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231225s2018 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.8b02991
|2 doi
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|a pubmed24n0967.xml
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|a (DE-627)NLM290173914
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|a (NLM)30383968
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Jannat, Mahbuba
|e verfasserin
|4 aut
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|a Immobilization of Enzymes on Flexible Tubing Surfaces for Continuous Bioassays
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|c 2018
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|2 rdamedia
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|a ƒa Online-Ressource
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|a Date Completed 04.02.2019
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|a Date Revised 15.02.2019
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a 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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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Amines
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|a Caseins
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|a Dextrans
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|a Enzymes, Immobilized
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|a Silanes
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|a dextran dialdehyde
|2 NLM
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|a 37317-99-0
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|a Hydrogen Peroxide
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|a BBX060AN9V
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|a Catalase
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|a EC 1.11.1.6
|2 NLM
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|a Yang, Kun-Lin
|e verfasserin
|4 aut
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 34(2018), 47 vom: 27. Nov., Seite 14226-14233
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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|g volume:34
|g year:2018
|g number:47
|g day:27
|g month:11
|g pages:14226-14233
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|u http://dx.doi.org/10.1021/acs.langmuir.8b02991
|3 Volltext
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