April 17, 2012

ORNL process improves catalytic rate of enzymes by 3,000 percent




The researchers introduced a light-activated molecular switch across two regions of the enzyme Candida antarctica lipase B, or CALB - which breaks down fat molecules -- identified through modeling performed on DOE's Jaguar supercomputer.

The Journal of Physical Chemistry Letters - Engineering a Hyper-catalytic Enzyme by Photoactivated Conformation Modulation

Enzyme engineering for improved catalysis has wide implications. We describe a novel chemical modification of Candida antarctica lipase B that allows modulation of the enzyme conformation to promote catalysis. Computational modeling was used to identify dynamical enzyme regions that impact the catalytic mechanism. Surface loop regions located distal to active site but showing dynamical coupling to the reaction were connected by a chemical bridge between Lys136 and Pro192, containing a derivative of azobenzene. The conformational modulation of the enzyme was achieved using two sources of light that alternated the azobenzene moiety in cis and trans conformations. Computational model predicted that mechanical energy from the conformational fluctuations facilitate the reaction in the active-site. The results were consistent with predictions as the activity of the engineered enzyme was found to be enhanced with photoactivation. Preliminary estimations indicate that the engineered enzyme achieved 8–52 fold better catalytic activity than the unmodulated enzyme.




Agarwal noted that enzymes are present in every organism and are widely used in industry as catalysts in the production of biofuels and countless other every day products. Researchers believe this finding could have immense potential for improving enzyme efficiency, especially as it relates to biofuels.


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