Characterization of immobilized enzyme systems
report
Recently methods have been developed to characterize immobilized enzyme systems. These methods have been discussed extensively in Progress in Industrial Microbiology [l] and consist in procedures to determine the effective diffusion coefficient and the intrinsic values for the maximum reaction rate V and the Michaelis-Menten constant K . In this article m m a short review will be given, followed by a description of the experi ments that have been conducted in order to test the methods. Spheres of gelatine and sodium alginate were prepared with and without the enzyme invertase, and subsequently a crosslinking with glutaraldehyde and CaCl^ respectively was performed. From the results of the experiments with sucrose as substrate it can be concluded that the effective diffusion is, within limits, proportional to the radius of the spheres and is about a factor two to three slower than it is in pure water. Experiments concerning the kinetic parameters learn that immobilization of invertase in alginate spheres hardly effects the enzyme, but that immobi lization in gelatine causes a 85% loss in activity due to the destroying crosslinking with glutaraldehyde.
Topics
TNO Identifier
250288
Publisher
TNO
Collation
23 p.
Place of publication
Apeldoorn