| 초록 |
Novel immobilization techniques have many potential applications. Although sol-gel method has been used to encapsulate various biomolecules, the harsh reaction condition limits its application. Recently, it is reported that Silaffin polypeptides derived from Cylindrotheca fusiformis catalyze the silica formation in vitro at mild condition. The synthetic peptide(R5), the repeat unit of the Silaffin polypeptide without posttranslational modification, shows the activity of silica formation within minutes when added to a silica precursor at ambient condition. In our research, we designed the GFP chimeric protein with R5 peptide. R5 peptide was genetically fused to C-terminus or N-terminus of the target protein(GFP). The biosilicification in vitro was carried out with the GFP-R5 chimeric protein by mixing with TMOS, a silica precursor. SEM and IR spectroscope analysis confirmed that the GFP was encapsulated in a silica matrix. The efficiency of protein immobilization was compared between GFP-R5 chimeric protein and R5 peptide alone. Compared with R5 peptide alone, GFP-R5 chimeric protein showed excellent immobilization efficiency. This novel immobilization method will be applicable for stabilizing commercially valuable enzyme & proteins. |
