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SummaryEnzymes can be sorbed on inorganic carriers followed by crosslinking with glutaraldehyde. I n some cases superior results are obtained when the support is precoated with a porous layer of titanium oxide. Immobilized lactase prepared in this way retains essentially all its activity when stored under water a t 23°C for long periods of time and loses activity only slowly while treating cheese whey a t 55°C over the course of several weeks contact time. Furthermore, catalyst activity is unaffected by frequent sanitization. Optimum p H for these immobilized-lactase catalysts (enzyme produced from A . niger) is about 3.0 and optimum temperature is about 60°C. Amyloglucosidase catalase, 1.-asparaginase, and trypsin have also been immobilized by these techniques.

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Cholinesterase has been bonded to Procion brilliant orange – DEAE-cellulose. The matrix-supported enzyme has a lower activity than the free enzyme in solution; thermal stability, however, is much greater. A marked difference in the Km (apparent) value of the derivatized protein was observed (substrate used was acetylcholine chloride, free Cholinesterase Km = 9.6 × 10−4 M, bound Cholinesterase Km = 1.0 × 10−2 M).