Improvement of extracellular secretion efficiency of Bacillus naganoensis pullulanase from recombinant Escherichia coli: Peptide fusion and cell wall modification

In this study, both strategies showed positive influence on the extracellular secretion of pullulanase. After fusing a negatively charged peptide at the N-terminal, the extracellular enzymatic activity increased by more than 4 times compared to the pullulanase without peptide fusion. By modifying the permeability of the cell wall, the extracellular enzymatic activity increased by 12 times. In addition, the two strategies were also used to improve the secretion efficiency of the truncated pullulanase ΔN106, which has higher enzymatic activity than the full-length protein. The strategies employed have valuable implications for increasing the extracellular secretion efficiency of target proteins from recombinant E. coli.
Source: Protein Expression and Purification - Category: Biochemistry Source Type: research