Effects of immobilization on the kinetics of enzyme-catalyzed reactions. I. Glucose oxidase in a recirculation reactor system
Glucose oxidase from Aspergillus niger was immobilized on nonporous glass beads by covalent bonding and its kinetics were studied in a packed-column recycle reactor. The optimum pH of the immobilized enzyme was the same as that of soluble enzyme; however, immobilized glucose oxidase showed a sharper...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
1976 |
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| Umfang: |
8 Ill. ; 3 Tab. 16 |
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| Reproduktion: |
Wiley InterScience Backfile Collection 1832-2000 |
|---|---|
| Übergeordnetes Werk: |
in: Biotechnology and Bioengineering - New York, NY [u.a.] : Wiley, 18(1976) vom: Mai, Seite 669-684 |
| Übergeordnetes Werk: |
volume:18 ; year:1976 ; month:05 ; pages:669-684 ; extent:16 |
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| 520 | |a Glucose oxidase from Aspergillus niger was immobilized on nonporous glass beads by covalent bonding and its kinetics were studied in a packed-column recycle reactor. The optimum pH of the immobilized enzyme was the same as that of soluble enzyme; however, immobilized glucose oxidase showed a sharper pH-activity profile than that of the soluble enzyme. The kinetic behavior of immobilized glucose oxidase at optimum pH and 25°C was similar to that of the soluble enzyme, but the immobilized material showed increased temperature sensitivity. Immobilized glucose oxidase showed no loss in activity on storage at 4°C for nearly ten weeks. On continuous use for 60 hr, the immobilized enzyme showed about a 40% loss in activity but no change in the kinetic constant. | ||
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(DE-627)NLEJ159610605 DE-627 ger DE-627 rakwb eng Effects of immobilization on the kinetics of enzyme-catalyzed reactions. I. Glucose oxidase in a recirculation reactor system 1976 8 Ill. 3 Tab. 16 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Glucose oxidase from Aspergillus niger was immobilized on nonporous glass beads by covalent bonding and its kinetics were studied in a packed-column recycle reactor. The optimum pH of the immobilized enzyme was the same as that of soluble enzyme; however, immobilized glucose oxidase showed a sharper pH-activity profile than that of the soluble enzyme. The kinetic behavior of immobilized glucose oxidase at optimum pH and 25°C was similar to that of the soluble enzyme, but the immobilized material showed increased temperature sensitivity. Immobilized glucose oxidase showed no loss in activity on storage at 4°C for nearly ten weeks. On continuous use for 60 hr, the immobilized enzyme showed about a 40% loss in activity but no change in the kinetic constant. Wiley InterScience Backfile Collection 1832-2000 Ramachandran, K. B. oth Perlmutter, D. D. oth in Biotechnology and Bioengineering New York, NY [u.a.] : Wiley 18(1976) vom: Mai, Seite 669-684 (DE-627)NLEJ159070678 (DE-600)1480809-2 0006-3592 nnns volume:18 year:1976 month:05 pages:669-684 extent:16 http://dx.doi.org/10.1002/bit.260180507 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 18 1976 5 669-684 16 |
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(DE-627)NLEJ159610605 DE-627 ger DE-627 rakwb eng Effects of immobilization on the kinetics of enzyme-catalyzed reactions. I. Glucose oxidase in a recirculation reactor system 1976 8 Ill. 3 Tab. 16 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Glucose oxidase from Aspergillus niger was immobilized on nonporous glass beads by covalent bonding and its kinetics were studied in a packed-column recycle reactor. The optimum pH of the immobilized enzyme was the same as that of soluble enzyme; however, immobilized glucose oxidase showed a sharper pH-activity profile than that of the soluble enzyme. The kinetic behavior of immobilized glucose oxidase at optimum pH and 25°C was similar to that of the soluble enzyme, but the immobilized material showed increased temperature sensitivity. Immobilized glucose oxidase showed no loss in activity on storage at 4°C for nearly ten weeks. On continuous use for 60 hr, the immobilized enzyme showed about a 40% loss in activity but no change in the kinetic constant. Wiley InterScience Backfile Collection 1832-2000 Ramachandran, K. B. oth Perlmutter, D. D. oth in Biotechnology and Bioengineering New York, NY [u.a.] : Wiley 18(1976) vom: Mai, Seite 669-684 (DE-627)NLEJ159070678 (DE-600)1480809-2 0006-3592 nnns volume:18 year:1976 month:05 pages:669-684 extent:16 http://dx.doi.org/10.1002/bit.260180507 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 18 1976 5 669-684 16 |
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(DE-627)NLEJ159610605 DE-627 ger DE-627 rakwb eng Effects of immobilization on the kinetics of enzyme-catalyzed reactions. I. Glucose oxidase in a recirculation reactor system 1976 8 Ill. 3 Tab. 16 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Glucose oxidase from Aspergillus niger was immobilized on nonporous glass beads by covalent bonding and its kinetics were studied in a packed-column recycle reactor. The optimum pH of the immobilized enzyme was the same as that of soluble enzyme; however, immobilized glucose oxidase showed a sharper pH-activity profile than that of the soluble enzyme. The kinetic behavior of immobilized glucose oxidase at optimum pH and 25°C was similar to that of the soluble enzyme, but the immobilized material showed increased temperature sensitivity. Immobilized glucose oxidase showed no loss in activity on storage at 4°C for nearly ten weeks. On continuous use for 60 hr, the immobilized enzyme showed about a 40% loss in activity but no change in the kinetic constant. Wiley InterScience Backfile Collection 1832-2000 Ramachandran, K. B. oth Perlmutter, D. D. oth in Biotechnology and Bioengineering New York, NY [u.a.] : Wiley 18(1976) vom: Mai, Seite 669-684 (DE-627)NLEJ159070678 (DE-600)1480809-2 0006-3592 nnns volume:18 year:1976 month:05 pages:669-684 extent:16 http://dx.doi.org/10.1002/bit.260180507 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 18 1976 5 669-684 16 |
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(DE-627)NLEJ159610605 DE-627 ger DE-627 rakwb eng Effects of immobilization on the kinetics of enzyme-catalyzed reactions. I. Glucose oxidase in a recirculation reactor system 1976 8 Ill. 3 Tab. 16 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Glucose oxidase from Aspergillus niger was immobilized on nonporous glass beads by covalent bonding and its kinetics were studied in a packed-column recycle reactor. The optimum pH of the immobilized enzyme was the same as that of soluble enzyme; however, immobilized glucose oxidase showed a sharper pH-activity profile than that of the soluble enzyme. The kinetic behavior of immobilized glucose oxidase at optimum pH and 25°C was similar to that of the soluble enzyme, but the immobilized material showed increased temperature sensitivity. Immobilized glucose oxidase showed no loss in activity on storage at 4°C for nearly ten weeks. On continuous use for 60 hr, the immobilized enzyme showed about a 40% loss in activity but no change in the kinetic constant. Wiley InterScience Backfile Collection 1832-2000 Ramachandran, K. B. oth Perlmutter, D. D. oth in Biotechnology and Bioengineering New York, NY [u.a.] : Wiley 18(1976) vom: Mai, Seite 669-684 (DE-627)NLEJ159070678 (DE-600)1480809-2 0006-3592 nnns volume:18 year:1976 month:05 pages:669-684 extent:16 http://dx.doi.org/10.1002/bit.260180507 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 18 1976 5 669-684 16 |
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(DE-627)NLEJ159610605 DE-627 ger DE-627 rakwb eng Effects of immobilization on the kinetics of enzyme-catalyzed reactions. I. Glucose oxidase in a recirculation reactor system 1976 8 Ill. 3 Tab. 16 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Glucose oxidase from Aspergillus niger was immobilized on nonporous glass beads by covalent bonding and its kinetics were studied in a packed-column recycle reactor. The optimum pH of the immobilized enzyme was the same as that of soluble enzyme; however, immobilized glucose oxidase showed a sharper pH-activity profile than that of the soluble enzyme. The kinetic behavior of immobilized glucose oxidase at optimum pH and 25°C was similar to that of the soluble enzyme, but the immobilized material showed increased temperature sensitivity. Immobilized glucose oxidase showed no loss in activity on storage at 4°C for nearly ten weeks. On continuous use for 60 hr, the immobilized enzyme showed about a 40% loss in activity but no change in the kinetic constant. Wiley InterScience Backfile Collection 1832-2000 Ramachandran, K. B. oth Perlmutter, D. D. oth in Biotechnology and Bioengineering New York, NY [u.a.] : Wiley 18(1976) vom: Mai, Seite 669-684 (DE-627)NLEJ159070678 (DE-600)1480809-2 0006-3592 nnns volume:18 year:1976 month:05 pages:669-684 extent:16 http://dx.doi.org/10.1002/bit.260180507 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 18 1976 5 669-684 16 |
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effects of immobilization on the kinetics of enzyme-catalyzed reactions. i. glucose oxidase in a recirculation reactor system |
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Effects of immobilization on the kinetics of enzyme-catalyzed reactions. I. Glucose oxidase in a recirculation reactor system |
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Glucose oxidase from Aspergillus niger was immobilized on nonporous glass beads by covalent bonding and its kinetics were studied in a packed-column recycle reactor. The optimum pH of the immobilized enzyme was the same as that of soluble enzyme; however, immobilized glucose oxidase showed a sharper pH-activity profile than that of the soluble enzyme. The kinetic behavior of immobilized glucose oxidase at optimum pH and 25°C was similar to that of the soluble enzyme, but the immobilized material showed increased temperature sensitivity. Immobilized glucose oxidase showed no loss in activity on storage at 4°C for nearly ten weeks. On continuous use for 60 hr, the immobilized enzyme showed about a 40% loss in activity but no change in the kinetic constant. |
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Glucose oxidase from Aspergillus niger was immobilized on nonporous glass beads by covalent bonding and its kinetics were studied in a packed-column recycle reactor. The optimum pH of the immobilized enzyme was the same as that of soluble enzyme; however, immobilized glucose oxidase showed a sharper pH-activity profile than that of the soluble enzyme. The kinetic behavior of immobilized glucose oxidase at optimum pH and 25°C was similar to that of the soluble enzyme, but the immobilized material showed increased temperature sensitivity. Immobilized glucose oxidase showed no loss in activity on storage at 4°C for nearly ten weeks. On continuous use for 60 hr, the immobilized enzyme showed about a 40% loss in activity but no change in the kinetic constant. |
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Glucose oxidase from Aspergillus niger was immobilized on nonporous glass beads by covalent bonding and its kinetics were studied in a packed-column recycle reactor. The optimum pH of the immobilized enzyme was the same as that of soluble enzyme; however, immobilized glucose oxidase showed a sharper pH-activity profile than that of the soluble enzyme. The kinetic behavior of immobilized glucose oxidase at optimum pH and 25°C was similar to that of the soluble enzyme, but the immobilized material showed increased temperature sensitivity. Immobilized glucose oxidase showed no loss in activity on storage at 4°C for nearly ten weeks. On continuous use for 60 hr, the immobilized enzyme showed about a 40% loss in activity but no change in the kinetic constant. |
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