The thioesterase activity of palmitoyl protein thioesterase (PPT1) and six commercial lipases was measured against the synthetic substrates, S-palmitoyl-N-acetylcysteamine (Ac-Cym-Pal) and S-(18-.methyleicosanoyl)-N-acetylcysteamine (Ac-Cym-18-MEA). PPTI showedgood activity against Ac-Cym-Pal but relatively low activity against the longer chain substrate, Ac-Cym-18-MEA. The highest activity was given by Lipolase 100L type EX (Novozyme) and Lipoprotein Lipase (Sigma) with greater than 90% hydrolysis of Ac-Cym-18-MEA within 10 min at pH 7.4. Other lipases to show high levels of thioesterase activity include Lipex 100L (Novozyme), Lipomod 34P (Biocatalysts) and Lipozyme CALB L (Novozyme). Chemical analysis of wool fibre and fabric treated with the above enzymes under optimal conditions showed that there was no hydrolysis of 18-MEA or other covalently bound fatty acids from the fibre surface. No change in the wettability of the fabric surface was observed following enzyme treatments. Scanning electron micrographs of the fabric treated with the most active enzyme, Lipolase 100L type EX, revealed that the surface of the fibres appeared to have a coating that was not removed by extensive extraction. Reasons for the inability of PPTI and the other esterases to hydrolyse 18-MEA from the wool fibre surface are discussed. (c) 2007 Elsevier Inc. All rights reserved.