THE PREPARATION OF HOMOCHIRAL DRUGS AND PEPTIDES USING CROSS-LINKED ENZYME CRYSTALS

Cross-linked enzyme crystal (''CLEC(TM)'') technology combines the exquisite selectivity (enantio-, diastereo-, chemo-, and regioselectivity) of enzymes, with the stability and predictability of a crystalline catalyst particle. The enantioselectivity of the Candida rugosa lipase (CRL) CLEC, being derived from a single, crystalline hydrolase is 2 to 50 times higher than that of the commercial CRL mixture of hydrolases in the resolution of a-substituted carboxylic acids. The stability (thermal and organic solvent) of Thermolysin protease CLEC and CRL CLEC is increased two to three orders of magnitude over that of the monomeric proteins. The CLEC particles are stable and recoverable, so they cart be used for multiple reaction cycles with minimal loss of activity. The combination of selectivity and stability in a rugged catalyst form offers a complete solution to the problem of biocatalyst commercialization.