Efficient and Stable Magnetic Chitosan-Lipase B from Candida Antarctica Bioconjugates in the Enzymatic Kinetic Resolution of Racemic Heteroarylethanols
Lipase B from Candida antarctica immobilized by covalent binding on sebacoyl-activated chitosan-coated magnetic nanoparticles proved to be an efficient biocatalyst (49.2–50% conversion in 3–16 h and >96% enantiomeric excess) for the enzymatic kinetic resolution of some racemic heteroarylethanols...
| Published in: | Molecules |
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| Main Authors: | , , , , , |
| Format: | Text |
| Language: | English |
| Published: |
Multidisciplinary Digital Publishing Institute
2020
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| Subjects: | |
| Online Access: | https://doi.org/10.3390/molecules25020350 |
| _version_ | 1821711696336519168 |
|---|---|
| author | Cristina Georgiana Spelmezan László Csaba Bencze Gabriel Katona Florin Dan Irimie Csaba Paizs Monica Ioana Toșa |
| author_facet | Cristina Georgiana Spelmezan László Csaba Bencze Gabriel Katona Florin Dan Irimie Csaba Paizs Monica Ioana Toșa |
| author_sort | Cristina Georgiana Spelmezan |
| collection | MDPI Open Access Publishing |
| container_issue | 2 |
| container_start_page | 350 |
| container_title | Molecules |
| container_volume | 25 |
| description | Lipase B from Candida antarctica immobilized by covalent binding on sebacoyl-activated chitosan-coated magnetic nanoparticles proved to be an efficient biocatalyst (49.2–50% conversion in 3–16 h and >96% enantiomeric excess) for the enzymatic kinetic resolution of some racemic heteroarylethanols through transesterification with vinyl acetate. Under optimal conditions (vinyl acetate, n-hexane, 45 °C), the biocatalyst remains active after 10 cycles. |
| format | Text |
| genre | Antarc* Antarctica |
| genre_facet | Antarc* Antarctica |
| id | ftmdpi:oai:mdpi.com:/1420-3049/25/2/350/ |
| institution | Open Polar |
| language | English |
| op_collection_id | ftmdpi |
| op_coverage | agris |
| op_doi | https://doi.org/10.3390/molecules25020350 |
| op_relation | Organic Chemistry https://dx.doi.org/10.3390/molecules25020350 |
| op_rights | https://creativecommons.org/licenses/by/4.0/ |
| op_source | Molecules; Volume 25; Issue 2; Pages: 350 |
| publishDate | 2020 |
| publisher | Multidisciplinary Digital Publishing Institute |
| record_format | openpolar |
| spelling | ftmdpi:oai:mdpi.com:/1420-3049/25/2/350/ 2025-01-16T19:16:37+00:00 Efficient and Stable Magnetic Chitosan-Lipase B from Candida Antarctica Bioconjugates in the Enzymatic Kinetic Resolution of Racemic Heteroarylethanols Cristina Georgiana Spelmezan László Csaba Bencze Gabriel Katona Florin Dan Irimie Csaba Paizs Monica Ioana Toșa agris 2020-01-15 application/pdf https://doi.org/10.3390/molecules25020350 EN eng Multidisciplinary Digital Publishing Institute Organic Chemistry https://dx.doi.org/10.3390/molecules25020350 https://creativecommons.org/licenses/by/4.0/ Molecules; Volume 25; Issue 2; Pages: 350 lipase B from Candida antarctica magnetic nanoparticle chitosan covalent immobilization enzymatic kinetic resolution Text 2020 ftmdpi https://doi.org/10.3390/molecules25020350 2023-07-31T23:00:06Z Lipase B from Candida antarctica immobilized by covalent binding on sebacoyl-activated chitosan-coated magnetic nanoparticles proved to be an efficient biocatalyst (49.2–50% conversion in 3–16 h and >96% enantiomeric excess) for the enzymatic kinetic resolution of some racemic heteroarylethanols through transesterification with vinyl acetate. Under optimal conditions (vinyl acetate, n-hexane, 45 °C), the biocatalyst remains active after 10 cycles. Text Antarc* Antarctica MDPI Open Access Publishing Molecules 25 2 350 |
| spellingShingle | lipase B from Candida antarctica magnetic nanoparticle chitosan covalent immobilization enzymatic kinetic resolution Cristina Georgiana Spelmezan László Csaba Bencze Gabriel Katona Florin Dan Irimie Csaba Paizs Monica Ioana Toșa Efficient and Stable Magnetic Chitosan-Lipase B from Candida Antarctica Bioconjugates in the Enzymatic Kinetic Resolution of Racemic Heteroarylethanols |
| title | Efficient and Stable Magnetic Chitosan-Lipase B from Candida Antarctica Bioconjugates in the Enzymatic Kinetic Resolution of Racemic Heteroarylethanols |
| title_full | Efficient and Stable Magnetic Chitosan-Lipase B from Candida Antarctica Bioconjugates in the Enzymatic Kinetic Resolution of Racemic Heteroarylethanols |
| title_fullStr | Efficient and Stable Magnetic Chitosan-Lipase B from Candida Antarctica Bioconjugates in the Enzymatic Kinetic Resolution of Racemic Heteroarylethanols |
| title_full_unstemmed | Efficient and Stable Magnetic Chitosan-Lipase B from Candida Antarctica Bioconjugates in the Enzymatic Kinetic Resolution of Racemic Heteroarylethanols |
| title_short | Efficient and Stable Magnetic Chitosan-Lipase B from Candida Antarctica Bioconjugates in the Enzymatic Kinetic Resolution of Racemic Heteroarylethanols |
| title_sort | efficient and stable magnetic chitosan-lipase b from candida antarctica bioconjugates in the enzymatic kinetic resolution of racemic heteroarylethanols |
| topic | lipase B from Candida antarctica magnetic nanoparticle chitosan covalent immobilization enzymatic kinetic resolution |
| topic_facet | lipase B from Candida antarctica magnetic nanoparticle chitosan covalent immobilization enzymatic kinetic resolution |
| url | https://doi.org/10.3390/molecules25020350 |