Human placental alkaline phosphatase covalently immobilized on a cross-flow microfiltration polyvinylidene difluoride membrane. Part I. Physicochemical effectors
M.G. Roig , J.F. Bello , S. Rodriguez , J.M. Cachaza , J.F. Kennedy
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引用次数: 2
Abstract
Human placental alkaline phosphatase has been chemically immobilized on a hydrophilic cross-flow microfiltration membrane made of polyvinylidene difluoride (PVDF) chemically labelled with 1-carbonylimidazole groups. Physicochemical characterization of this immobilized biocatalyst focused especially on attributes such as the immobilization isotherms (Langmuir type) of the enzyme to the support, the stability of the catalytic activity, the effects of pH and temperature on this activity and the existence of limitations of external diffusion for H+, substrate and/or products. Regarding enzyme stability and its dependence on different experimental conditions, patterns of hysteresis or memory are proposed.
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