Abstract
The enzyme amyloglucosidase was immobilized on oxidized DIOL silica and used to separate enantiomers of amino alcohols. The influence of pore size on enantioselectivity was studied and an optimum in the separation factors was found using 500 A DIOL silica as the starting material. About twice the amount of the protein could be immobilized on the 500 A DIOL silica material as on the 300 and 1000 A materials. The immobilization procedure was easy to reproduce and no significant difference in the chromatographic behavior was observed between two amyloglucosidase columns produced in-house. The effect of solute structure on enantioselective retention was studied using a set of 10 closely related amino alcohols. High separation factors (α>2) were obtained and the efficiency of the amyloglucosidase columns was greater than 25 000 plates/m based on the last eluted enantiomer.
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