Significance of membrane bioreactor design on the biocatalytic performance of glucose oxidase and catalase: Free vs. immobilized enzyme systems
[Display omitted] •Xylose-glucose separation is improved by converting glucose into gluconic acid.•Oxygen required for glucose oxidase catalysis is provided by catalase catalysis.•Biocatalytic productivity of coupled reactions is dependent on oxygen availability.•Free enzyme system is compared to th...
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Published in | Biochemical engineering journal Vol. 117; pp. 41 - 47 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
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Elsevier B.V
15.01.2017
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Abstract | [Display omitted]
•Xylose-glucose separation is improved by converting glucose into gluconic acid.•Oxygen required for glucose oxidase catalysis is provided by catalase catalysis.•Biocatalytic productivity of coupled reactions is dependent on oxygen availability.•Free enzyme system is compared to three enzyme immobilization systems.•Fouling-induced enzyme immobilization enables high enzyme loadings.
Membrane separation of xylose and glucose can be accomplished via oxidation of glucose to gluconic acid by enzymatic glucose oxidase catalysis. Oxygen for this reaction can be supplied via decomposition of hydrogen peroxide by enzymatic catalase catalysis. In order to maximize the biocatalytic productivity of glucose oxidase and catalase (gluconic acid yield per total amount of enzyme) the following system set-ups were compared: immobilization of glucose oxidase alone; co-immobilization of glucose oxidase and catalase; glucose oxidase and catalase free in the membrane bioreactor. Fouling-induced enzyme immobilization in the porous support of an ultrafiltration membrane was used as strategy for entrapment of glucose oxidase and catalase. The biocatalytic productivity of the membrane reactor was found to be highly related to the oxygen availability, which in turn depended on the reactor configuration, hydrogen peroxide concentration and catalase origin. When glucose oxidase and catalase (from Aspergillus niger) were free in the membrane bioreactor a total biocatalytic productivity of 122mg gluconic acid/mg enzyme was obtained after five consecutive reaction cycles. The free enzymes showed superior performance compared to the immobilized systems as a result of limited substrate and product diffusion in the latter case. |
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AbstractList | [Display omitted]
•Xylose-glucose separation is improved by converting glucose into gluconic acid.•Oxygen required for glucose oxidase catalysis is provided by catalase catalysis.•Biocatalytic productivity of coupled reactions is dependent on oxygen availability.•Free enzyme system is compared to three enzyme immobilization systems.•Fouling-induced enzyme immobilization enables high enzyme loadings.
Membrane separation of xylose and glucose can be accomplished via oxidation of glucose to gluconic acid by enzymatic glucose oxidase catalysis. Oxygen for this reaction can be supplied via decomposition of hydrogen peroxide by enzymatic catalase catalysis. In order to maximize the biocatalytic productivity of glucose oxidase and catalase (gluconic acid yield per total amount of enzyme) the following system set-ups were compared: immobilization of glucose oxidase alone; co-immobilization of glucose oxidase and catalase; glucose oxidase and catalase free in the membrane bioreactor. Fouling-induced enzyme immobilization in the porous support of an ultrafiltration membrane was used as strategy for entrapment of glucose oxidase and catalase. The biocatalytic productivity of the membrane reactor was found to be highly related to the oxygen availability, which in turn depended on the reactor configuration, hydrogen peroxide concentration and catalase origin. When glucose oxidase and catalase (from Aspergillus niger) were free in the membrane bioreactor a total biocatalytic productivity of 122mg gluconic acid/mg enzyme was obtained after five consecutive reaction cycles. The free enzymes showed superior performance compared to the immobilized systems as a result of limited substrate and product diffusion in the latter case. |
Author | Meyer, Anne S. Morthensen, Sofie T. Pinelo, Manuel Jørgensen, Henning |
Author_xml | – sequence: 1 givenname: Sofie T. surname: Morthensen fullname: Morthensen, Sofie T. email: soth@kt.dtu.dk – sequence: 2 givenname: Anne S. surname: Meyer fullname: Meyer, Anne S. email: am@kt.dtu.dk – sequence: 3 givenname: Henning orcidid: 0000-0003-1220-6893 surname: Jørgensen fullname: Jørgensen, Henning email: hejr@kt.dtu.dk – sequence: 4 givenname: Manuel surname: Pinelo fullname: Pinelo, Manuel email: mp@kt.dtu.dk |
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Keywords | Polydopamine Glucose oxidase Catalase Biocatalytic productivity Fouling-induced enzyme immobilization |
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•Xylose-glucose separation is improved by converting glucose into gluconic acid.•Oxygen required for glucose oxidase catalysis is provided by... |
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SubjectTerms | Biocatalytic productivity Catalase Fouling-induced enzyme immobilization Glucose oxidase Polydopamine |
Title | Significance of membrane bioreactor design on the biocatalytic performance of glucose oxidase and catalase: Free vs. immobilized enzyme systems |
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