Georges Belfort

Georges Belfort
Institute Professor
Contact Information
Office: CBIS 2151
Phone: 518-276-6948
Ph.D. Chemical Engineering, University of California at Irvine, 1972
M.S. Chemical Engineering, University of California at Irvine, 1969
B.S. Chemical Engineering, University of Cape Town, South Africa, 1963
Dr. Georges Belfort: Endowed chair Russell Sage Professor of Chemical and Biological Engineering at RPI. He received his BS degree in CHME at the University of Cape Town and PhD in Engineering from UC Irvine. He has broad research interests include mass transfer and membrane filtration, protein misfolding and kinetics, single molecule force spectroscopy, and bioseparations. He has received the two major awards in the US on Separations (ACS (1995) and AIChE (2000)), the ACS Murphree Award in Industrial and Engineering Chemistry (2008), and is one of the "100 Chemical Engineers of the Modern Era" as part of the AIChE Centennial Celebration in 2008. He was elected a member of the US National Academy of Engineering, February 2003.
Research Interests
Membrane separation processes, Transport phenomena, Interfacial phenomena and rheology, Bioseparations and sensors, Protein misfolding and aggregation, Intein technology
Current Research
We have (i) developed an inexpensive, fast, reproducible and scalable high throughput synthesis and testing method for selecting the optimal surfaces against fouling from 100s of surfaces (e.g. membranes) in weeks rather than years, (ii) used magnetic resonance imaging to verify the existence of self cleaning Dean vortices (secondary flow) during filtration of colloidal feeds in curved channel flow, (iii) measured the rheological properties (shear viscosity and modulus) of adsorbed films (brushes, gels etc.) for layer upon layer deposition of polyelectrolytes and sensor development, (iv) fractionated and determined the effects of additives (e.g. osmolytes) on amyloid fibril nucleation kinetics, and (v) applied a biological switch (intein cleavage and splicing) for bioseparations of proteins in one step, for sensor development and fundamental insight into its mechanism.