Glutaraldehyde Cross-Linking of Lipases Adsorbed on Aminated Supports in the Presence of Detergents Leads to Improved Performance
Lipases from Candida rugosa (CRL) and lipase isoforms A and B from Candida antarctica (CAL-A and CAL-B) were adsorbed on aminated supports in the presence of detergents to have individual lipase molecules. Then, one fraction was washed to eliminate the detergent, and both preparations were treated w...
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ftciteseerx:oai:CiteSeerX.psu:10.1.1.625.6179 2023-05-15T14:02:29+02:00 Glutaraldehyde Cross-Linking of Lipases Adsorbed on Aminated Supports in the Presence of Detergents Leads to Improved Performance Jose M. Palomo Cesar Mateo Roberto Munilla Claudia Ortiz Zaida Cabrera Jose M. Guisán The Pennsylvania State University CiteSeerX Archives 2006 application/pdf http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.625.6179 http://canli.dicp.ac.cn/Articles of Group Seminars/20070106zhangyanmei.pdf en eng http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.625.6179 http://canli.dicp.ac.cn/Articles of Group Seminars/20070106zhangyanmei.pdf Metadata may be used without restrictions as long as the oai identifier remains attached to it. http://canli.dicp.ac.cn/Articles of Group Seminars/20070106zhangyanmei.pdf text 2006 ftciteseerx 2016-01-08T15:12:31Z Lipases from Candida rugosa (CRL) and lipase isoforms A and B from Candida antarctica (CAL-A and CAL-B) were adsorbed on aminated supports in the presence of detergents to have individual lipase molecules. Then, one fraction was washed to eliminate the detergent, and both preparations were treated with glutaraldehyde. The presence of detergent during the cross-linking of the lipases to the support permitted an increase in the recovered activity (in some instances, even by a 10-fold factor). This activity was higher even than that exhibited by the just adsorbed lipases, suggesting that it was not a result of some protective effect of the detergent in the enzyme activity during glutaraldehyde chemical modification. Moreover, the enantioselectivity of the different enzyme preparations was very different if the glutaraldehyde was offered in the presence or in the absence of detergent, in some cases increasing the E value (even by a 7-fold factor in the case of CAL-A in the hydrolysis of (()-2-hydroxy-4-phenylbutyric acid ethyl ester), in other cases even inverting the enantio preference (e.g., in the case of CRL). The irreversible chemical inhibition of the enzyme that was immobilized and cross-linked with glutaraldehyde in the presence of detergents was more rapid than that in the other preparations (by more than a 10-fold factor). This experiment reveals an exposition degree of the active serine in the preparation cross-linked with the support in the presence of detergent that is higher than that in the other preparations. The results suggested that different enzyme structures were “stabilized ” by the glutaraldehyde treatment if performed in the presence or in the absence of detergent, and that, in the presence of detergent, a form of the lipase with the serine residue more exposed to the medium and much more active could be obtained. This strategy seems to be of general use to improve the lipase activity to be used in macroaqueous media. Text Antarc* Antarctica Unknown Rugosa ENVELOPE(-61.250,-61.250,-62.633,-62.633) |
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Open Polar |
collection |
Unknown |
op_collection_id |
ftciteseerx |
language |
English |
description |
Lipases from Candida rugosa (CRL) and lipase isoforms A and B from Candida antarctica (CAL-A and CAL-B) were adsorbed on aminated supports in the presence of detergents to have individual lipase molecules. Then, one fraction was washed to eliminate the detergent, and both preparations were treated with glutaraldehyde. The presence of detergent during the cross-linking of the lipases to the support permitted an increase in the recovered activity (in some instances, even by a 10-fold factor). This activity was higher even than that exhibited by the just adsorbed lipases, suggesting that it was not a result of some protective effect of the detergent in the enzyme activity during glutaraldehyde chemical modification. Moreover, the enantioselectivity of the different enzyme preparations was very different if the glutaraldehyde was offered in the presence or in the absence of detergent, in some cases increasing the E value (even by a 7-fold factor in the case of CAL-A in the hydrolysis of (()-2-hydroxy-4-phenylbutyric acid ethyl ester), in other cases even inverting the enantio preference (e.g., in the case of CRL). The irreversible chemical inhibition of the enzyme that was immobilized and cross-linked with glutaraldehyde in the presence of detergents was more rapid than that in the other preparations (by more than a 10-fold factor). This experiment reveals an exposition degree of the active serine in the preparation cross-linked with the support in the presence of detergent that is higher than that in the other preparations. The results suggested that different enzyme structures were “stabilized ” by the glutaraldehyde treatment if performed in the presence or in the absence of detergent, and that, in the presence of detergent, a form of the lipase with the serine residue more exposed to the medium and much more active could be obtained. This strategy seems to be of general use to improve the lipase activity to be used in macroaqueous media. |
author2 |
The Pennsylvania State University CiteSeerX Archives |
format |
Text |
author |
Jose M. Palomo Cesar Mateo Roberto Munilla Claudia Ortiz Zaida Cabrera Jose M. Guisán |
spellingShingle |
Jose M. Palomo Cesar Mateo Roberto Munilla Claudia Ortiz Zaida Cabrera Jose M. Guisán Glutaraldehyde Cross-Linking of Lipases Adsorbed on Aminated Supports in the Presence of Detergents Leads to Improved Performance |
author_facet |
Jose M. Palomo Cesar Mateo Roberto Munilla Claudia Ortiz Zaida Cabrera Jose M. Guisán |
author_sort |
Jose M. Palomo |
title |
Glutaraldehyde Cross-Linking of Lipases Adsorbed on Aminated Supports in the Presence of Detergents Leads to Improved Performance |
title_short |
Glutaraldehyde Cross-Linking of Lipases Adsorbed on Aminated Supports in the Presence of Detergents Leads to Improved Performance |
title_full |
Glutaraldehyde Cross-Linking of Lipases Adsorbed on Aminated Supports in the Presence of Detergents Leads to Improved Performance |
title_fullStr |
Glutaraldehyde Cross-Linking of Lipases Adsorbed on Aminated Supports in the Presence of Detergents Leads to Improved Performance |
title_full_unstemmed |
Glutaraldehyde Cross-Linking of Lipases Adsorbed on Aminated Supports in the Presence of Detergents Leads to Improved Performance |
title_sort |
glutaraldehyde cross-linking of lipases adsorbed on aminated supports in the presence of detergents leads to improved performance |
publishDate |
2006 |
url |
http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.625.6179 http://canli.dicp.ac.cn/Articles of Group Seminars/20070106zhangyanmei.pdf |
long_lat |
ENVELOPE(-61.250,-61.250,-62.633,-62.633) |
geographic |
Rugosa |
geographic_facet |
Rugosa |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
http://canli.dicp.ac.cn/Articles of Group Seminars/20070106zhangyanmei.pdf |
op_relation |
http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.625.6179 http://canli.dicp.ac.cn/Articles of Group Seminars/20070106zhangyanmei.pdf |
op_rights |
Metadata may be used without restrictions as long as the oai identifier remains attached to it. |
_version_ |
1766272752772186112 |