Abts André, Mavaro Antonino, Stindt Jan, Bakkes Patrick J, Metzger Sabine, Driessen Arnold J M, Smits Sander H J, Schmitt Lutz
Institute of Biochemistry, Heinrich Heine University Düsseldorf, Universitätsstrabe 1, 40225 Düsseldorf, Germany.
Int J Pept. 2011;2011:175145. doi: 10.1155/2011/175145. Epub 2011 Sep 18.
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.
乳链菌肽是由几种乳酸乳球菌菌株产生并分泌的一种抗菌肽,对革兰氏阳性菌具有特异性活性。在先前的研究中,乳链菌肽是在低pH值下通过阳离子交换色谱法,采用1 M NaCl一步洗脱进行纯化的。在此,我们描述了一种优化的纯化方案,使用五步NaCl洗脱来去除污染物。所获得的乳链菌肽不含杂质,并且对乳链菌肽敏感的乳酸乳球菌菌株NZ9000显示出高杀菌活性。纯化后的乳链菌肽的半数抑制浓度(IC50)约为3 nM,与通过一步洗脱程序获得的乳链菌肽相比有了十倍的提高。