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利用与乳酸乳球菌中PrtP融合的纤维素结合结构域进行细胞固定化研究。

Cell immobilization studies using a cellulose-binding domain fused to PrtP in Lactococcus lactis.

作者信息

Liu Shanna, Kylä-Nikkilä Kari, Saris Per E J

机构信息

School of Chemical Engineering and Technology, Tianjin University, Tianjin, China.

出版信息

Bioeng Bugs. 2011 May-Jun;2(3):160-2. doi: 10.4161/bbug.2.3.15348. Epub 2011 May 1.

Abstract

The cellulose-binding domain (CBD) of XylA was fused with PrtP, NisP and AcmA anchors derived from Lactococcus lactis under P45 promoter and Usp45 secretion signal. The fusion construct with the anchor PrtP (334 aa) was shown to exhibit the most efficient immobilization. The CBD-PrtP construct on the other hand was not efficiently attached to the cell wall and as such was found mainly in the supernatant. Results also showed that expression of the CBD-NisP anchor fusion led to a similar result. This raised the question if more efficient binding of the anchor to the cell wall by sortase could enhance the efficiency of cell immobilization to the cellulosic material. However, expressing sortase with the CBD-PrtP fusion did not improve the immobilization of the cells to cellulose.

摘要

在P45启动子和Usp45分泌信号的作用下,木聚糖酶A(XylA)的纤维素结合结构域(CBD)与源自乳酸乳球菌的PrtP、NisP和AcmA锚定蛋白融合。带有PrtP锚定蛋白(334个氨基酸)的融合构建体表现出最有效的固定化效果。另一方面,CBD-PrtP构建体不能有效地附着在细胞壁上,因此主要存在于上清液中。结果还表明,CBD-NisP锚定融合蛋白的表达也导致了类似的结果。这就提出了一个问题,即分选酶是否能更有效地将锚定蛋白与细胞壁结合,从而提高细胞固定在纤维素材料上的效率。然而,将分选酶与CBD-PrtP融合表达并没有改善细胞在纤维素上的固定化效果。

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