Immobilization of Candida antarctica Lipase B on Fumed Silica
Enzymes are usually immobilized on solid supports or solubilized when they are to be used in organic solvents with poor enzyme solubility. We have reported previously on a novel immobilization method for s. Carlsberg on fumed silica with results that reached some of the best previously reported cata...
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ftkansassu:oai:krex.k-state.edu:2097/4494 2023-05-15T13:47:54+02:00 Immobilization of Candida antarctica Lipase B on Fumed Silica Cruz, Juan C. Pfromm, Peter H. Rezac, Mary E. pfromm rezac 2009 application/pdf http://hdl.handle.net/2097/4494 unknown http://doi.org/10.1016/j.procbio.2008.09.011 http://hdl.handle.net/2097/4494 This Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/ CALB Hexane Enzyme immobilization Fumed silica Adsorption Enzyme stability Text 2009 ftkansassu https://doi.org/10.1016/j.procbio.2008.09.011 2022-03-05T18:33:23Z Enzymes are usually immobilized on solid supports or solubilized when they are to be used in organic solvents with poor enzyme solubility. We have reported previously on a novel immobilization method for s. Carlsberg on fumed silica with results that reached some of the best previously reported catalytic activities in hexane for this enzyme. Here we extend our method to Candida antarctica lipase B (CALB) as an attractive target due to the many potential applications of this enzyme in solvents. Our CALB/fumed silica preparations approached the catalytic activity of commercial Novozym 435 for a model esterification in hexane at 90wt% fumed silica (relative to the mass of the preparation). An intriguing observation was that the catalytic activity at first increases as more fumed silica was made available to the enzyme but then decreased precipitously when 90wt% fumed silica was exceeded. This was not the case for s. Carlsberg where the catalytic activity leveled off at high relative amounts of fumed silica. We determined adsorption kinetics, performed variations of the pre-immobilization aqueous pH, determined the stability, and applied fluorescence microscopy to the preparations. A comparison with recent concepts by Gross et al. may point towards a rationale for an optimum intermediate surface coverage for some enzymes on solid supports. Text Antarc* Antarctica Kansas State University: K-State Research Exchange (K-REx) Process Biochemistry 44 1 62 69 |
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Kansas State University: K-State Research Exchange (K-REx) |
op_collection_id |
ftkansassu |
language |
unknown |
topic |
CALB Hexane Enzyme immobilization Fumed silica Adsorption Enzyme stability |
spellingShingle |
CALB Hexane Enzyme immobilization Fumed silica Adsorption Enzyme stability Cruz, Juan C. Pfromm, Peter H. Rezac, Mary E. Immobilization of Candida antarctica Lipase B on Fumed Silica |
topic_facet |
CALB Hexane Enzyme immobilization Fumed silica Adsorption Enzyme stability |
description |
Enzymes are usually immobilized on solid supports or solubilized when they are to be used in organic solvents with poor enzyme solubility. We have reported previously on a novel immobilization method for s. Carlsberg on fumed silica with results that reached some of the best previously reported catalytic activities in hexane for this enzyme. Here we extend our method to Candida antarctica lipase B (CALB) as an attractive target due to the many potential applications of this enzyme in solvents. Our CALB/fumed silica preparations approached the catalytic activity of commercial Novozym 435 for a model esterification in hexane at 90wt% fumed silica (relative to the mass of the preparation). An intriguing observation was that the catalytic activity at first increases as more fumed silica was made available to the enzyme but then decreased precipitously when 90wt% fumed silica was exceeded. This was not the case for s. Carlsberg where the catalytic activity leveled off at high relative amounts of fumed silica. We determined adsorption kinetics, performed variations of the pre-immobilization aqueous pH, determined the stability, and applied fluorescence microscopy to the preparations. A comparison with recent concepts by Gross et al. may point towards a rationale for an optimum intermediate surface coverage for some enzymes on solid supports. |
author2 |
pfromm rezac |
format |
Text |
author |
Cruz, Juan C. Pfromm, Peter H. Rezac, Mary E. |
author_facet |
Cruz, Juan C. Pfromm, Peter H. Rezac, Mary E. |
author_sort |
Cruz, Juan C. |
title |
Immobilization of Candida antarctica Lipase B on Fumed Silica |
title_short |
Immobilization of Candida antarctica Lipase B on Fumed Silica |
title_full |
Immobilization of Candida antarctica Lipase B on Fumed Silica |
title_fullStr |
Immobilization of Candida antarctica Lipase B on Fumed Silica |
title_full_unstemmed |
Immobilization of Candida antarctica Lipase B on Fumed Silica |
title_sort |
immobilization of candida antarctica lipase b on fumed silica |
publishDate |
2009 |
url |
http://hdl.handle.net/2097/4494 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
http://doi.org/10.1016/j.procbio.2008.09.011 http://hdl.handle.net/2097/4494 |
op_rights |
This Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/ |
op_doi |
https://doi.org/10.1016/j.procbio.2008.09.011 |
container_title |
Process Biochemistry |
container_volume |
44 |
container_issue |
1 |
container_start_page |
62 |
op_container_end_page |
69 |
_version_ |
1766247994823278592 |