Stability and activity of enzyme aggregates of Calb in supercritical CO2

The activity and stability of a cross-linked enzyme aggregate of Candida antarctica lipase B (CLEA-Calb) in supercrit. carbon dioxide (SC-CO2) have been studied. The model reaction used is the esterification of isoamyl alc. with acetic acid. The catalytic performance of CLEA-Calb is evaluated both i...

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Main Authors: Dijkstra, ZJ Zwannet, Merchant, RZ, Keurentjes, JTF Jos
Format: Article in Journal/Newspaper
Language:English
Published: 2007
Subjects:
Antarc*
Antarctica
Online Access:http://repository.tue.nl/640836
id ftuniveindhoven:oai:library.tue.nl:640836
record_format openpolar
spelling ftuniveindhoven:oai:library.tue.nl:640836 2023-05-15T13:56:31+02:00 Stability and activity of enzyme aggregates of Calb in supercritical CO2 Dijkstra, ZJ Zwannet Merchant, RZ Keurentjes, JTF Jos 2007 application/pdf http://repository.tue.nl/640836 en eng Copyright (c) Dijkstra, ZJ Zwannet Copyright (c) Merchant, RZ Copyright (c) Keurentjes, JTF Jos ISSN:0896-8446 Article / Letter to the editor 2007 ftuniveindhoven 2018-12-26T13:34:47Z The activity and stability of a cross-linked enzyme aggregate of Candida antarctica lipase B (CLEA-Calb) in supercrit. carbon dioxide (SC-CO2) have been studied. The model reaction used is the esterification of isoamyl alc. with acetic acid. The catalytic performance of CLEA-Calb is evaluated both in batch and in continuous expts., with a focus on the effect of water prodn. upon reaction. The results of the batch expts. show a decreasing initial activity of the CLEA-Calb with an increase in pressure. Moreover, CLEAs appear to be highly stable in supercrit. carbon dioxide and also remain active during continuous reactions. Suggestions for improved process designs are given for which the optimal design depends on the specific reaction requirements. Article in Journal/Newspaper Antarc* Antarctica Eindhoven University of Technology (TU/e): Research Portal
institution Open Polar
collection Eindhoven University of Technology (TU/e): Research Portal
op_collection_id ftuniveindhoven
language English
description The activity and stability of a cross-linked enzyme aggregate of Candida antarctica lipase B (CLEA-Calb) in supercrit. carbon dioxide (SC-CO2) have been studied. The model reaction used is the esterification of isoamyl alc. with acetic acid. The catalytic performance of CLEA-Calb is evaluated both in batch and in continuous expts., with a focus on the effect of water prodn. upon reaction. The results of the batch expts. show a decreasing initial activity of the CLEA-Calb with an increase in pressure. Moreover, CLEAs appear to be highly stable in supercrit. carbon dioxide and also remain active during continuous reactions. Suggestions for improved process designs are given for which the optimal design depends on the specific reaction requirements.
format Article in Journal/Newspaper
author Dijkstra, ZJ Zwannet
Merchant, RZ
Keurentjes, JTF Jos
spellingShingle Dijkstra, ZJ Zwannet
Merchant, RZ
Keurentjes, JTF Jos
Stability and activity of enzyme aggregates of Calb in supercritical CO2
author_facet Dijkstra, ZJ Zwannet
Merchant, RZ
Keurentjes, JTF Jos
author_sort Dijkstra, ZJ Zwannet
title Stability and activity of enzyme aggregates of Calb in supercritical CO2
title_short Stability and activity of enzyme aggregates of Calb in supercritical CO2
title_full Stability and activity of enzyme aggregates of Calb in supercritical CO2
title_fullStr Stability and activity of enzyme aggregates of Calb in supercritical CO2
title_full_unstemmed Stability and activity of enzyme aggregates of Calb in supercritical CO2
title_sort stability and activity of enzyme aggregates of calb in supercritical co2
publishDate 2007
url http://repository.tue.nl/640836
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_source ISSN:0896-8446
op_rights Copyright (c) Dijkstra, ZJ Zwannet
Copyright (c) Merchant, RZ
Copyright (c) Keurentjes, JTF Jos
_version_ 1766264023527981056

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