Comparison of mesoporous silicate supports for the immobilisation and activity of cytochrome c and lipase
peer-reviewed The activity and stability of Candida antartica lipase B (CALB) and cytochrome c immobilised on to, SBA-15 and a porous spherical silicate material (PPS), were examined. The materials possess similar pore diameters but have different morphologies, pore volumes and surface areas. CALB e...
Published in: | Journal of Molecular Catalysis B: Enzymatic |
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Online Access: | http://hdl.handle.net/10344/4698 https://doi.org/10.1016/j.molcatb.2014.06.007 |
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ftunivlimerick:oai:ulir.ul.ie:10344/4698 2023-05-15T14:15:48+02:00 Comparison of mesoporous silicate supports for the immobilisation and activity of cytochrome c and lipase Abdallah, Noreldeen Hassan. Schlumpberger, Miriam. Gaffney, Darragh Hanrahan, John P. Tobin, Joseph M. Magner, Edmond IRC SFI HEA 2014 http://hdl.handle.net/10344/4698 https://doi.org/10.1016/j.molcatb.2014.06.007 eng eng Elsevier Journal of Molecular Catalysis B: Enzymatic108, pp. 82-88 http://dx.doi.org/10.1016/j.molcatb.2014.06.007 RFP/06/CHP001 http://hdl.handle.net/10344/4698 doi:10.1016/j.molcatb.2014.06.007 This is the author’s version of a work that was accepted for publication in Journal of Molecular Catalysis B: Enzymatic . Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Journal of Molecular Catalysis B: Enzymatic, 108, pp. 82-88, http://dx.doi.org/10.1016/j.molcatb.2014.06.007 info:eu-repo/semantics/openAccess mesoporous silicate immobilisation lipase cytochrome c info:eu-repo/semantics/article all_ul_research ul_published_reviewed 2014 ftunivlimerick https://doi.org/10.1016/j.molcatb.2014.06.007 2022-05-23T15:13:33Z peer-reviewed The activity and stability of Candida antartica lipase B (CALB) and cytochrome c immobilised on to, SBA-15 and a porous spherical silicate material (PPS), were examined. The materials possess similar pore diameters but have different morphologies, pore volumes and surface areas. CALB exhibited higher catalytic activity and stability on SBA-15 when compared to PPS, while cytochrome c showed similar catalytic activity on both materials. The activity of CALB immobilised on SBA-15 was retained (95%) after 7 uses, while CALB immobilised on PPS retained only 43% activity. Such changes can be mainly ascribed to the different physical properties (pore volume, surface area and pore shape) of the supports. Article in Journal/Newspaper antartic* University of Limerick: Institutional Repository (ULIR) Journal of Molecular Catalysis B: Enzymatic 108 82 88 |
institution |
Open Polar |
collection |
University of Limerick: Institutional Repository (ULIR) |
op_collection_id |
ftunivlimerick |
language |
English |
topic |
mesoporous silicate immobilisation lipase cytochrome c |
spellingShingle |
mesoporous silicate immobilisation lipase cytochrome c Abdallah, Noreldeen Hassan. Schlumpberger, Miriam. Gaffney, Darragh Hanrahan, John P. Tobin, Joseph M. Magner, Edmond Comparison of mesoporous silicate supports for the immobilisation and activity of cytochrome c and lipase |
topic_facet |
mesoporous silicate immobilisation lipase cytochrome c |
description |
peer-reviewed The activity and stability of Candida antartica lipase B (CALB) and cytochrome c immobilised on to, SBA-15 and a porous spherical silicate material (PPS), were examined. The materials possess similar pore diameters but have different morphologies, pore volumes and surface areas. CALB exhibited higher catalytic activity and stability on SBA-15 when compared to PPS, while cytochrome c showed similar catalytic activity on both materials. The activity of CALB immobilised on SBA-15 was retained (95%) after 7 uses, while CALB immobilised on PPS retained only 43% activity. Such changes can be mainly ascribed to the different physical properties (pore volume, surface area and pore shape) of the supports. |
author2 |
IRC SFI HEA |
format |
Article in Journal/Newspaper |
author |
Abdallah, Noreldeen Hassan. Schlumpberger, Miriam. Gaffney, Darragh Hanrahan, John P. Tobin, Joseph M. Magner, Edmond |
author_facet |
Abdallah, Noreldeen Hassan. Schlumpberger, Miriam. Gaffney, Darragh Hanrahan, John P. Tobin, Joseph M. Magner, Edmond |
author_sort |
Abdallah, Noreldeen Hassan. |
title |
Comparison of mesoporous silicate supports for the immobilisation and activity of cytochrome c and lipase |
title_short |
Comparison of mesoporous silicate supports for the immobilisation and activity of cytochrome c and lipase |
title_full |
Comparison of mesoporous silicate supports for the immobilisation and activity of cytochrome c and lipase |
title_fullStr |
Comparison of mesoporous silicate supports for the immobilisation and activity of cytochrome c and lipase |
title_full_unstemmed |
Comparison of mesoporous silicate supports for the immobilisation and activity of cytochrome c and lipase |
title_sort |
comparison of mesoporous silicate supports for the immobilisation and activity of cytochrome c and lipase |
publisher |
Elsevier |
publishDate |
2014 |
url |
http://hdl.handle.net/10344/4698 https://doi.org/10.1016/j.molcatb.2014.06.007 |
genre |
antartic* |
genre_facet |
antartic* |
op_relation |
Journal of Molecular Catalysis B: Enzymatic108, pp. 82-88 http://dx.doi.org/10.1016/j.molcatb.2014.06.007 RFP/06/CHP001 http://hdl.handle.net/10344/4698 doi:10.1016/j.molcatb.2014.06.007 |
op_rights |
This is the author’s version of a work that was accepted for publication in Journal of Molecular Catalysis B: Enzymatic . Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Journal of Molecular Catalysis B: Enzymatic, 108, pp. 82-88, http://dx.doi.org/10.1016/j.molcatb.2014.06.007 info:eu-repo/semantics/openAccess |
op_doi |
https://doi.org/10.1016/j.molcatb.2014.06.007 |
container_title |
Journal of Molecular Catalysis B: Enzymatic |
container_volume |
108 |
container_start_page |
82 |
op_container_end_page |
88 |
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1766288079564308480 |