Engineering and molecular characterization of proteins and enzyme biocatalysts
The main goal of our research is to successfully modify enzyme biocatalysts aimed at environmental and pharmaceutical applications, with a broader interest focused on understanding the role between structure, function and flexibility in various enzymatic systems. Our research strategy combines directed evolution and semi-random mutagenesis experiments coupled with biochemical and biophysical characterization such as nuclear magnetic resonance (NMR), molecular biology, enzyme kinetics, and molecular modeling. Using this combined approach, we specifically focus on achieving the following aims:
1) To understand how the amino acid sequence and local structural environment of conserved residues determine the motional and functional properties of enzymes
2) To investigate how functionally and structurally related enzymes retain their motional properties within similar folds;
3) To modify, reproduce and apply this 'structure-function' and 'flexibility-function' information to the design of new and improved molecular biocatalysts.
We have taken part in numerous university/private-sector partnerships, and develop new technologies aimed at using enzymes for green chemistry and industrial biocatalysis purposes. Our infrastructure allows us to modify, improve, produce and characterize enzymes with high industrial potential.
- Molecular biology
- Enzyme expression
- Purification
- Characterization
- Agriculture, animal science and food
- Chemical industries
- Environmental technologies and related services
- Forestry and forest-based industries
- Life sciences, pharmaceuticals and medical equipment
- Manufacturing and processing
Specialized labs and equipment
Equipment |
Function |
---|---|
Isothermal titration calorimeter (ITC) |
Calculation of protein-protein and protein-ligand interactions |
Circular diochrism (CD) spectropolarimeter |
Estimation of protein structure and denaturing parameters |
UV-visible spectrophotometer |
Enzyme kinetics |
Fluorimeter |
Enzyme kinetics |
NanoDrop spectrophotometer |
Microvolume assaying and kinetics |
Electroporator |
Transformation of bacterial DNA |
Refrigerated shaking incubator |
Bacterial culture |
Shaking incubator |
Bacterial culture |
Sonicator |
Bacterial cell lysis |
Tabletop refrigerated centrifuge |
Centrifuging |
Refrigerated microcentrifuge |
Centrifuging |
Avanti centrifuge |
Centrifuging |
Stirred-cell concentrators |
Volume concentration |
Thermocycler |
DNA polymerase chain reaction (PCR) amplification |
-80°C refrigerator |
Conservation of bacterial cultures |
pH meters |
pH measuring |
FPLC/HPLC |
Fast protein liquid chromatography, high-performance liquid chromatography, compound separation, protein purification |
Microplate reader |
High-speed spectrophotometry and fluorometry |
Analytical balances |
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Additional information
Title |
URL |
---|---|
Isolation and characterization of EstC, a new cold-active esterase from Streptomyces coelicolor A3(2) |
|
Conservation of flexible residue clusters among structural and functional enzyme homologues |
|
Nuclear Magnetic Resonance Spectroscopy Laboratory | https://inrs.ca/en/research/research-facilities/find-a-research-facilitie/nuclear-magnetic-resonanc…; |
Nicolas Doucet |