Enhancing the Acyltransferase Activity of Candida antarctica Lipase A by Rational Design
Abstract A few lipases, such as Candida antarctica lipase A (CAL‐A), are known to possess acyltransferase activity. This enables the enzyme to synthesize fatty acid esters from natural oils and alcohols even in the presence of bulk water. Unfortunately, fatty acids are still formed in these reaction...
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crwiley:10.1002/cbic.201500187 2024-06-02T07:58:21+00:00 Enhancing the Acyltransferase Activity of Candida antarctica Lipase A by Rational Design Müller, Janett Sowa, Miriam A. Fredrich, Birte Brundiek, Henrike Bornscheuer, Uwe T. 2015 http://dx.doi.org/10.1002/cbic.201500187 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fcbic.201500187 https://onlinelibrary.wiley.com/doi/full/10.1002/cbic.201500187 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor ChemBioChem volume 16, issue 12, page 1791-1796 ISSN 1439-4227 1439-7633 journal-article 2015 crwiley https://doi.org/10.1002/cbic.201500187 2024-05-03T10:40:53Z Abstract A few lipases, such as Candida antarctica lipase A (CAL‐A), are known to possess acyltransferase activity. This enables the enzyme to synthesize fatty acid esters from natural oils and alcohols even in the presence of bulk water. Unfortunately, fatty acids are still formed in these reactions as undesired side‐products. To reduce the amount of fatty acids, several CAL‐A variants were rationally designed based on its crystal structure. These variants were expressed in Escherichia coli and Pichia pastoris , purified, and their acyltransferase/hydrolase activities were investigated by various biocatalytic approaches. Among the investigated variants, mutant Asp122Leu showed a significant decrease in the hydrolytic activity, thus reducing the side‐product yield during acylation. As desired, this variant retained wild‐type process‐relevant features like pH profile and thermostability. Article in Journal/Newspaper Antarc* Antarctica Wiley Online Library ChemBioChem 16 12 1791 1796 |
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Wiley Online Library |
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crwiley |
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English |
description |
Abstract A few lipases, such as Candida antarctica lipase A (CAL‐A), are known to possess acyltransferase activity. This enables the enzyme to synthesize fatty acid esters from natural oils and alcohols even in the presence of bulk water. Unfortunately, fatty acids are still formed in these reactions as undesired side‐products. To reduce the amount of fatty acids, several CAL‐A variants were rationally designed based on its crystal structure. These variants were expressed in Escherichia coli and Pichia pastoris , purified, and their acyltransferase/hydrolase activities were investigated by various biocatalytic approaches. Among the investigated variants, mutant Asp122Leu showed a significant decrease in the hydrolytic activity, thus reducing the side‐product yield during acylation. As desired, this variant retained wild‐type process‐relevant features like pH profile and thermostability. |
format |
Article in Journal/Newspaper |
author |
Müller, Janett Sowa, Miriam A. Fredrich, Birte Brundiek, Henrike Bornscheuer, Uwe T. |
spellingShingle |
Müller, Janett Sowa, Miriam A. Fredrich, Birte Brundiek, Henrike Bornscheuer, Uwe T. Enhancing the Acyltransferase Activity of Candida antarctica Lipase A by Rational Design |
author_facet |
Müller, Janett Sowa, Miriam A. Fredrich, Birte Brundiek, Henrike Bornscheuer, Uwe T. |
author_sort |
Müller, Janett |
title |
Enhancing the Acyltransferase Activity of Candida antarctica Lipase A by Rational Design |
title_short |
Enhancing the Acyltransferase Activity of Candida antarctica Lipase A by Rational Design |
title_full |
Enhancing the Acyltransferase Activity of Candida antarctica Lipase A by Rational Design |
title_fullStr |
Enhancing the Acyltransferase Activity of Candida antarctica Lipase A by Rational Design |
title_full_unstemmed |
Enhancing the Acyltransferase Activity of Candida antarctica Lipase A by Rational Design |
title_sort |
enhancing the acyltransferase activity of candida antarctica lipase a by rational design |
publisher |
Wiley |
publishDate |
2015 |
url |
http://dx.doi.org/10.1002/cbic.201500187 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fcbic.201500187 https://onlinelibrary.wiley.com/doi/full/10.1002/cbic.201500187 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
ChemBioChem volume 16, issue 12, page 1791-1796 ISSN 1439-4227 1439-7633 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/cbic.201500187 |
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ChemBioChem |
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16 |
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12 |
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1791 |
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1796 |
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1800741662556684288 |