Trisaccharides, enzyme stabilization

Figure 3. Alcohol oxidase stabilization by mono-, di-, and trisaccharides. Sugars were added to the enzyme at concentrations of 1—10% immediately prior to drying. The solutions were dried in shallow dishes at 30 C under a vacuum and then harvested, ground to a powder, and stored in vials at 37 C. Enzyme activity was assayed with methanol as a substrate using an oxygen electrode and colorimetric assay.

Other examples of enzyme immobilization have also been reported. For example, the recombinant human al,3/l,4-fucosyltransferase were immobilized on Ni -agarose through a 6His tag and exhibited a remarkable stability. It was exploited in the synthesis of Le and Le trisaccharides (184). 

The immobilized enzyme was used for repeated synthesis of the above sialylated trisaccharides without adding detergent to the system, which was used in previous synthesis with the soluble enzyme (42), The use of detergent complicates isolation of the products. The stability of the enzyme preparation was good and no decrease of activity was observed on repeated preparative synthesis. Recently, immobilization to CNBr-activated agarose of the a2-6sialyltransferase was reported (50),... 

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