高活性nisin的简易快速纯化。

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

摘要

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。

Easy and rapid purification of highly active nisin.

Easy and rapid purification of highly active nisin.

Easy and rapid purification of highly active nisin.

Easy and rapid purification of highly active nisin.

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.

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