Immobilization of glucoamylase from Aspergillus niger on poly(ethylenimine)-coated non-porous glass beads |
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Authors: | Bruce P Wasserman Daniel Burke Bruce S Jacobson |
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Institution: | Department of Biochemistry, University of Massachusetts, Amherst MA 01003, USA |
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Abstract: | Glucoamylase (1,4-α-d-glucan glucohydrolase, EC 3.2.1.3) from A. niger was immobilized on cationic nonporous glass beads (13–44 μm) by electrostatic adsorption followed by rosslinking with glutaraldehyde. Over 80% of the enzyme's total soluble activity was expressed upon immobilization. d-Glucose production from maltodextrins was virtually complete, suggesting that the lack of pores can eliminate the problem of product reversion. Immobilized glucoamylase showed decreased stability upon heating, compared with the soluble enzyme. |
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Keywords: | Thermal stability immobilization EC 3 2 1 3 Aspergillus niger non-porous glass poly(ethylenimine) |
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