Lipase-catalysed stereoselective esterifications using gelatin-based hydrogels

A hydrogel stable in an organic solvent has been developed. This pseudo-solid aqueous gel (PAG) consists of only native gelatin and water, and has been used for immobilization of enzymes. A relatively high amount of gelatin is required in order to obtain stable gels. PAGs containing the enzyme Candida antarctica lipase (SP 525) were successfully used in catalysing the esterification of R/S-(±)-2-octanol and hexanoic acid in hexane. The conversions as well as the enantiomeric excess values of the product, R-(−)-2-octyl hexanoate, were high and comparable to those obtained with microemulsion-based gels. The PAGs containing immobilized lipase gave reproducible results and may be re-used several times. The gels are easy to prepare and use, non-toxic and biocompatible. The PAGs retain their integrity in organic solvents and may be used in preparative-scale synthesis of organic compounds.