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- W25463225 abstract "Publisher Summary This chapter discusses an experiment to study the altered kinetic behavior of immobilized glycosidases. In the experiment, partially-purified glycosidases from both the liver of the gastropod, Turbo cornutus, and the neonatal rat brain were immobilized by co-crosslinking with glutaraldehyde and an inert carrier protein. The preparation was allowed to polymerize in the form of a membranous sheet with a thickness of 80 nm. After immobilization, both α-galactosidase and β-N-acetyl-hexosaminidase from T. cornutus displayed two pH optima, one above and one below the pH optimum of the soluble enzyme. From the results of the experiment, it can be suggested that most of the alterations in the kinetic behavior of the immobilized enzymes can be ascribed to the properties of the immobilization matrix. By a judicious choice of these matrix properties, it should be possible to engineer the kinetic behavior of immobilized glycosidases in such a way that they will become more suitable for various possible medical and analytical applications." @default.
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- W25463225 date "1979-01-01" @default.
- W25463225 modified "2023-09-27" @default.
- W25463225 title "Altered Kinetic Behavior of Immobilized Glycosidases" @default.
- W25463225 doi "https://doi.org/10.1016/b978-0-12-301302-6.50071-3" @default.
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