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Studiul cinetic al procesului de zaharificare a maltodextrinei, utilizand amiloglucozidaza imobilizata pe membrane prin legare covalenta
Date issued
2008
Author(s)
Garganciuc, Dana
Olteanu, Mihaela
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 α-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.
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 α-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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