Hydrolysis of Hydrophobic Esters in a Bicontinuous Microemulsion Catalysed by Lipase B from Candida antarctica
Abstract Selective enzyme‐catalysed biotransformations offer great potential in organic chemistry. However, special requirements are needed to achieve optimum enzyme activity and stability. A bicontinuous microemulsion is proposed as reaction medium because of its large connected interface between o...
Published in: | Chemistry - A European Journal |
---|---|
Main Authors: | , , , |
Other Authors: | |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
Wiley
2014
|
Subjects: | |
Online Access: | http://dx.doi.org/10.1002/chem.201405335 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fchem.201405335 https://onlinelibrary.wiley.com/doi/full/10.1002/chem.201405335 |
id |
crwiley:10.1002/chem.201405335 |
---|---|
record_format |
openpolar |
spelling |
crwiley:10.1002/chem.201405335 2024-06-02T07:57:47+00:00 Hydrolysis of Hydrophobic Esters in a Bicontinuous Microemulsion Catalysed by Lipase B from Candida antarctica Steudle, Anne K. Subinya, Mireia Nestl, Bettina M. Stubenrauch, Cosima EPRSC 2014 http://dx.doi.org/10.1002/chem.201405335 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fchem.201405335 https://onlinelibrary.wiley.com/doi/full/10.1002/chem.201405335 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Chemistry – A European Journal volume 21, issue 6, page 2691-2700 ISSN 0947-6539 1521-3765 journal-article 2014 crwiley https://doi.org/10.1002/chem.201405335 2024-05-03T11:56:21Z Abstract Selective enzyme‐catalysed biotransformations offer great potential in organic chemistry. However, special requirements are needed to achieve optimum enzyme activity and stability. A bicontinuous microemulsion is proposed as reaction medium because of its large connected interface between oil and water domains at which a lipase can adsorb and convert substrates in the oil phase of the microemulsion. Herein, a microemulsion consisting of buffer– n ‐octane–nonionic surfactant C i E j was used to investigate the key factors that determine hydrolyses of p ‐nitrophenyl esters catalysed by the lipase B from Candida antarctica (CalB). The highest CalB activity was found around 44 °C in the absence of NaCl and substrates with larger alkyl chains were better hydrolysed than their short‐chained homologues. The CalB activity was determined using two different co‐surfactants, namely the phospholipid 1,2‐dioleoyl‐ sn ‐glycero‐3‐phosphocholine (DOPC) and the sugar surfactant decyl β‐ D ‐glucopyranoside (β‐C 10 G 1 ). The results show the CalB activity as linear function of both enzyme and substrate concentration with an enhanced activity when the sugar surfactant is used as co‐surfactant. Article in Journal/Newspaper Antarc* Antarctica Wiley Online Library Chemistry - A European Journal 21 6 2691 2700 |
institution |
Open Polar |
collection |
Wiley Online Library |
op_collection_id |
crwiley |
language |
English |
description |
Abstract Selective enzyme‐catalysed biotransformations offer great potential in organic chemistry. However, special requirements are needed to achieve optimum enzyme activity and stability. A bicontinuous microemulsion is proposed as reaction medium because of its large connected interface between oil and water domains at which a lipase can adsorb and convert substrates in the oil phase of the microemulsion. Herein, a microemulsion consisting of buffer– n ‐octane–nonionic surfactant C i E j was used to investigate the key factors that determine hydrolyses of p ‐nitrophenyl esters catalysed by the lipase B from Candida antarctica (CalB). The highest CalB activity was found around 44 °C in the absence of NaCl and substrates with larger alkyl chains were better hydrolysed than their short‐chained homologues. The CalB activity was determined using two different co‐surfactants, namely the phospholipid 1,2‐dioleoyl‐ sn ‐glycero‐3‐phosphocholine (DOPC) and the sugar surfactant decyl β‐ D ‐glucopyranoside (β‐C 10 G 1 ). The results show the CalB activity as linear function of both enzyme and substrate concentration with an enhanced activity when the sugar surfactant is used as co‐surfactant. |
author2 |
EPRSC |
format |
Article in Journal/Newspaper |
author |
Steudle, Anne K. Subinya, Mireia Nestl, Bettina M. Stubenrauch, Cosima |
spellingShingle |
Steudle, Anne K. Subinya, Mireia Nestl, Bettina M. Stubenrauch, Cosima Hydrolysis of Hydrophobic Esters in a Bicontinuous Microemulsion Catalysed by Lipase B from Candida antarctica |
author_facet |
Steudle, Anne K. Subinya, Mireia Nestl, Bettina M. Stubenrauch, Cosima |
author_sort |
Steudle, Anne K. |
title |
Hydrolysis of Hydrophobic Esters in a Bicontinuous Microemulsion Catalysed by Lipase B from Candida antarctica |
title_short |
Hydrolysis of Hydrophobic Esters in a Bicontinuous Microemulsion Catalysed by Lipase B from Candida antarctica |
title_full |
Hydrolysis of Hydrophobic Esters in a Bicontinuous Microemulsion Catalysed by Lipase B from Candida antarctica |
title_fullStr |
Hydrolysis of Hydrophobic Esters in a Bicontinuous Microemulsion Catalysed by Lipase B from Candida antarctica |
title_full_unstemmed |
Hydrolysis of Hydrophobic Esters in a Bicontinuous Microemulsion Catalysed by Lipase B from Candida antarctica |
title_sort |
hydrolysis of hydrophobic esters in a bicontinuous microemulsion catalysed by lipase b from candida antarctica |
publisher |
Wiley |
publishDate |
2014 |
url |
http://dx.doi.org/10.1002/chem.201405335 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fchem.201405335 https://onlinelibrary.wiley.com/doi/full/10.1002/chem.201405335 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Chemistry – A European Journal volume 21, issue 6, page 2691-2700 ISSN 0947-6539 1521-3765 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/chem.201405335 |
container_title |
Chemistry - A European Journal |
container_volume |
21 |
container_issue |
6 |
container_start_page |
2691 |
op_container_end_page |
2700 |
_version_ |
1800740984813780992 |