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

Shanna Liu, Kari Kylä-Nikkilä, Per E J Saris
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引用次数: 7

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.  

在乳酸乳球菌中使用纤维素结合结构域与PrtP融合的细胞固定化研究。
XylA的纤维素结合域(CBD)在P45启动子和Usp45分泌信号下与乳球菌衍生的PrtP、NisP和AcmA锚点融合。与锚定PrtP (334 aa)的融合结构显示出最有效的固定。另一方面,CBD-PrtP结构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,表达CBD-NisP锚点融合导致类似的结果。这就提出了一个问题,如果通过分选酶更有效地将锚点结合到细胞壁上,是否可以提高细胞固定到纤维素材料上的效率。然而,用CBD-PrtP融合表达分选酶并没有提高细胞对纤维素的固定化。
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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