Spongin-Based Scaffolds from Hippospongia communis Demosponge as an Effective Support for Lipase Immobilization

The main purpose of the study was to achieve effective immobilization of lipase B from Candida antarctica (CALB) onto 3D spongin-based scaffolds from Hippospongia communis marine demosponge for rapeseed oil transesterification. Successful immobilization onto the marine sponge skeleton was confirmed...

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Published in:Catalysts
Main Authors: Jakub Zdarta, Małgorzata Norman, Wojciech Smułek, Dariusz Moszyński, Ewa Kaczorek, Allison Stelling, Hermann Ehrlich, Teofil Jesionowski
Format: Text
Language:English
Published: Multidisciplinary Digital Publishing Institute 2017
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Online Access:https://doi.org/10.3390/catal7050147
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spelling ftmdpi:oai:mdpi.com:/2073-4344/7/5/147/ 2023-08-20T04:02:34+02:00 Spongin-Based Scaffolds from Hippospongia communis Demosponge as an Effective Support for Lipase Immobilization Jakub Zdarta Małgorzata Norman Wojciech Smułek Dariusz Moszyński Ewa Kaczorek Allison Stelling Hermann Ehrlich Teofil Jesionowski 2017-05-10 application/pdf https://doi.org/10.3390/catal7050147 EN eng Multidisciplinary Digital Publishing Institute https://dx.doi.org/10.3390/catal7050147 https://creativecommons.org/licenses/by/4.0/ Catalysts; Volume 7; Issue 5; Pages: 147 Hippospongia communis scaffolds lipase B from Candida antarctica lipase immobilization immobilized lipase stability and reusability rapeseed oil transesterification Text 2017 ftmdpi https://doi.org/10.3390/catal7050147 2023-07-31T21:06:53Z The main purpose of the study was to achieve effective immobilization of lipase B from Candida antarctica (CALB) onto 3D spongin-based scaffolds from Hippospongia communis marine demosponge for rapeseed oil transesterification. Successful immobilization onto the marine sponge skeleton was confirmed for the first time. Lipase B-containing biocatalytic system exhibited the highest catalytic activity retention (89%) after 60 min of immobilization at pH 7 and temperature of 4 °C. Immobilization was found to improve the thermal and chemical stability compared to free lipase, and retain over 80% of its initial catalytic activity over a wide range of temperature (30–60 °C) and pH (6–9). Additionally, immobilized lipase has good storage stability and retains over 70% of its initial activity even after catalyzing of 25 reaction cycles. The obtained product was used in a transesterification reaction of rapeseed oil with methanol and proved to be an efficient biocatalyst for biofuel production. The highest conversion value and fatty acids methyl esters (FAME) concentration were observed after a process conducted at 40 °C and pH 10. The possible mechanism of interaction between the enzyme and the spongin-based support is proposed and discussed. Text Antarc* Antarctica MDPI Open Access Publishing Catalysts 7 5 147
institution Open Polar
collection MDPI Open Access Publishing
op_collection_id ftmdpi
language English
topic Hippospongia communis scaffolds
lipase B from Candida antarctica
lipase immobilization
immobilized lipase stability and reusability
rapeseed oil transesterification
spellingShingle Hippospongia communis scaffolds
lipase B from Candida antarctica
lipase immobilization
immobilized lipase stability and reusability
rapeseed oil transesterification
Jakub Zdarta
Małgorzata Norman
Wojciech Smułek
Dariusz Moszyński
Ewa Kaczorek
Allison Stelling
Hermann Ehrlich
Teofil Jesionowski
Spongin-Based Scaffolds from Hippospongia communis Demosponge as an Effective Support for Lipase Immobilization
topic_facet Hippospongia communis scaffolds
lipase B from Candida antarctica
lipase immobilization
immobilized lipase stability and reusability
rapeseed oil transesterification
description The main purpose of the study was to achieve effective immobilization of lipase B from Candida antarctica (CALB) onto 3D spongin-based scaffolds from Hippospongia communis marine demosponge for rapeseed oil transesterification. Successful immobilization onto the marine sponge skeleton was confirmed for the first time. Lipase B-containing biocatalytic system exhibited the highest catalytic activity retention (89%) after 60 min of immobilization at pH 7 and temperature of 4 °C. Immobilization was found to improve the thermal and chemical stability compared to free lipase, and retain over 80% of its initial catalytic activity over a wide range of temperature (30–60 °C) and pH (6–9). Additionally, immobilized lipase has good storage stability and retains over 70% of its initial activity even after catalyzing of 25 reaction cycles. The obtained product was used in a transesterification reaction of rapeseed oil with methanol and proved to be an efficient biocatalyst for biofuel production. The highest conversion value and fatty acids methyl esters (FAME) concentration were observed after a process conducted at 40 °C and pH 10. The possible mechanism of interaction between the enzyme and the spongin-based support is proposed and discussed.
format Text
author Jakub Zdarta
Małgorzata Norman
Wojciech Smułek
Dariusz Moszyński
Ewa Kaczorek
Allison Stelling
Hermann Ehrlich
Teofil Jesionowski
author_facet Jakub Zdarta
Małgorzata Norman
Wojciech Smułek
Dariusz Moszyński
Ewa Kaczorek
Allison Stelling
Hermann Ehrlich
Teofil Jesionowski
author_sort Jakub Zdarta
title Spongin-Based Scaffolds from Hippospongia communis Demosponge as an Effective Support for Lipase Immobilization
title_short Spongin-Based Scaffolds from Hippospongia communis Demosponge as an Effective Support for Lipase Immobilization
title_full Spongin-Based Scaffolds from Hippospongia communis Demosponge as an Effective Support for Lipase Immobilization
title_fullStr Spongin-Based Scaffolds from Hippospongia communis Demosponge as an Effective Support for Lipase Immobilization
title_full_unstemmed Spongin-Based Scaffolds from Hippospongia communis Demosponge as an Effective Support for Lipase Immobilization
title_sort spongin-based scaffolds from hippospongia communis demosponge as an effective support for lipase immobilization
publisher Multidisciplinary Digital Publishing Institute
publishDate 2017
url https://doi.org/10.3390/catal7050147
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_source Catalysts; Volume 7; Issue 5; Pages: 147
op_relation https://dx.doi.org/10.3390/catal7050147
op_rights https://creativecommons.org/licenses/by/4.0/
op_doi https://doi.org/10.3390/catal7050147
container_title Catalysts
container_volume 7
container_issue 5
container_start_page 147
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