Filtration System Purifies Proteins Having Close Molecular Weights

Oct 06, 2004

Kamalesh K. Sirkar, PhD

Chemical engineers at the New Jersey Institute of Technology (NJIT), Newark, say they’ve developed an advanced ultrafiltration system that enables separation and purification of two different kinds of proteins having a molecular weight ratio of just 1.03. Until now, proteins had to differ by five to six times in their molecular weight to allow them to be separated by traditional ultrafiltration.


“We know the process will work with a mixture of two proteins. We think it can be used (if the mixtures contain three or four proteins), but we don’t know,” says Kamalesh K. Sirkar, PhD, professor of chemical engineering and the project’s lead researcher, and co-author of a report in Biotechnology and Bioengineering.

The key to the new system is a different composite membrane that allows a one-stage purification process.

“We believe that pharmaceutical companies will immediately be able to put our research to work. Purification of protein is important to its end use.”

NJIT has funded this research to date, but Sirkar hopes to get outside funding to continue the work. Further research will address questions like: can the system be used on viruses or endotoxins (the outer coating of a particular type of bacteria)?  Will the process work with non-biological macromolecules such as dextran?

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