Immobilization of Lipase B from <i>Candida antarctica</i> on Magnetic Nanoparticles Enhances Its Selectivity in Kinetic Resolutions of Chiral Amines with Several Acylating Agents
In lipase-catalyzed kinetic resolutions (KRs), the choice of immobilization support and acylating agents (AAs) is crucial. Lipase B from <i>Candida antarctica</i> immobilized onto magnetic nanoparticles (CaLB-MNPs) has been successfully used for diverse KRs of racemic compounds, but ther...
| Main Authors: | , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2023-07-01
|
| Series: | Life |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2075-1729/13/7/1560 |
| _version_ | 1797588591899049984 |
|---|---|
| author | Fausto M. W. G. Silva József Szemes Akan Mustashev Orsolya Takács Ali O. Imarah László Poppe |
| author_facet | Fausto M. W. G. Silva József Szemes Akan Mustashev Orsolya Takács Ali O. Imarah László Poppe |
| author_sort | Fausto M. W. G. Silva |
| collection | DOAJ |
| description | In lipase-catalyzed kinetic resolutions (KRs), the choice of immobilization support and acylating agents (AAs) is crucial. Lipase B from <i>Candida antarctica</i> immobilized onto magnetic nanoparticles (CaLB-MNPs) has been successfully used for diverse KRs of racemic compounds, but there is a lack of studies of the utilization of this potent biocatalyst in the KR of chiral amines, important pharmaceutical building blocks. Therefore, in this work, several racemic amines (heptane-2-amine, 1-methoxypropan-2-amine, 1-phenylethan-1-amine, and 4-phenylbutan-2-amine, (±)-<b>1a</b>–<b>d</b>, respectively) were studied in batch and continuous-flow mode utilizing different AAs, such as diisopropyl malonate <b>2A</b>, isopropyl 2-cyanoacetate <b>2B</b>, and isopropyl 2-ethoxyacetate <b>2C</b>. The reactions performed with CaLB-MNPs were compared with Novozym 435 (N435) and the results in the literature. CaLB-MNPs were less active than N435, leading to lower conversion, but demonstrated a higher enantiomer selectivity, proving to be a good alternative to the commercial form. Compound <b>2C</b> resulted in the best balance between conversion and enantiomer selectivity among the acylating agents. CaLB-MNPs proved to be efficient in the KR of chiral amines, having comparable or superior properties to other CaLB forms utilizing porous matrices for immobilization. An additional advantage of using CaLB-MNPs is that the purification and reuse processes are facilitated via magnetic retention/separation. In the continuous-flow mode, the usability and operational stability of CaLB-MNPs were reaffirmed, corroborating with previous studies, and the results overall improve our understanding of this potent biocatalyst and the convenient U-shape reactor used. |
| first_indexed | 2024-03-11T00:54:14Z |
| format | Article |
| id | doaj.art-d1aedcf7e6614246bc9894bb710efe62 |
| institution | Directory Open Access Journal |
| issn | 2075-1729 |
| language | English |
| last_indexed | 2024-03-11T00:54:14Z |
| publishDate | 2023-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Life |
| spelling | doaj.art-d1aedcf7e6614246bc9894bb710efe622023-11-18T20:10:13ZengMDPI AGLife2075-17292023-07-01137156010.3390/life13071560Immobilization of Lipase B from <i>Candida antarctica</i> on Magnetic Nanoparticles Enhances Its Selectivity in Kinetic Resolutions of Chiral Amines with Several Acylating AgentsFausto M. W. G. Silva0József Szemes1Akan Mustashev2Orsolya Takács3Ali O. Imarah4László Poppe5Department of Organic Chemistry and Technology, Budapest University of Technology and Economics, Műegyetem rkp. 3, H-1111 Budapest, HungaryDepartment of Organic Chemistry and Technology, Budapest University of Technology and Economics, Műegyetem rkp. 3, H-1111 Budapest, HungaryDepartment of Organic Chemistry and Technology, Budapest University of Technology and Economics, Műegyetem rkp. 3, H-1111 Budapest, HungaryDepartment of Organic Chemistry and Technology, Budapest University of Technology and Economics, Műegyetem rkp. 3, H-1111 Budapest, HungaryDepartment of Organic Chemistry and Technology, Budapest University of Technology and Economics, Műegyetem rkp. 3, H-1111 Budapest, HungaryDepartment of Organic Chemistry and Technology, Budapest University of Technology and Economics, Műegyetem rkp. 3, H-1111 Budapest, HungaryIn lipase-catalyzed kinetic resolutions (KRs), the choice of immobilization support and acylating agents (AAs) is crucial. Lipase B from <i>Candida antarctica</i> immobilized onto magnetic nanoparticles (CaLB-MNPs) has been successfully used for diverse KRs of racemic compounds, but there is a lack of studies of the utilization of this potent biocatalyst in the KR of chiral amines, important pharmaceutical building blocks. Therefore, in this work, several racemic amines (heptane-2-amine, 1-methoxypropan-2-amine, 1-phenylethan-1-amine, and 4-phenylbutan-2-amine, (±)-<b>1a</b>–<b>d</b>, respectively) were studied in batch and continuous-flow mode utilizing different AAs, such as diisopropyl malonate <b>2A</b>, isopropyl 2-cyanoacetate <b>2B</b>, and isopropyl 2-ethoxyacetate <b>2C</b>. The reactions performed with CaLB-MNPs were compared with Novozym 435 (N435) and the results in the literature. CaLB-MNPs were less active than N435, leading to lower conversion, but demonstrated a higher enantiomer selectivity, proving to be a good alternative to the commercial form. Compound <b>2C</b> resulted in the best balance between conversion and enantiomer selectivity among the acylating agents. CaLB-MNPs proved to be efficient in the KR of chiral amines, having comparable or superior properties to other CaLB forms utilizing porous matrices for immobilization. An additional advantage of using CaLB-MNPs is that the purification and reuse processes are facilitated via magnetic retention/separation. In the continuous-flow mode, the usability and operational stability of CaLB-MNPs were reaffirmed, corroborating with previous studies, and the results overall improve our understanding of this potent biocatalyst and the convenient U-shape reactor used.https://www.mdpi.com/2075-1729/13/7/1560biocatalysiskinetic resolutionchiral aminesacylationlipase B from <i>Candida antarctica</i>magnetic nanoparticles |
| spellingShingle | Fausto M. W. G. Silva József Szemes Akan Mustashev Orsolya Takács Ali O. Imarah László Poppe Immobilization of Lipase B from <i>Candida antarctica</i> on Magnetic Nanoparticles Enhances Its Selectivity in Kinetic Resolutions of Chiral Amines with Several Acylating Agents Life biocatalysis kinetic resolution chiral amines acylation lipase B from <i>Candida antarctica</i> magnetic nanoparticles |
| title | Immobilization of Lipase B from <i>Candida antarctica</i> on Magnetic Nanoparticles Enhances Its Selectivity in Kinetic Resolutions of Chiral Amines with Several Acylating Agents |
| title_full | Immobilization of Lipase B from <i>Candida antarctica</i> on Magnetic Nanoparticles Enhances Its Selectivity in Kinetic Resolutions of Chiral Amines with Several Acylating Agents |
| title_fullStr | Immobilization of Lipase B from <i>Candida antarctica</i> on Magnetic Nanoparticles Enhances Its Selectivity in Kinetic Resolutions of Chiral Amines with Several Acylating Agents |
| title_full_unstemmed | Immobilization of Lipase B from <i>Candida antarctica</i> on Magnetic Nanoparticles Enhances Its Selectivity in Kinetic Resolutions of Chiral Amines with Several Acylating Agents |
| title_short | Immobilization of Lipase B from <i>Candida antarctica</i> on Magnetic Nanoparticles Enhances Its Selectivity in Kinetic Resolutions of Chiral Amines with Several Acylating Agents |
| title_sort | immobilization of lipase b from i candida antarctica i on magnetic nanoparticles enhances its selectivity in kinetic resolutions of chiral amines with several acylating agents |
| topic | biocatalysis kinetic resolution chiral amines acylation lipase B from <i>Candida antarctica</i> magnetic nanoparticles |
| url | https://www.mdpi.com/2075-1729/13/7/1560 |
| work_keys_str_mv | AT faustomwgsilva immobilizationoflipasebfromicandidaantarcticaionmagneticnanoparticlesenhancesitsselectivityinkineticresolutionsofchiralamineswithseveralacylatingagents AT jozsefszemes immobilizationoflipasebfromicandidaantarcticaionmagneticnanoparticlesenhancesitsselectivityinkineticresolutionsofchiralamineswithseveralacylatingagents AT akanmustashev immobilizationoflipasebfromicandidaantarcticaionmagneticnanoparticlesenhancesitsselectivityinkineticresolutionsofchiralamineswithseveralacylatingagents AT orsolyatakacs immobilizationoflipasebfromicandidaantarcticaionmagneticnanoparticlesenhancesitsselectivityinkineticresolutionsofchiralamineswithseveralacylatingagents AT alioimarah immobilizationoflipasebfromicandidaantarcticaionmagneticnanoparticlesenhancesitsselectivityinkineticresolutionsofchiralamineswithseveralacylatingagents AT laszlopoppe immobilizationoflipasebfromicandidaantarcticaionmagneticnanoparticlesenhancesitsselectivityinkineticresolutionsofchiralamineswithseveralacylatingagents |