期刊
COLLOIDS AND SURFACES B-BIOINTERFACES
卷 25, 期 2, 页码 119-128出版社
ELSEVIER
DOI: 10.1016/S0927-7765(01)00302-2
关键词
alkaline phosphatase; dimyristoyl phosphatidic acid; Langmuir monolayers; enzymatic catalysis; adsorption isotherm; non-ionic surfactant
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 mug 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. (C) 2002 Elsevier Science B.V. All rights reserved.
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