Easy and Rapid Purification of Highly Active Nisin. (18th September 2011)

• Record Type: Journal Article
• Authors: Abts, André; Mavaro, Antonino; Stindt, Jan; Bakkes, Patrick J.; Metzger, Sabine; Driessen, Arnold J. M.; Smits, Sander H. J.; Schmitt, Lutz
• Other Names: Temussi Piero Andrea Academic Editor.
• Is Part Of: International journal of peptides. Volume 2011(2011)
• Publication Date: 2011-09-18
• Subjects: Peptides -- Periodicals; Peptides; Peptides; Electronic journals; Periodical; Periodicals; Periodicals; Internet Resources; Fulltext
• DOI: 10.1155/2011/175145
• Languages: English
• ISSNs: 1687-9767

Abstract

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 IC50 of ~3 nM, which is a tenfold improvement as compared to nisin obtained via the one-step elution procedure.