This technology is available from Temarex Corporation.




Inventor(s): R. Viola, A. Saribas, M. Jayasekera

Disclosure 310 U.S. Patent not yet issued

This invention relates to truncated derivatives of aspartase having enhanced catalytic activity and/or enhanced clot dissolution properties relative to aspartase obtained from Escherichia coli (E. coli). The derivatized enzymes are created by site-directed mutagenesis of the gene encoding for aspartase.

This innovation addresses industry's need for an enhanced aspartase that is more efficient in the industrial production of L-aspartic acid (i.e. faster and/or cheaper) than the existing native enzyme that is currently in use. Laboratory experiments have shown these new enzyme derivatives to have greater than 200% increase in its catalytic properties under a defined set of conditions. Additionally, the novel enzymes of the present invention are similar in structure to the native aspartase enzyme of E. coli and maintain the extremely high selectivity and specificity of the native enzyme.

Potential uses include:

Tissue plasminogen activator (tPA) such as Activase (R) and/or other thrombolytic (clot-dissolving) agents are used clinically to activate plasminogen to help dissolve blood clots. According to the American Heart Association, thrombolytic agents reduce the amount of damage to the heart muscle - and reduce the number of heart attack deaths. Preliminary studies show that these derivatized enzymes improve the ability of tPA to dissolve blood clots.

L-aspartic acid is used in the pharmaceutical industry to treat certain ion deficiencies, in the food industry as a component of the artificial sweetener aspartame, a high-intensity sweetener (HIS), such as NutraSweet (R), in the consumer/industrial industry to produce polyaspartase for use in detergents and in the agricultural industry for the enhancement of nutrient absorption. Another application includes biodegradable chelating agents.