Efficient synthesis of vitamin E intermediate by lipase-catalyzed regioselective transesterification

Trimethylhydroquinone-l-monoacetate (TMHQ-1-MA) is a valuable synthetic intermediate for vitamin E acetate. Immobilized Lipozyme RM IM from Mucor miehei was shown to be the best biocatalyst for the production of TMHQ-1-MA through regioselective transesterification between trimethylhydroquinone diacetate (TMHQ-DA) and alcohol. The effects of lipase-catalyzed reaction conditions including solvent, acyl receptor, substrate mole ratio, reaction temperature and agitation speed were investigated. The optimum conditions for Lipozyme RM IM catalyzed regioselective transesterification were achieved at a substrate mole ratio of 1:1, an agitation of 200 rpm at 50 degrees C in MTBE/n-hexane (3:7). Under the above conditions, Lipozyme RM IM exhibited high substrate tolerance (substrate concentrations of 1.06M). Recycling experiments demonstrated that Lipozyme RM IM was quite steady under the reaction conditions. The analysis of kinetic experiment showed that the enzymatic reaction obeys the Ping-Pang bi-bi mechanism with n-butanol inhibition. (C) 2014 Elsevier B.V. All rights reserved.