Two enzymes were purified from P. cyclopium in a 1980 study:a triacylglycerol lipase (Lipase I) and a partial glyceride hydrolase (Lipase II) Lipase II was purified in 2000, and the enzyme was found to exist in several glycosylated forms with MW 40–43 kDa. In order to enhance the production of the enzyme, Vanot et al.used response surface methodology (RSM) to optimize the conditions for production of partial acylglycerol lipase by P. cyclopium,but the lipolytic activity only ranging from 2 to 6 lipase units per mL medium . We have achieved heterologous expression of P.cyclopium MDL (now renamed as Lipase GH1) in Pichia pastorisstrain GS115 and it had higher enzyme activity .