Flow-through immobilization of Candida rugosa lipase on hierarchical micro-/macroporous carbon monolith
Hierarchical micro-/macroporous carbon monoliths are prepared as enzyme carriers for flow-through process. The immobilization of Candida rugosa lipase on micro-/macroporous carbon monoliths is studied. Lipase is immobilized by physical adsorption which lipase solution is circulated through the micro...
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th-cmuir.6653943832-386152015-06-16T07:53:37Z Flow-through immobilization of Candida rugosa lipase on hierarchical micro-/macroporous carbon monolith Luangon,B. Siyasukh,A. Winayanuwattikun,P. Tanthapanichakoon,W. Tonanon,N. Catalysis Bioengineering Biochemistry Process Chemistry and Technology Hierarchical micro-/macroporous carbon monoliths are prepared as enzyme carriers for flow-through process. The immobilization of Candida rugosa lipase on micro-/macroporous carbon monoliths is studied. Lipase is immobilized by physical adsorption which lipase solution is circulated through the micro-/macroporous carbon monolith. An accessibility of lipase to the surface inside the micro-/macroporous carbon monolith is enhanced by flow-through method which promotes enzyme-surface interaction and finally leads to rapid enzyme immobilization. After immobilization is conducted for 10 min, the maximum protein binding can be measured. In terms of substrate-immobilized lipase reactions, flowing of substrate through lipase immobilized micro-/macroporous carbon monolith promotes high efficiency in both reaction and product withdrawal. Moreover, at high flow rates of lipase solution in immobilization step, the lipase activity increases. Oxygenated surface of micro-/macroporous carbon monoliths support also demonstrates an interesting effect on lipase immobilization and biocatalyst activity. The initial reaction rate of lipase immobilized on oxygenated surface carbon monolith support has higher activity compared with normal surface. © 2011 Elsevier B.V. All rights reserved. 2015-06-16T07:53:37Z 2015-06-16T07:53:37Z 2012-03-01 Article 13811177 2-s2.0-84855278988 10.1016/j.molcatb.2011.11.017 http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84855278988&origin=inward http://cmuir.cmu.ac.th/handle/6653943832/38615 Elsevier |
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Catalysis Bioengineering Biochemistry Process Chemistry and Technology Luangon,B. Siyasukh,A. Winayanuwattikun,P. Tanthapanichakoon,W. Tonanon,N. Flow-through immobilization of Candida rugosa lipase on hierarchical micro-/macroporous carbon monolith |
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Hierarchical micro-/macroporous carbon monoliths are prepared as enzyme carriers for flow-through process. The immobilization of Candida rugosa lipase on micro-/macroporous carbon monoliths is studied. Lipase is immobilized by physical adsorption which lipase solution is circulated through the micro-/macroporous carbon monolith. An accessibility of lipase to the surface inside the micro-/macroporous carbon monolith is enhanced by flow-through method which promotes enzyme-surface interaction and finally leads to rapid enzyme immobilization. After immobilization is conducted for 10 min, the maximum protein binding can be measured. In terms of substrate-immobilized lipase reactions, flowing of substrate through lipase immobilized micro-/macroporous carbon monolith promotes high efficiency in both reaction and product withdrawal. Moreover, at high flow rates of lipase solution in immobilization step, the lipase activity increases. Oxygenated surface of micro-/macroporous carbon monoliths support also demonstrates an interesting effect on lipase immobilization and biocatalyst activity. The initial reaction rate of lipase immobilized on oxygenated surface carbon monolith support has higher activity compared with normal surface. © 2011 Elsevier B.V. All rights reserved. |
format |
Article |
author |
Luangon,B. Siyasukh,A. Winayanuwattikun,P. Tanthapanichakoon,W. Tonanon,N. |
author_facet |
Luangon,B. Siyasukh,A. Winayanuwattikun,P. Tanthapanichakoon,W. Tonanon,N. |
author_sort |
Luangon,B. |
title |
Flow-through immobilization of Candida rugosa lipase on hierarchical micro-/macroporous carbon monolith |
title_short |
Flow-through immobilization of Candida rugosa lipase on hierarchical micro-/macroporous carbon monolith |
title_full |
Flow-through immobilization of Candida rugosa lipase on hierarchical micro-/macroporous carbon monolith |
title_fullStr |
Flow-through immobilization of Candida rugosa lipase on hierarchical micro-/macroporous carbon monolith |
title_full_unstemmed |
Flow-through immobilization of Candida rugosa lipase on hierarchical micro-/macroporous carbon monolith |
title_sort |
flow-through immobilization of candida rugosa lipase on hierarchical micro-/macroporous carbon monolith |
publisher |
Elsevier |
publishDate |
2015 |
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http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84855278988&origin=inward http://cmuir.cmu.ac.th/handle/6653943832/38615 |
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