Abstract
The membranes with immobilized enzymes have a double role, as a separation barrier and a biocatalyst. The membranes immobilize the enzymes in insoluble state by direct binding (e.g. covalent binding) or in soluble state, by adsorption at the separation surface, depending on the polymer nature and the membrane structure. The researches purpose was to emphasize the biocatalytic activity of a membrane-immobilized enzyme system. This paper relates the original results from the kinetic study of maltodextrine saccharification process. The dextrines are obtained by enzymatic hydrolise of starch with a-amilase.The process took place into an enzymatic membrane bioreactor equipped with an active membrane from brominated polyphenileneoxide with 28% bromination degree, having amyloglucosidase covalently immobilized. In this bioreactor carries on the conversion of dextrines to maltose and glucose, under the biocatalytic action of amyloglucosidase.
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