Murein Hydrolase Activity in the Surface Layer of Lactobacillus acidophilus ATCC 4356
Murein Hydrolase Activity in the Surface Layer of Lactobacillus acidophilus ATCC 4356
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DOI：
10.1128/aem.01712-08
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发表时间：
2008-12-01
影响因子：
4.4
通讯作者：
Ruzal, Sandra M.
中科院分区：
文献类型：
--
作者：
Prado Acosta, Mariano;Mercedes Palomino, Maria;Ruzal, Sandra M.
我们描述了嗜酸乳杆菌ATCC 4356的表面层（S层）的新的酶功能，即针对肠道沙门氏菌血清型纽波特的细胞壁的内肽酶活性，通过酶谱测定并通过蛋白质印迹鉴定。基于氨基酸序列比较，水解酶活性被预测位于C末端。随后在枯草芽孢杆菌中克隆和表达C-末端结构域，导致酶活性的功能验证。
We describe a new enzymatic functionality for the surface layer (S-layer) of Lactobacillus acidophilus ATCC 4356, namely, an endopeptidase activity against the cell wall of Salmonella enterica serovar Newport, assayed via zymograms and identified by Western blotting. Based on amino acid sequence comparisons, the hydrolase activity was predicted to be located at the C terminus. Subsequent cloning and expression of the C-terminal domain in Bacillus subtilis resulted in the functional verification of the enzymatic activity.