Abstract
Esterifications catalysed by immobilised lipase from Candida rugosa (CRL) in cyclohexane at constant water activity (aw = 0.76) were studied using 2-methyl substituted octa-, nona- or decanoic acids and n-alcohols of varying chain length as substrates. The importance of controlling the water activity and choosing the right alcohol for obtaining maximum enantioselectivity is demonstrated. The immobilised lipase was easily recovered without loss of activity and enantioselectivity.