An extracellular lipase LII from Mucor racemosus was purified by anion exchange and gel filtration chromatography using DEAE-Sepharose and Sephacryl S-200 columns, respectively. A molecular weight of 20 kDa was estimated for M. racemosus LII by Sephacryl S-200 column and SDS-PAGE. LII had an acidic pl at 4.8. V(max) and K(m) for LII were estimated to be 55.5 mu mol oleic acid/min/ml and 2% olive oil, respectively. The highest lipolytic activity was detected with linseed oil as the substrate. The optimal pH and temperature for LII was 5.0 and 40 degrees C, respectively. The enzyme was stable up to 70 degrees C. The lipase activity was strongly enhanced by Cu(2+). Al(3+) and Fe(3+), and slightly enhanced by Mg(2+), Ni(2+) and Mn(2+), whereas Ca(2+), Co(2+), K(+) and Hg(2+) showed no effect. Pb(2+) only caused a partial inhibition of the enzyme. The residual lipase activity in carbopol 934 base gel was 385% after storage at 4 degrees C for 420 days. The characteristic properties of M. racemsus lipase formulated in the carbopol 934 gel was utilized for topical treatment of cellulite, and the results were positive for reducing thigh circumference. (C) 2010 Elsevier Ltd. All rights reserved.