Immobilization of Enzymes on Flexible Tubing Surfaces for Continuous Bioassays
Immobilized enzymes can be used to catalyze biochemical reactions in a batch process, however, it is more difficult to use them in a continuous process. Herein, we develop an enzyme immobilization technique for flexible tubing surfaces, which can be used to catalyze biochemical reactions in a contin...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 34(2018), 47 vom: 27. Nov., Seite 14226-14233 |
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| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2018
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Amines Caseins Dextrans Enzymes, Immobilized Silanes dextran dialdehyde 37317-99-0 Hydrogen Peroxide mehr... |
| Zusammenfassung: | Immobilized enzymes can be used to catalyze biochemical reactions in a batch process, however, it is more difficult to use them in a continuous process. Herein, we develop an enzyme immobilization technique for flexible tubing surfaces, which can be used to catalyze biochemical reactions in a continuous process. In this technique, the tubing is first treated with (3-aminopropyl)triethoxysilane at 50 °C and baked at 100 °C in vacuum to form a network of reactive amine functional group on the inner tubing surface. Subsequently, dextran polyaldehyde, a polymeric cross-linker, is used to immobilize crude protease extract and catalase for hydrolyzing casein and degrading H2O2, respectively, in a continuous process. The immobilized proteases are highly stable even after a long-term storage at 4 °C. After 12 weeks of storage, 90% of the original protease activity can be preserved. Meanwhile, the immobilized catalase is able to degrade 0.1% H2O2 solution flowing at 5 μL/min. The immobilization technique is potentially useful for bioassays and industrial wastewater treatments when continuous processes are preferred |
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| Beschreibung: | Date Completed 04.02.2019 Date Revised 15.02.2019 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/acs.langmuir.8b02991 |