Two different immobilisation techniques for lipases were investigated: adsorption on to Accurel EP-100 and deposition on to Celite. The specific activities were in the same order of magnitude, 2.9 (mu mol min(-1) mg protein) when Celite was used as support and 2.3 (mu mol min(-1) mg(-1) protein) when Accurel EP-100 was used as support, even if the amount of lipase loaded differed by 2 orders of magnitude. Immobilisation on Accurel EP-100 was the preferred technique since 40-100 times more protein can be loaded/per g carrier, thus yielding a more active catalyst. The water activity profiles in lipase catalysed esterification were influenced by the amount of protein adsorbed to Accurel EP-100. Higher protein loading (40 mg g(-1)) resulted in a bell- shaped water activity profile with highest specific activity (6.1 mu mol min(-1) mg(-1) protein) at a(w)=0.11, while an enzyme preparation with low protein loading (4 mg g(-1)) showed highest specific activity at a(w)=0.75.