Easy and Rapid Purification of Highly Active NisinAbts, A., Mavaro, A., Stindt, J., Bakkes, P. J., Metzger, S., Driessen, A. J. M., Smits, S. H. J. & Schmitt, L., 2011, In : International Journal of Peptides. 2011, 1, p. 1-9 10 p., 175145.
Research output: Contribution to journal › Article › Academic › peer-review
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 1M 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.
|Number of pages||10|
|Journal||International Journal of Peptides|
|Publication status||Published - 2011|
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