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...

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Bibliographic Details
Published in:Journal of Molecular Catalysis B: Enzymatic
Main Authors: Abdallah, Noreldeen Hassan., Schlumpberger, Miriam., Gaffney, Darragh, Hanrahan, John P., Tobin, Joseph M., Magner, Edmond
Other Authors: IRC, SFI, HEA
Format: Article in Journal/Newspaper
Language:English
Published: Elsevier 2014
Subjects:
Online Access:http://hdl.handle.net/10344/4698
https://doi.org/10.1016/j.molcatb.2014.06.007
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spelling 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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