We explore unique extreme environments to identify novel microbial strains. Using advanced genomic tools, we perform 'gene mining' to discover potential protein sequences that offer superior stability or unique catalytic properties.
Once a target gene is identified, we employ recombinant DNA technology to clone and express these proteins in host systems. Our goal is to achieve high-yield production of pure, functional proteins for further analysis.
Using various chromatography techniques, we isolate proteins to high purity. We then conduct rigorous biochemical characterization to determine their optimal pH & temperature, stability, kinetic parameters, and substrate specificity.
To push the limits of nature, we use site-directed mutagenesis and directed evolution to enhance protein performance. This includes increasing thermal resistance, improving catalytic efficiency, or tailoring enzymes for specific industrial applications.
For industrial viability, enzymes must be reusable. We research various matrices and methods for enzyme immobilization to increase their longevity, stability, and ease of recovery during large-scale bioprocesses.
We bridge the lab-to-market gap by optimizing production parameters using fermenters. Our research focuses on maximizing protein yield through precisely controlled growth environments and feeding strategies.
In collaboration with leading institutions, we delve into the 3D architecture of proteins. By utilizing techniques such as Single Particle Analysis (Cryo-EM), we visualize protein structures at near-atomic resolution to understand the fundamental relationship between a protein’s shape and its extraordinary function.