Optimizing immobilized enzyme performance in cell-free environments to produce liquid fuels.
The overall goal of this project was to optimize enzyme performance for the production of bio-diesel fuel. Enzyme immobilization has attracted much attention as a means to increase productivity. Mesorporous silica materials have been known to be best suited for immobilizing enzymes. A major challenge is to ensure that the enzymatic activity is retained after immobilization. Two major factors which drive enzymatic deactivation are protein-surface and inter-protein interactions. Previously, we studied protein stability inside pores and how to optimize protein-surface interactions to minimize protein denaturation. In this work we studied eh effect of surface curvature and chemistry on inter-protein interactions. Our goal was to find suitable immobilization supports which minimize these inter-protein interactions. Our studies carried out in the frame work of Hydrophobic-Polar (HP) model showed that enzymes immobilized inside hydrophobic pores of optimal sizes are best suited to minimize these inter-protein interactions. Besides, this study is also of biological importance to understand the role of chaperonins in protein disaggregation. Both of these aspects profited immensely with collaborations with our experimental colleague, Prof. Georges Belfort (RPI), who performed the experimental analog of our theoretical works.
- Research Organization:
- Columbia Univ., New York, NY (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC)
- DOE Contract Number:
- SC0007019
- OSTI ID:
- 1177494
- Report Number(s):
- GG006023
- Country of Publication:
- United States
- Language:
- English
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