Kinetic resolution of drug intermediates catalyzed by lipase B from Candida antarctica immobilized on immobead‐350
Novozyme 435, which is a commercial immobilized lipase B from Candida antarctica (CALB), has been proven to be inadequate for the kinetic resolution of rac‐indanyl acetate. As it has been previously described that different immobilization protocols may greatly alter lipase features, in this work, CA...
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crwiley:10.1002/btpr.2630 2024-06-09T07:38:38+00:00 Kinetic resolution of drug intermediates catalyzed by lipase B from Candida antarctica immobilized on immobead‐350 Pinheiro, Maísa Pessoa Rios, Nathalia Saraiva Fonseca, Thiago de S. Bezerra, Francisco de Aquino Rodríguez‐Castellón, Enrique Fernandez‐Lafuente, Roberto Carlos de Mattos, Marcos dos Santos, José C. S. Gonçalves, Luciana R. B. Fundação Cearense de Apoio ao Desenvolvimento Científico e Tecnológico Conselho Nacional de Desenvolvimento Científico e Tecnológico Coordenação de Aperfeiçoamento de Pessoal de Nível Superior MINECO 2018 http://dx.doi.org/10.1002/btpr.2630 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbtpr.2630 http://onlinelibrary.wiley.com/wol1/doi/10.1002/btpr.2630/fullpdf en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Biotechnology Progress volume 34, issue 4, page 878-889 ISSN 8756-7938 1520-6033 journal-article 2018 crwiley https://doi.org/10.1002/btpr.2630 2024-05-16T14:27:58Z Novozyme 435, which is a commercial immobilized lipase B from Candida antarctica (CALB), has been proven to be inadequate for the kinetic resolution of rac‐indanyl acetate. As it has been previously described that different immobilization protocols may greatly alter lipase features, in this work, CALB was covalently immobilized on epoxy Immobead‐350 (IB‐350) and on glyoxyl‐agarose to ascertain if better kinetic resolution would result. Afterwards, all CALB biocatalysts were utilized in the hydrolytic resolution of rac ‐indanyl acetate and rac ‐(chloromethyl)‐2‐( o ‐methoxyphenoxy) ethyl acetate. After optimization of the immobilization protocol on IB‐350, its loading capacity was 150 mg protein/g dried support. Furthermore, the CALB‐IB‐350 thermal and solvent stabilities were higher than that of the soluble enzyme (e.g., by a 14‐fold factor at pH 5–70°C and by a 11‐fold factor in dioxane 30%–65°C) and that of the glyoxyl‐agarose‐CALB (e.g., by a 12‐fold factor at pH 10–50°C and by a 21‐fold factor in dioxane 30%–65°C). The CALB‐IB‐350 preparation (with 98% immobilization yield and activity versus p‐nitrophenyl butyrate of 6.26 ± 0.2 U/g) was used in the hydrolysis of rac ‐indanyl acetate using a biocatalyst/substrate ratio of 2:1 and a pH value of 7.0 at 30°C for 24 h. The conversion obtained was 48% and the enantiomeric excess of the product (e.e. p ) was 97%. These values were much higher than the ones obtained with Novozyme 435, 13% and 26% of conversion and e.e.p, respectively. © 2018 American Institute of Chemical Engineers Biotechnol. Prog. , 34:878–889, 2018 Article in Journal/Newspaper Antarc* Antarctica Wiley Online Library Biotechnology Progress 34 4 878 889 |
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Wiley Online Library |
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English |
description |
Novozyme 435, which is a commercial immobilized lipase B from Candida antarctica (CALB), has been proven to be inadequate for the kinetic resolution of rac‐indanyl acetate. As it has been previously described that different immobilization protocols may greatly alter lipase features, in this work, CALB was covalently immobilized on epoxy Immobead‐350 (IB‐350) and on glyoxyl‐agarose to ascertain if better kinetic resolution would result. Afterwards, all CALB biocatalysts were utilized in the hydrolytic resolution of rac ‐indanyl acetate and rac ‐(chloromethyl)‐2‐( o ‐methoxyphenoxy) ethyl acetate. After optimization of the immobilization protocol on IB‐350, its loading capacity was 150 mg protein/g dried support. Furthermore, the CALB‐IB‐350 thermal and solvent stabilities were higher than that of the soluble enzyme (e.g., by a 14‐fold factor at pH 5–70°C and by a 11‐fold factor in dioxane 30%–65°C) and that of the glyoxyl‐agarose‐CALB (e.g., by a 12‐fold factor at pH 10–50°C and by a 21‐fold factor in dioxane 30%–65°C). The CALB‐IB‐350 preparation (with 98% immobilization yield and activity versus p‐nitrophenyl butyrate of 6.26 ± 0.2 U/g) was used in the hydrolysis of rac ‐indanyl acetate using a biocatalyst/substrate ratio of 2:1 and a pH value of 7.0 at 30°C for 24 h. The conversion obtained was 48% and the enantiomeric excess of the product (e.e. p ) was 97%. These values were much higher than the ones obtained with Novozyme 435, 13% and 26% of conversion and e.e.p, respectively. © 2018 American Institute of Chemical Engineers Biotechnol. Prog. , 34:878–889, 2018 |
author2 |
Fundação Cearense de Apoio ao Desenvolvimento Científico e Tecnológico Conselho Nacional de Desenvolvimento Científico e Tecnológico Coordenação de Aperfeiçoamento de Pessoal de Nível Superior MINECO |
format |
Article in Journal/Newspaper |
author |
Pinheiro, Maísa Pessoa Rios, Nathalia Saraiva Fonseca, Thiago de S. Bezerra, Francisco de Aquino Rodríguez‐Castellón, Enrique Fernandez‐Lafuente, Roberto Carlos de Mattos, Marcos dos Santos, José C. S. Gonçalves, Luciana R. B. |
spellingShingle |
Pinheiro, Maísa Pessoa Rios, Nathalia Saraiva Fonseca, Thiago de S. Bezerra, Francisco de Aquino Rodríguez‐Castellón, Enrique Fernandez‐Lafuente, Roberto Carlos de Mattos, Marcos dos Santos, José C. S. Gonçalves, Luciana R. B. Kinetic resolution of drug intermediates catalyzed by lipase B from Candida antarctica immobilized on immobead‐350 |
author_facet |
Pinheiro, Maísa Pessoa Rios, Nathalia Saraiva Fonseca, Thiago de S. Bezerra, Francisco de Aquino Rodríguez‐Castellón, Enrique Fernandez‐Lafuente, Roberto Carlos de Mattos, Marcos dos Santos, José C. S. Gonçalves, Luciana R. B. |
author_sort |
Pinheiro, Maísa Pessoa |
title |
Kinetic resolution of drug intermediates catalyzed by lipase B from Candida antarctica immobilized on immobead‐350 |
title_short |
Kinetic resolution of drug intermediates catalyzed by lipase B from Candida antarctica immobilized on immobead‐350 |
title_full |
Kinetic resolution of drug intermediates catalyzed by lipase B from Candida antarctica immobilized on immobead‐350 |
title_fullStr |
Kinetic resolution of drug intermediates catalyzed by lipase B from Candida antarctica immobilized on immobead‐350 |
title_full_unstemmed |
Kinetic resolution of drug intermediates catalyzed by lipase B from Candida antarctica immobilized on immobead‐350 |
title_sort |
kinetic resolution of drug intermediates catalyzed by lipase b from candida antarctica immobilized on immobead‐350 |
publisher |
Wiley |
publishDate |
2018 |
url |
http://dx.doi.org/10.1002/btpr.2630 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbtpr.2630 http://onlinelibrary.wiley.com/wol1/doi/10.1002/btpr.2630/fullpdf |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Biotechnology Progress volume 34, issue 4, page 878-889 ISSN 8756-7938 1520-6033 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/btpr.2630 |
container_title |
Biotechnology Progress |
container_volume |
34 |
container_issue |
4 |
container_start_page |
878 |
op_container_end_page |
889 |
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1801374354821349376 |