Commercial lipase immobilization on Accurel MP 1004 porous polypropylene |
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Authors: | Andrea Salis Enrico Sanjust Vincenzo Solinas Maura Monduzzi |
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Affiliation: | 1. Dipartimento di Scienze Chimiche, CSGI, S.S. 554 Bivio Sestu, 09042, Monserrato – Cagliari, Italyasalis@unica.it;3. Dipartimento di Scienze e Tecnologie Biomediche –, Università di Cagliari, Cittadella MonserratoUniversità di Cagliari, Cittadella Monserrato, S.S. 554 Bivio Sestu, 09042, Monserrato – Cagliari, Italy;4. Dipartimento di Scienze Chimiche, CSGI, S.S. 554 Bivio Sestu, 09042, Monserrato – Cagliari, Italy |
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Abstract: | Three commercial lipases (CLs), A Amano 6 (from Aspergillus niger), 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. |
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Keywords: | commercial lipases immobilization adsorption porous polypropylene support enzymatic activity |
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