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Expanding the range of nature's catalysts for industrial applications
Date:1/30/2014

s properly only when folded into this shape, and typically retains its structure within a narrow range of conditions. If subjected to temperature, pH, or pressure outside these tolerances, the enzyme begins to denature, losing its shape and functionality.

Makhatadze seeks to boost the high-temperature tolerances for a given enzyme by adjusting the electrostatic interactions on the protein surface. In research culminating with the 2009 PNAS paper, Makhatadze developed a computer program allowing researchers to expand the temperature range at which a given enzyme would remain functional by altering the electrical charges on the protein surface.

"Many forces the packing of the core, hydrophobic interactions, hydrogen bonding, salt bridges, disulfide bridges are important for protein stability, and 40 years of research has gone into establishing the rules that govern this process," said Makhatadze. "Our contribution has been on the particular role of the interactions between the charges on the protein surface, and a recognition that they can be manipulated to modulate protein stability."

In the context of industrial processes like paper manufacturing, the expanded functional range could make an enzymatic approach more attractive and economically feasible. The next step, said Makhatadze, and the focus of the NSF grant, is to understand the speed at which proteins fold and unfold, in order to slow their deterioration, and further expand their functional range.

"We've learned to make changes in the stability of the protein. But every protein has a limit; there's nothing you can do to make a protein stable at 500 degrees, for example," said Makhatadze. "So can we somehow make it unfold more slowly by modulating the charge-charge interactions? If you can extend that process, it will function at a high temperature for a longer period of time, and that's beneficial."

Within CBIS, the $1.7 million commitment from the NSF is one o
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Contact: Mary Martialay
martim12@rpi.edu
Rensselaer Polytechnic Institute
Source:Eurekalert

Page: 1 2 3

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