Cell immobilization studies using a cellulose-binding domain fused to PrtP in Lactococcus lactis
- Resource Type
- Authors
- Per E. J. Saris; Kari Kylä-Nikkilä; Shanna Liu
- Source
- Bioengineered bugs. 2(3)
- Subject
- Recombinant Fusion Proteins
Cell
Bioengineering
Plasma protein binding
Applied Microbiology and Biotechnology
Cell wall
chemistry.chemical_compound
Bacterial Proteins
Sortase
medicine
Secretion
Cellulose
biology
Lactococcus lactis
Cells, Immobilized
biology.organism_classification
Cellulose binding
digestive system diseases
Protein Structure, Tertiary
Cysteine Endopeptidases
surgical procedures, operative
medicine.anatomical_structure
chemistry
Biochemistry
Biotechnology
Protein Binding
- Language
- ISSN
- 1949-1026
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.