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Lipase, Enzymatically Active in a Monolayer
Gloger, T. M. Maksymiw, R. Erdmann, Helmut Nitsch, W.
Gloger, T. M.
Maksymiw, R.
Erdmann, Helmut
Nitsch, W.
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Issue Date
1991
Submitted date
2024-03-27
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Abstract
The present work is focussed on the interfacial behaviour and the enzymatic activity of Staphylococcus carnosus lipase monolayersat the water/air and water/tolueneinterface. Stable enzyme layers were established at the water/air interface by quantitative spreading according to Trurnit (1). Thus, a monolayer with a definite number of molecules is obtained, exclusively. Therefore the resulting pressure/area diagramscanbeinvestigated with regard to molecular data. A characteristic feature is the occuranceof a critical pressure 7, ~ 18 mN/m in the pressure/area diagrams. This critical pressure occurs in many protein pressure/area diagrams. In the caseoflipase, Tig is pHindependent and can be demonstrated to correspond to a closely packed monolayer of compact molecules. From the corresponding molecular area A. (= 5000 A2) the molecules can be postulated to be discs lying flat on the surface and the radius and thickness can be calculated to 40 Aand 20 A, respectively. The covering of the monolayer with a toluene-phase changes the intermolecular interactions: The pressure/area curve progresses beyondthe corresponding water/air curve. For pressureshigher than rm, and molecular areas smaller than A, the difference diminishes. The values of m,/A, at water/air and water/toluene were the same. Asfor the water/air interface thecritical pressure is pH-independent. For studying enzymatic activity at the water/air interface a novel apparatus is presented, which combines a filmbalance with a convection reactor. Thus, it is possible to study the enzymatic reaction of a definite monolayer in a defined hydrodynamical environment. The enzymatic monolayerturns out ta be active and its reaction resembles the corresponding homogeneous reaction. Thus support is given for the view,that enzymes are not necessarily denatured on their contact with an interface, but can keep a compact and active configuration.
Citation
Lipases : structure, mechanism and genetic engineering, 403 - 406
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Book chapter
conference paper
conference paper
Language
en
Description
Series/Report no.
GBF monographs ; Volume 16
ISSN
0930-4320
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ISBN
156081165X
3527283323
3527283323
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Attribution-NonCommercial-ShareAlike 4.0 International