A lipase-based platform technology that can be used in the production of fine chemicals, detergents, and pharmaceuticals.
- Enhanced thermostability, activity, and enantioselectivity of enantiopure compounds including bulky substrates.
- Can be used at a concentration 100x less than that of other enzymes.
Lipases are a group of specialized enzymes that are also important biocatalysts for the chiral synthesis of the active ingredients of pharmaceuticals and specialty chemicals. Among the most commonly used biocatalysts is lipase B from Candida Antarctica (CALB). The broad substrate specificity of CALB accompanied by its ability to function in both aqueous and organic reactions make it a versatile tool for the kinetic resolution and polymerization of esters.
Emory University researchers have generated a library of CALB variants that can be used to optimize the enantioselective esterification of select laboratory and commercial compounds including ibuprofen. By creating circular permutants of CALB, Dr. Lutz and colleagues have generated a library of lipases with catalytic activity superior to wild type CALB. Importantly, the inherent enantioselectivity of CALB is not disrupted. Therefore, these novel CALB variants can be used to maximize the efficiency of a wide range of enzymatic reactions including the production of fine chemicals, detergents and pharmaceuticals.
- Enzyme variants have been characterized and optimal ones have been selected.
- Proof of principle has been established using select CALB variants.