Dipartimento di Scienze Molecolari Agroalimentari, Università degli Studi, Milano, Italy.
FEMS Microbiol Lett. 2012 Sep;334(2):143-9. doi: 10.1111/j.1574-6968.2012.02630.x. Epub 2012 Aug 2.
Sakacin A was purified to homogeneity through simple chromatographic procedures from cultures of Lactobacillus sakei DSMZ 6333 grown on a low-cost medium. The highly purified protein dissipated both transmembrane potential (ΔΨ) and transmembrane pH gradient (ΔpH) in Listeria cells in a very intense, rapid, and energy-dependent fashion. On a slower timescale, purified sakacin A also showed a lytic activity toward isolated cell walls of Listeria. Mass spectrometry was used to analyze the products of sakacin A action on cell walls, evidencing that sakacin A acts on various types of bonds within peptoglycans.
通过从在低成本培养基上生长的乳杆菌属 sakei DSMZ 6333 的培养物中进行简单的色谱程序,将 Sakacin A 纯化为均质。高度纯化的蛋白质以非常强烈、快速和能量依赖的方式耗散李斯特菌细胞中的跨膜电势 (ΔΨ) 和跨膜 pH 梯度 (ΔpH)。在较慢的时间尺度上,纯化的 sakacin A 也对李斯特菌的分离细胞壁表现出溶细胞活性。质谱法用于分析 sakacin A 对细胞壁作用的产物,证明 sakacin A 作用于肽聚糖中的各种类型的键。