Commercial lipase immobilization on Accurel MP 1004 porous polypropylene

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Abstract
Three commercial lipases (CLs), A Amano 6 (from Aspergillus;tiger), M Amano 10 (from Mucor javanicus), and R Amano (from Penicillium roqueforti) - called lipase A, M and R, respectively - were characterized in terms of carbohydrate content, protein content and enzymatic activity (p-nitrophenylacetate assay). All the CL preparations contained different proteins as observed from electrophoresis. Lipases were immobilized on Accurel MP1004 porous polypropylene by physical adsorption. The immobilization process caused a loss of enzymatic activity. The retained activity was similar for lipase M and R (about 15%). In contrast, lipase A retained only the 1.3% of the specific activity of the free lipase. The retained activity of lipases M and R seems to be due to a feature of the support, while the lower activity a of lipase A may be attributed to a strong structure distortion caused by lipase-support interaction