Acidification and aggregation in biohydrogen production

• Publisher: John Wiley and Sons
• Year: 2007
• Tongue: English
• Weight: 61 KB
• Volume: 96
• Category: Article
• ISSN: 0006-3592
• DOI: 10.1002/bit.21402

✦ Synopsis

Targeting functional proteins to specific sites on a silicon device is required for the development of new biosensors. So far addition of nine arginine residues (poly-Arg) to a protein has been proposed for direct adsorption of a fusion protein on a silica surface with retention of enzymatic activity. However, poly-Arg tagged protein is released from the silica surface after a long incubation. Kuroda and co-workers have found a protein that binds tightly to silicon particles, which have surfaces that are oxidized to silica. The silica-binding protein bound more tightly than a poly-Arg tag to the silica surface and after its fusion with green-fluorescent protein (GFP) was retained on the surface even after a 24 h incubation. Therefore, this silica binding protein-which the authors tentatively designate ''Si-tag''-can be used for one step targeting of proteins to silica surfaces. This technology would contribute to silicon-based biosensors and protein array technologies.