatography at low pH employing a single-step elution using 1 M NaCl. Here, we describe an optimized purification protocol using a five-step NaCl elution to remove contaminants. The obtained nisin is devoid of impurities and shows high bactericidal activity against the nisin-sensitive L. lactis strain NZ9000. Purified nisin exhibits an IC(50) of ~3 nM, which is a tenfold improvement as compared to nisin obtained via the one-step elution procedure.
authors.affiliation: Institute of Biochemistry, Heinrich Heine University Düsseldorf, Universitätsstrabe 1, 40225 Düsseldorf, Germany.
authors.forename: André
authors.initials: A
authors.lastname: Abts
authors.forename: Antonino
authors.initials: A
authors.lastname: Mavaro
authors.forename: Jan
authors.initials: J
authors.lastname: Stindt
authors.forename: Patrick J
authors.initials: PJ
authors.lastname: Bakkes
authors.forename: Sabine
authors.initials: S
authors.lastname: Metzger
authors.forename: Arnold J M
authors.initials: AJ
authors.lastname: Driessen
authors.forename: Sander H J
authors.initials: SH
authors.lastname: Smits
authors.forename: Lutz
authors.initials: L
authors.lastname: Schmitt