Easy and rapid purification of highly active nisin.

International Journal of Peptides Pub Date : 2011-01-01 Epub Date: 2011-09-18 DOI:10.1155/2011/175145
André Abts, Antonino Mavaro, Jan Stindt, Patrick J Bakkes, Sabine Metzger, Arnold J M Driessen, Sander H J Smits, Lutz Schmitt
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引用次数: 58

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.

Abstract Image

Abstract Image

Abstract Image

高活性nisin的简易快速纯化。
Nisin是由几种乳杆菌菌株产生和分泌的抗菌肽,对革兰氏阳性菌具有特异性活性。在以前的研究中,nisin是通过低pH下的阳离子交换色谱纯化的,采用1 M NaCl一步洗脱。在这里,我们描述了一种优化的净化方案,使用五步NaCl洗脱去除污染物。所得nisin不含杂质,对nisin敏感乳杆菌NZ9000具有较高的杀菌活性。纯化的nisin显示出~3 nM的IC(50),与通过一步洗脱程序获得的nisin相比,这是十倍的改进。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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