Immobilization of lipase B from Candida antarctica on porous styrene–divinylbenzene beads improves butyl acetate synthesis
Abstract A new biocatalyst of lipase B from Candida antarctica (MCI‐CALB) immobilized on styrene–divinylbenzene beads (MCI GEL CHP20P) was compared with the commercial Novozym 435 (immobilized lipase) in terms of their performances as biocatalysts for the esterification of acetic acid and n‐butanol....
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crwiley:10.1002/btpr.1508 2024-09-15T17:47:52+00:00 Immobilization of lipase B from Candida antarctica on porous styrene–divinylbenzene beads improves butyl acetate synthesis Graebin, Natália G. Martins, Andréa B. Lorenzoni, André S. G. Garcia‐Galan, Cristina Fernandez‐Lafuente, Roberto Ayub, Marco A. Z. Rodrigues, Rafael C. 2012 http://dx.doi.org/10.1002/btpr.1508 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbtpr.1508 https://onlinelibrary.wiley.com/doi/full/10.1002/btpr.1508 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Biotechnology Progress volume 28, issue 2, page 406-412 ISSN 8756-7938 1520-6033 journal-article 2012 crwiley https://doi.org/10.1002/btpr.1508 2024-08-27T04:25:32Z Abstract A new biocatalyst of lipase B from Candida antarctica (MCI‐CALB) immobilized on styrene–divinylbenzene beads (MCI GEL CHP20P) was compared with the commercial Novozym 435 (immobilized lipase) in terms of their performances as biocatalysts for the esterification of acetic acid and n‐butanol. The effects of experimental conditions on reaction rates differed for each biocatalyst, showing different optimal values for water content, temperature, and substrate molar ratio. MCI‐CALB could be used at higher acid concentrations, up to 0.5 M, while Novozym 435 became inactivated at these acid concentrations. Although Novozym 435 exhibited 30% higher initial activity than MCI‐CALB for the butyl acetate synthesis, the reaction course was much more linear using the new preparation, meaning that the MCI‐CALB allows for higher productivities per cycle. Both preparations produced around 90% of yield conversions after only 2 h of reaction, using 10% (mass fraction) of enzyme. However, the main advantage of the new biocatalyst was the superior performance during reuse. While Novozym 435 was fully inactivated after only two batches, MCI‐CALB could be reused for six consecutive cycles without any washings and keeping around 70% of its initial activity. It is proposed that this effect is due to the higher hydrophobicity of the new support, which does not retain water or acid in the enzyme environment. MCI‐CALB has shown to be a very promising biocatalyst for the esterification of small‐molecule acids and alcohols. © 2012 American Institute of Chemical Engineers Biotechnol. Prog.,, 2012 Article in Journal/Newspaper Antarc* Antarctica Wiley Online Library Biotechnology Progress 28 2 406 412 |
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English |
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Abstract A new biocatalyst of lipase B from Candida antarctica (MCI‐CALB) immobilized on styrene–divinylbenzene beads (MCI GEL CHP20P) was compared with the commercial Novozym 435 (immobilized lipase) in terms of their performances as biocatalysts for the esterification of acetic acid and n‐butanol. The effects of experimental conditions on reaction rates differed for each biocatalyst, showing different optimal values for water content, temperature, and substrate molar ratio. MCI‐CALB could be used at higher acid concentrations, up to 0.5 M, while Novozym 435 became inactivated at these acid concentrations. Although Novozym 435 exhibited 30% higher initial activity than MCI‐CALB for the butyl acetate synthesis, the reaction course was much more linear using the new preparation, meaning that the MCI‐CALB allows for higher productivities per cycle. Both preparations produced around 90% of yield conversions after only 2 h of reaction, using 10% (mass fraction) of enzyme. However, the main advantage of the new biocatalyst was the superior performance during reuse. While Novozym 435 was fully inactivated after only two batches, MCI‐CALB could be reused for six consecutive cycles without any washings and keeping around 70% of its initial activity. It is proposed that this effect is due to the higher hydrophobicity of the new support, which does not retain water or acid in the enzyme environment. MCI‐CALB has shown to be a very promising biocatalyst for the esterification of small‐molecule acids and alcohols. © 2012 American Institute of Chemical Engineers Biotechnol. Prog.,, 2012 |
format |
Article in Journal/Newspaper |
author |
Graebin, Natália G. Martins, Andréa B. Lorenzoni, André S. G. Garcia‐Galan, Cristina Fernandez‐Lafuente, Roberto Ayub, Marco A. Z. Rodrigues, Rafael C. |
spellingShingle |
Graebin, Natália G. Martins, Andréa B. Lorenzoni, André S. G. Garcia‐Galan, Cristina Fernandez‐Lafuente, Roberto Ayub, Marco A. Z. Rodrigues, Rafael C. Immobilization of lipase B from Candida antarctica on porous styrene–divinylbenzene beads improves butyl acetate synthesis |
author_facet |
Graebin, Natália G. Martins, Andréa B. Lorenzoni, André S. G. Garcia‐Galan, Cristina Fernandez‐Lafuente, Roberto Ayub, Marco A. Z. Rodrigues, Rafael C. |
author_sort |
Graebin, Natália G. |
title |
Immobilization of lipase B from Candida antarctica on porous styrene–divinylbenzene beads improves butyl acetate synthesis |
title_short |
Immobilization of lipase B from Candida antarctica on porous styrene–divinylbenzene beads improves butyl acetate synthesis |
title_full |
Immobilization of lipase B from Candida antarctica on porous styrene–divinylbenzene beads improves butyl acetate synthesis |
title_fullStr |
Immobilization of lipase B from Candida antarctica on porous styrene–divinylbenzene beads improves butyl acetate synthesis |
title_full_unstemmed |
Immobilization of lipase B from Candida antarctica on porous styrene–divinylbenzene beads improves butyl acetate synthesis |
title_sort |
immobilization of lipase b from candida antarctica on porous styrene–divinylbenzene beads improves butyl acetate synthesis |
publisher |
Wiley |
publishDate |
2012 |
url |
http://dx.doi.org/10.1002/btpr.1508 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbtpr.1508 https://onlinelibrary.wiley.com/doi/full/10.1002/btpr.1508 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Biotechnology Progress volume 28, issue 2, page 406-412 ISSN 8756-7938 1520-6033 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/btpr.1508 |
container_title |
Biotechnology Progress |
container_volume |
28 |
container_issue |
2 |
container_start_page |
406 |
op_container_end_page |
412 |
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1810497560344788992 |