Synthesis of Benzyl Acetate Catalyzed by Lipase Immobilized in Nontoxic Chitosan-Polyphosphate Beads
Enzymes serve as biocatalysts for innumerable important reactions, however, their application has limitations, which can in many cases be overcome by using appropriate immobilization strategies. Here, a new support for immobilizing enzymes is proposed. This hybrid organic-inorganic support is compos...
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ftdoajarticles:oai:doaj.org/article:3dace6ff752549c0a1ab23cbd79f042c 2023-05-15T13:44:17+02:00 Synthesis of Benzyl Acetate Catalyzed by Lipase Immobilized in Nontoxic Chitosan-Polyphosphate Beads Ana D. Q. Melo Francisco F. M. Silva José C. S. dos Santos Roberto Fernández-Lafuente Telma L. G. Lemos Francisco A. Dias Filho 2017-12-01T00:00:00Z https://doi.org/10.3390/molecules22122165 https://doaj.org/article/3dace6ff752549c0a1ab23cbd79f042c EN eng MDPI AG https://www.mdpi.com/1420-3049/22/12/2165 https://doaj.org/toc/1420-3049 1420-3049 doi:10.3390/molecules22122165 https://doaj.org/article/3dace6ff752549c0a1ab23cbd79f042c Molecules, Vol 22, Iss 12, p 2165 (2017) chitosan polyphosphate microspheres immobilization lipase CALB Organic chemistry QD241-441 article 2017 ftdoajarticles https://doi.org/10.3390/molecules22122165 2022-12-31T16:32:17Z Enzymes serve as biocatalysts for innumerable important reactions, however, their application has limitations, which can in many cases be overcome by using appropriate immobilization strategies. Here, a new support for immobilizing enzymes is proposed. This hybrid organic-inorganic support is composed of chitosan—a natural, nontoxic, biodegradable, and edible biopolymer—and sodium polyphosphate as the inorganic component. Lipase B from Candida antarctica (CALB) was immobilized on microspheres by encapsulation using these polymers. The characterization of the composites (by infrared spectroscopy, thermogravimetric analysis, and confocal Raman microscopy) confirmed the hybrid nature of the support, whose external part consisted of polyphosphate and core was composed of chitosan. The immobilized enzyme had the following advantages: possibility of enzyme reuse, easy biocatalyst recovery, increased resistance to variations in temperature (activity declined from 60 °C and the enzyme was inactivated at 80 °C), and increased catalytic activity in the transesterification reactions. The encapsulated enzymes were utilized as biocatalysts for transesterification reactions to produce the compound responsible for the aroma of jasmine. Article in Journal/Newspaper Antarc* Antarctica Directory of Open Access Journals: DOAJ Articles Molecules 22 12 2165 |
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Open Polar |
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Directory of Open Access Journals: DOAJ Articles |
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ftdoajarticles |
language |
English |
topic |
chitosan polyphosphate microspheres immobilization lipase CALB Organic chemistry QD241-441 |
spellingShingle |
chitosan polyphosphate microspheres immobilization lipase CALB Organic chemistry QD241-441 Ana D. Q. Melo Francisco F. M. Silva José C. S. dos Santos Roberto Fernández-Lafuente Telma L. G. Lemos Francisco A. Dias Filho Synthesis of Benzyl Acetate Catalyzed by Lipase Immobilized in Nontoxic Chitosan-Polyphosphate Beads |
topic_facet |
chitosan polyphosphate microspheres immobilization lipase CALB Organic chemistry QD241-441 |
description |
Enzymes serve as biocatalysts for innumerable important reactions, however, their application has limitations, which can in many cases be overcome by using appropriate immobilization strategies. Here, a new support for immobilizing enzymes is proposed. This hybrid organic-inorganic support is composed of chitosan—a natural, nontoxic, biodegradable, and edible biopolymer—and sodium polyphosphate as the inorganic component. Lipase B from Candida antarctica (CALB) was immobilized on microspheres by encapsulation using these polymers. The characterization of the composites (by infrared spectroscopy, thermogravimetric analysis, and confocal Raman microscopy) confirmed the hybrid nature of the support, whose external part consisted of polyphosphate and core was composed of chitosan. The immobilized enzyme had the following advantages: possibility of enzyme reuse, easy biocatalyst recovery, increased resistance to variations in temperature (activity declined from 60 °C and the enzyme was inactivated at 80 °C), and increased catalytic activity in the transesterification reactions. The encapsulated enzymes were utilized as biocatalysts for transesterification reactions to produce the compound responsible for the aroma of jasmine. |
format |
Article in Journal/Newspaper |
author |
Ana D. Q. Melo Francisco F. M. Silva José C. S. dos Santos Roberto Fernández-Lafuente Telma L. G. Lemos Francisco A. Dias Filho |
author_facet |
Ana D. Q. Melo Francisco F. M. Silva José C. S. dos Santos Roberto Fernández-Lafuente Telma L. G. Lemos Francisco A. Dias Filho |
author_sort |
Ana D. Q. Melo |
title |
Synthesis of Benzyl Acetate Catalyzed by Lipase Immobilized in Nontoxic Chitosan-Polyphosphate Beads |
title_short |
Synthesis of Benzyl Acetate Catalyzed by Lipase Immobilized in Nontoxic Chitosan-Polyphosphate Beads |
title_full |
Synthesis of Benzyl Acetate Catalyzed by Lipase Immobilized in Nontoxic Chitosan-Polyphosphate Beads |
title_fullStr |
Synthesis of Benzyl Acetate Catalyzed by Lipase Immobilized in Nontoxic Chitosan-Polyphosphate Beads |
title_full_unstemmed |
Synthesis of Benzyl Acetate Catalyzed by Lipase Immobilized in Nontoxic Chitosan-Polyphosphate Beads |
title_sort |
synthesis of benzyl acetate catalyzed by lipase immobilized in nontoxic chitosan-polyphosphate beads |
publisher |
MDPI AG |
publishDate |
2017 |
url |
https://doi.org/10.3390/molecules22122165 https://doaj.org/article/3dace6ff752549c0a1ab23cbd79f042c |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Molecules, Vol 22, Iss 12, p 2165 (2017) |
op_relation |
https://www.mdpi.com/1420-3049/22/12/2165 https://doaj.org/toc/1420-3049 1420-3049 doi:10.3390/molecules22122165 https://doaj.org/article/3dace6ff752549c0a1ab23cbd79f042c |
op_doi |
https://doi.org/10.3390/molecules22122165 |
container_title |
Molecules |
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22 |
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12 |
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2165 |
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1766199772260073472 |