Biochemical characterization of a thermoactive and thermostable lipase from a newly isolated Trichosporon coremiiforme strain

Abstract

Nonstop demand for greatly thermostable and thermoactive active lipase encourages the research for the new enzyme sources. In this study, a strain of Trichosporon coremiiforme was isolated from the traditional tannery in the city of Fez in Morocco, lipase production and their lipolytic activity was studied. Pure T. coremiiforme lipase (TCL) was obtained after ammonium sulfate fractionation, G-75 gel filtration and cation exchanger chromatography (Mono-S), having a molecular weight of 67 kDa. TCL presents a maximal activity at pH 8 and 50°C. After a 5 min treatment at 80°C, the enzyme maintained 50% of its activity, which is so far as is known. TCL previously characterized is found to be stable between pH 5 and 10 after 60 min incubation. TCL hydrolyses the long chains triacylglycerols more efficiently than the short ones. A specific activity of 1800 U/mg was measured on tributyrin or olive oil emulsion as substrate. This newly isolated lipase can be considered as a good candidature for industrial and biotechnological applications.