Engineering of Candida antarctica Lipase B for Enhanced Perhydrolysis Activity by Modulating the Potential Water Channel
Abstract Although Candida antarctica lipase B (CAL‐B) naturally hydrolyzes an ester compounds, it can catalyze a variety of promiscuous reactions, such as perhydrolysis, aldol reaction, and Michael‐type reactions. Perhydrolysis is similar to hydrolysis but uses hydrogen peroxide instead of water mol...
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crwiley:10.1002/cctc.202301177 2024-06-02T07:57:42+00:00 Engineering of Candida antarctica Lipase B for Enhanced Perhydrolysis Activity by Modulating the Potential Water Channel Jeon, Minjeong Park, Seongsoon 2024 http://dx.doi.org/10.1002/cctc.202301177 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor ChemCatChem volume 16, issue 7 ISSN 1867-3880 1867-3899 journal-article 2024 crwiley https://doi.org/10.1002/cctc.202301177 2024-05-03T10:44:15Z Abstract Although Candida antarctica lipase B (CAL‐B) naturally hydrolyzes an ester compounds, it can catalyze a variety of promiscuous reactions, such as perhydrolysis, aldol reaction, and Michael‐type reactions. Perhydrolysis is similar to hydrolysis but uses hydrogen peroxide instead of water molecules. It was recently proposed that water molecules access the active site of CAL‐B through a water channel. We hypothesized that hydrogen peroxide may also use the channel to enter the active site, and that the access of hydrogen peroxide is one of the key factors for perhydrolysis activity. We investigated the effects of mutations at two residues in the water channel of CAL‐B on the perhydrolysis activity. The residues, Pro280 and Ala281, are located at the constricted area of the water channel. We found that the substitution of Ala281 to a small and polar amino acid, such as serine or threonine, resulted in a noticeable increase in hydrolysis and perhydrolysis activity. The activity of the variant enzymes was up to three times and twice higher for the activities of hydrolysis and perhydrolysis, respectively, than those of CAL‐B. In contrast, the substitution of the Pro280 residue with a small and polar amino acid decreased both hydrolysis and perhydrolysis activities. Article in Journal/Newspaper Antarc* Antarctica Wiley Online Library ChemCatChem |
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Wiley Online Library |
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English |
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Abstract Although Candida antarctica lipase B (CAL‐B) naturally hydrolyzes an ester compounds, it can catalyze a variety of promiscuous reactions, such as perhydrolysis, aldol reaction, and Michael‐type reactions. Perhydrolysis is similar to hydrolysis but uses hydrogen peroxide instead of water molecules. It was recently proposed that water molecules access the active site of CAL‐B through a water channel. We hypothesized that hydrogen peroxide may also use the channel to enter the active site, and that the access of hydrogen peroxide is one of the key factors for perhydrolysis activity. We investigated the effects of mutations at two residues in the water channel of CAL‐B on the perhydrolysis activity. The residues, Pro280 and Ala281, are located at the constricted area of the water channel. We found that the substitution of Ala281 to a small and polar amino acid, such as serine or threonine, resulted in a noticeable increase in hydrolysis and perhydrolysis activity. The activity of the variant enzymes was up to three times and twice higher for the activities of hydrolysis and perhydrolysis, respectively, than those of CAL‐B. In contrast, the substitution of the Pro280 residue with a small and polar amino acid decreased both hydrolysis and perhydrolysis activities. |
format |
Article in Journal/Newspaper |
author |
Jeon, Minjeong Park, Seongsoon |
spellingShingle |
Jeon, Minjeong Park, Seongsoon Engineering of Candida antarctica Lipase B for Enhanced Perhydrolysis Activity by Modulating the Potential Water Channel |
author_facet |
Jeon, Minjeong Park, Seongsoon |
author_sort |
Jeon, Minjeong |
title |
Engineering of Candida antarctica Lipase B for Enhanced Perhydrolysis Activity by Modulating the Potential Water Channel |
title_short |
Engineering of Candida antarctica Lipase B for Enhanced Perhydrolysis Activity by Modulating the Potential Water Channel |
title_full |
Engineering of Candida antarctica Lipase B for Enhanced Perhydrolysis Activity by Modulating the Potential Water Channel |
title_fullStr |
Engineering of Candida antarctica Lipase B for Enhanced Perhydrolysis Activity by Modulating the Potential Water Channel |
title_full_unstemmed |
Engineering of Candida antarctica Lipase B for Enhanced Perhydrolysis Activity by Modulating the Potential Water Channel |
title_sort |
engineering of candida antarctica lipase b for enhanced perhydrolysis activity by modulating the potential water channel |
publisher |
Wiley |
publishDate |
2024 |
url |
http://dx.doi.org/10.1002/cctc.202301177 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
ChemCatChem volume 16, issue 7 ISSN 1867-3880 1867-3899 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/cctc.202301177 |
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ChemCatChem |
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1800740891798798336 |