원문정보
초록
영어
In the diatom Cylindrotheca fusiformis, modified peptidescalled silaffin polypeptides are responsible for silica deposition in vitro at ambient conditions. Recently, it is discovered that the synthetic peptide called R5 peptide, the repeat unit of the silaffin polypeptide without posttranslational modification, was capable of precipitating silica in vitro within minutes as well when added to a silicic acid at ambient condition. Herein we generated GFP chimeric protein, which is a model protein, by incorporating synthetic silaffin R5 peptide as well as other
unmodified silaffin domains (R1~R7) identified from Cylindrotheca fusiformis through genetic engineering technology and studied the aspect of biosilicification according to each domain. Chimeric protein showed the same activity of silica precipitation in vitro and got entrapped in the silica matrices during reaction process at ambient condition. We also studied protein immobilization efficiency by protein/silaffin chimeric proteins. The immobilization efficiency was
unexpectedly high and it is discovered that R1 silaffin domain showed excellent immobilization efficiency at broad range of pH condition indicating that it may be a new novel domain for protein immobilization by genetic engineering technology.