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    Enzymatic activity of alkaline phosphatase adsorbed on dimyristoylphosphatidic acid Langmuir-Blodgett films

    Year: 2002

    Journal: Colloids and Surfaces B: Biointerfaces 25 (2002) 119-128, 20111221

    Authors: Luciano Caseli, Maria Elisabete Darbello Zaniquelli, Rosa Prazeres Melo Furriel, Francisco Assis Leone

    Organizations: Departamento de Quimica, Faculdade de Filosofia, Universidade de Sao Paulo, Ciancias e Letras de Ribeirao Preto, 14040- 901 Ribeirao Preto, SP, Brazil

    The kinetics and the adsorption isotherms of the surfactant-solubilized alkaline phosphatase from rat osseous plate adsorbed by dip-coating on dimyristoyl phosphatidic acid (DMPA) Langmuir-Blodgett (LB) films were studied. The phosphomonohydrolase activity of the enzyme on the LB film was estimated by the hydrolysis of p- nitrophenylphosphate (PNPP). Films prepared from solutions containing 0.30  µg ml-1 of protein showed maximum activity for the supported enzyme above the critical micellar concentration of the non-ionic surfactant (polyoxyethylene-9-lauryl ether) used for enzyme solubilization. The surface density of the enzyme on DMPA LB films was determined from quartz crystal microbalance measurements. A consistent explanation concerning the maximum enzymatic activity is supported by data of surface tension for the mixed non-ionic surfactant-enzyme system.