Abstract
Two commercially available enzymes, Dextrozyme (α-amylase) and Esperase (protease), were covalently immobilized on non-woven electrospun poly(styrene-co-maleic anhydride) nanofiber mats with partial retention of their catalytic activity. Immobilization was achieved for the enzymes on their own as well as in different combinations with an additional enzyme, β-galactosidase, on the same non-woven nanofiber mat. This experiment yielded a universal method for immobilizing different combinations of enzymes with nanofibrous mats containing maleic anhydride (MAnh) residues in the polymer backbone.
Highlights
Enzymes play a key role in catalyzing biological reactions
Enzyme immobilization is often associated with a decrease in catalytic activity when compared to native enzymes in solution [26,28]
Similar results have been reported for co-immobilized cholesterol oxidase (COD) and horseradish peroxidase (HRP) [29]
Summary
Enzymes play a key role in catalyzing biological reactions. As a result, they are often active under relatively mild conditions and their catalysis can be highly specific. They are often active under relatively mild conditions and their catalysis can be highly specific Due to these characteristics, enzymes are increasingly being used in modern biotechnological settings, such as the food, biofuel and fine chemical industries [1]. Advances in recombinant enzyme technology have enabled the production of large quantities of robust enzymes, functionalized to meet industrial demands [5,6]. Enzymes may be immobilized by adsorption or covalent attachment to polymers and other high-surface-area substrates that find application in fine-chemical synthesis, fabrication of biosensors, food processing, protein digestion, and bioremediation [8]
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