Shedding Light on Lipase Stability in Natural Deep Eutectic Solvents
This study presents the potential role of natural deep eutectic solvents (NADESs) in a lipase-catalyzed hydrolysis reaction as both a co-solvent in an aqueous solution and as a main solvent. Ammonium salts such as choline chloride (ChCl) were paired with different hydrogen bond donors such as glycer...
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Croatian Society of Chemical Engineers
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ftdoajarticles:oai:doaj.org/article:bdee6e745557434ebc34fae34dfd27e3 2023-05-15T14:15:31+02:00 Shedding Light on Lipase Stability in Natural Deep Eutectic Solvents A. A. Elgharbawy A. Hayyan M. Hayyan S. N. Rashid M. R. M. Nor M. Y. Zulkifli Y. Alias M. E. S. Mirghani 2018-10-01T00:00:00Z https://doi.org/10.15255/CABEQ.2018.1335 https://doaj.org/article/bdee6e745557434ebc34fae34dfd27e3 EN eng Croatian Society of Chemical Engineers http://silverstripe.fkit.hr/cabeq/assets/Uploads/08-3-2018.pdf https://doaj.org/toc/0352-9568 https://doaj.org/toc/1846-5153 doi:10.15255/CABEQ.2018.1335 0352-9568 1846-5153 https://doaj.org/article/bdee6e745557434ebc34fae34dfd27e3 Chemical and Biochemical Engineering Quarterly, Vol 32, Iss 3, Pp 359-370 (2018) biotransformation biotechnology ionic liquids choline chloride p-nitrophenyl palmitate lipase B Candida antartica Chemical engineering TP155-156 article 2018 ftdoajarticles https://doi.org/10.15255/CABEQ.2018.1335 2022-12-31T10:02:39Z This study presents the potential role of natural deep eutectic solvents (NADESs) in a lipase-catalyzed hydrolysis reaction as both a co-solvent in an aqueous solution and as a main solvent. Ammonium salts such as choline chloride (ChCl) were paired with different hydrogen bond donors such as glycerol and malonic acid and sugars (glucose, fructose and sucrose). The hydrolysis of p-nitrophenyl palmitate by six different lipases: lipase from porcine pancreas (PR), lipase from Candida rugosa (CR), Amano lipase PS, from Burkholderia cepacia (AM), lipase from Rhizopus niveus (RN), lipase acrylic resin from Candida antartica (ARC), lipase B Candida antartica immobilized on Immobead 150, recombinant from Aspergillus oryzae (CALB), were tested in five NADESs. The results showed that NADES3 prepared from ChCl/sucrose was the most promising solvent as it enhanced the activities of both CALB and lipase from porcine pancreas to 355 % and 345 %. The kinetics investigation confirmed the higher catalytic efficiency (kcat/Km) of lipases in the 40 % of (NADES3) and compared with the aqueous form. The trend achieved by NADES may be a promising approach for applications and further perspectives as genuinely green industrial solvents. Article in Journal/Newspaper antartic* Directory of Open Access Journals: DOAJ Articles Rugosa ENVELOPE(-61.250,-61.250,-62.633,-62.633) Chemical and Biochemical Engineering Quarterly 32 3 359 370 |
institution |
Open Polar |
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Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
biotransformation biotechnology ionic liquids choline chloride p-nitrophenyl palmitate lipase B Candida antartica Chemical engineering TP155-156 |
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biotransformation biotechnology ionic liquids choline chloride p-nitrophenyl palmitate lipase B Candida antartica Chemical engineering TP155-156 A. A. Elgharbawy A. Hayyan M. Hayyan S. N. Rashid M. R. M. Nor M. Y. Zulkifli Y. Alias M. E. S. Mirghani Shedding Light on Lipase Stability in Natural Deep Eutectic Solvents |
topic_facet |
biotransformation biotechnology ionic liquids choline chloride p-nitrophenyl palmitate lipase B Candida antartica Chemical engineering TP155-156 |
description |
This study presents the potential role of natural deep eutectic solvents (NADESs) in a lipase-catalyzed hydrolysis reaction as both a co-solvent in an aqueous solution and as a main solvent. Ammonium salts such as choline chloride (ChCl) were paired with different hydrogen bond donors such as glycerol and malonic acid and sugars (glucose, fructose and sucrose). The hydrolysis of p-nitrophenyl palmitate by six different lipases: lipase from porcine pancreas (PR), lipase from Candida rugosa (CR), Amano lipase PS, from Burkholderia cepacia (AM), lipase from Rhizopus niveus (RN), lipase acrylic resin from Candida antartica (ARC), lipase B Candida antartica immobilized on Immobead 150, recombinant from Aspergillus oryzae (CALB), were tested in five NADESs. The results showed that NADES3 prepared from ChCl/sucrose was the most promising solvent as it enhanced the activities of both CALB and lipase from porcine pancreas to 355 % and 345 %. The kinetics investigation confirmed the higher catalytic efficiency (kcat/Km) of lipases in the 40 % of (NADES3) and compared with the aqueous form. The trend achieved by NADES may be a promising approach for applications and further perspectives as genuinely green industrial solvents. |
format |
Article in Journal/Newspaper |
author |
A. A. Elgharbawy A. Hayyan M. Hayyan S. N. Rashid M. R. M. Nor M. Y. Zulkifli Y. Alias M. E. S. Mirghani |
author_facet |
A. A. Elgharbawy A. Hayyan M. Hayyan S. N. Rashid M. R. M. Nor M. Y. Zulkifli Y. Alias M. E. S. Mirghani |
author_sort |
A. A. Elgharbawy |
title |
Shedding Light on Lipase Stability in Natural Deep Eutectic Solvents |
title_short |
Shedding Light on Lipase Stability in Natural Deep Eutectic Solvents |
title_full |
Shedding Light on Lipase Stability in Natural Deep Eutectic Solvents |
title_fullStr |
Shedding Light on Lipase Stability in Natural Deep Eutectic Solvents |
title_full_unstemmed |
Shedding Light on Lipase Stability in Natural Deep Eutectic Solvents |
title_sort |
shedding light on lipase stability in natural deep eutectic solvents |
publisher |
Croatian Society of Chemical Engineers |
publishDate |
2018 |
url |
https://doi.org/10.15255/CABEQ.2018.1335 https://doaj.org/article/bdee6e745557434ebc34fae34dfd27e3 |
long_lat |
ENVELOPE(-61.250,-61.250,-62.633,-62.633) |
geographic |
Rugosa |
geographic_facet |
Rugosa |
genre |
antartic* |
genre_facet |
antartic* |
op_source |
Chemical and Biochemical Engineering Quarterly, Vol 32, Iss 3, Pp 359-370 (2018) |
op_relation |
http://silverstripe.fkit.hr/cabeq/assets/Uploads/08-3-2018.pdf https://doaj.org/toc/0352-9568 https://doaj.org/toc/1846-5153 doi:10.15255/CABEQ.2018.1335 0352-9568 1846-5153 https://doaj.org/article/bdee6e745557434ebc34fae34dfd27e3 |
op_doi |
https://doi.org/10.15255/CABEQ.2018.1335 |
container_title |
Chemical and Biochemical Engineering Quarterly |
container_volume |
32 |
container_issue |
3 |
container_start_page |
359 |
op_container_end_page |
370 |
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