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A mutant L206F/P207F/L259F of  Talaromyces thermophilus  lipase (TTL) exhibited high hydrolytic activity towards 2-carboxyethyl-3-cyano-5-methylhexanoic acid ethyl ester (CNDE) for synthesis of ( S )-2-carboxyethyl-3-cyano-5-methylhexanoic acid ( S -CCMA), a key chiral intermediate of pregabalin. However, low conversion at high CNDE concentration and unreusability of the free TTL mutant restricted its industrial applications. In this study, the TTL mutant was immobilized onto epoxy resin and its catalytic properties for kinetic resolution of CNDE were investigated. Under the optimized conditions, the immobilized lipase exhibited an increased catalytic efficiency even at a CNDE concentration of 3 M with 49.7% conversion and 95%  ee  p . The conversion retained higher than 46.3% even after 10 times repeated use of the immobilized lipase in  n -heptane-water biphasic system. These results demonstrated great potential of the immobilized TTL mutant for industrial production of the chiral intermediate of pregabalin.

Efficient Biocatalytic Synthesis of Chiral Intermediate of Pregabalin Using Immobilized Talaromyces thermophilus Lipase