Abstract
The newly isolated fungus Talaromyces thermophilus was found to exhibit an extracellular lipase activity depending on the growth conditions. A 39 kDa monomeric lipase (TTL) was purified from the culture supernatant using ammonium sulphate precipitation, gel filtration and anion exchange chromatography. TTL N-terminal amino acid sequence showed a high similarity with Thermomyces lanuginosa lipase, a well-known lipase with multiple applications. The specific activity of about 7300 ± 122 and 9868 ± 139 U mg −1 was obtained using tributyrin and olive oil emulsion as substrate, respectively, at pH 9.5 and 50 °C. TTL maximum specific activities were found to be 24,110 ± 390 U mg −1 on trioctanoin. TTL was found to be fairly stable and active on long chain triglycerides at pH 9.5. Interestingly, TTL was found to be resistant to interfacial denaturation since it did not require any detergent to show its maximum activity on pure triglycerides. These findings are particularly important for lipase applications, in particular when variable temperatures and high pH values can be encountered, as well as its ability to show high levels activity in the presence of various surfactants and compatibility with some commercial wash agents and bleach agents.
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