Controlling performance of lipase immobilised on bioinspired silica

Lipase (Candida antarctica lipase B) was immobilised on silica that was produced via a mild route using a recently developed biologically inspired silica formation method. This route of immobilisation was favourable compared to traditional methods due to its simplicity, mild conditions, low cost, on...

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Published in:Journal of Materials Chemistry B
Main Authors: Forsyth, Claire, Patwardhan, Siddharth
Format: Article in Journal/Newspaper
Language:unknown
Published: 2013
Subjects:
Online Access:https://strathprints.strath.ac.uk/42459/
https://doi.org/10.1039/C2TB00462C
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author Forsyth, Claire
Patwardhan, Siddharth
author_facet Forsyth, Claire
Patwardhan, Siddharth
author_sort Forsyth, Claire
collection University of Strathclyde Glasgow: Strathprints
container_issue 8
container_start_page 1164
container_title Journal of Materials Chemistry B
container_volume 1
description Lipase (Candida antarctica lipase B) was immobilised on silica that was produced via a mild route using a recently developed biologically inspired silica formation method. This route of immobilisation was favourable compared to traditional methods due to its simplicity, mild conditions, low cost, one-step procedure and short preparation time. Lipase was chosen as the enzyme due to its wide implementation in industry, particularly in the food and pharmaceutical industries. Compared to other methods using bioinspired silica entrapment of enzymes, we demonstrate several significant improvements in the performance of the biocatalysts produced. Very high immobilisation efficiencies (close to 100%) were achieved under optimised conditions. The immobilised enzymes also displayed high levels of activity, which exceeded those reported in previous studies of lipase that was immobilised on bioinspired silica. Furthermore, we demonstrate the control over enzyme activity which was achieved through the entrapment conditions by regulating surface area, the average pore diameter and the mean particle size of the silica support. The immobilised enzymes also had very good reuse potential, and showed improved thermal and pH stability. The biocatalysts also performed well in turbulent conditions, showed good storage properties and were successfully used in bench-top reactors, therefore strongly supporting their use in commercial applications. The immobilised enzymes also performed comparably to or better than the industrial benchmark, Novozym® 435. The bioinspired method of immobilisation used has significant benefits over current methods, and these factors could increase potential applications in industry.
format Article in Journal/Newspaper
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op_doi https://doi.org/10.1039/C2TB00462C
op_relation Forsyth, Claire <https://strathprints.strath.ac.uk/view/author/570557.html> and Patwardhan, Siddharth <https://strathprints.strath.ac.uk/view/author/713409.html> (2013 <https://strathprints.strath.ac.uk/view/year/2013.html>) Controlling performance of lipase immobilised on bioinspired silica. Journal of Materials Chemistry B <https://strathprints.strath.ac.uk/view/publications/Journal_of_Materials_Chemistry_B.html>, 1. pp. 1164-1174. C2TB00462C.
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spelling ftustrathclyde:oai:strathprints.strath.ac.uk:42459 2025-04-20T14:24:28+00:00 Controlling performance of lipase immobilised on bioinspired silica Forsyth, Claire Patwardhan, Siddharth 2013 https://strathprints.strath.ac.uk/42459/ https://doi.org/10.1039/C2TB00462C unknown Forsyth, Claire <https://strathprints.strath.ac.uk/view/author/570557.html> and Patwardhan, Siddharth <https://strathprints.strath.ac.uk/view/author/713409.html> (2013 <https://strathprints.strath.ac.uk/view/year/2013.html>) Controlling performance of lipase immobilised on bioinspired silica. Journal of Materials Chemistry B <https://strathprints.strath.ac.uk/view/publications/Journal_of_Materials_Chemistry_B.html>, 1. pp. 1164-1174. C2TB00462C. Chemical engineering Article PeerReviewed 2013 ftustrathclyde https://doi.org/10.1039/C2TB00462C 2025-03-21T05:43:31Z Lipase (Candida antarctica lipase B) was immobilised on silica that was produced via a mild route using a recently developed biologically inspired silica formation method. This route of immobilisation was favourable compared to traditional methods due to its simplicity, mild conditions, low cost, one-step procedure and short preparation time. Lipase was chosen as the enzyme due to its wide implementation in industry, particularly in the food and pharmaceutical industries. Compared to other methods using bioinspired silica entrapment of enzymes, we demonstrate several significant improvements in the performance of the biocatalysts produced. Very high immobilisation efficiencies (close to 100%) were achieved under optimised conditions. The immobilised enzymes also displayed high levels of activity, which exceeded those reported in previous studies of lipase that was immobilised on bioinspired silica. Furthermore, we demonstrate the control over enzyme activity which was achieved through the entrapment conditions by regulating surface area, the average pore diameter and the mean particle size of the silica support. The immobilised enzymes also had very good reuse potential, and showed improved thermal and pH stability. The biocatalysts also performed well in turbulent conditions, showed good storage properties and were successfully used in bench-top reactors, therefore strongly supporting their use in commercial applications. The immobilised enzymes also performed comparably to or better than the industrial benchmark, Novozym® 435. The bioinspired method of immobilisation used has significant benefits over current methods, and these factors could increase potential applications in industry. Article in Journal/Newspaper Antarc* Antarctica University of Strathclyde Glasgow: Strathprints Journal of Materials Chemistry B 1 8 1164
spellingShingle Chemical engineering
Forsyth, Claire
Patwardhan, Siddharth
Controlling performance of lipase immobilised on bioinspired silica
title Controlling performance of lipase immobilised on bioinspired silica
title_full Controlling performance of lipase immobilised on bioinspired silica
title_fullStr Controlling performance of lipase immobilised on bioinspired silica
title_full_unstemmed Controlling performance of lipase immobilised on bioinspired silica
title_short Controlling performance of lipase immobilised on bioinspired silica
title_sort controlling performance of lipase immobilised on bioinspired silica
topic Chemical engineering
topic_facet Chemical engineering
url https://strathprints.strath.ac.uk/42459/
https://doi.org/10.1039/C2TB00462C