Lipase activity enhancement by SC-CO2 treatment
The activity of lipases from porcine pancreas, Candida antartica recombinant from Aspergillus oryzae, Candida cylindracea (immobilized), Penicilium roqueforti, Aspergillus niger, Rhizopus arrhizus, Mucor miehei (two types of immobilization), and Pseudomonas cepacia (two types of immobilization) was...
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ftcyprusunivt:oai:ktisis.cut.ac.cy:20.500.14279/27523 2024-04-21T07:53:04+00:00 Lipase activity enhancement by SC-CO2 treatment Hlavsová, Klára Wimmer, Zdeněk Xanthakis, Epameinondas Bernášek, Prokop Sovová, Helena Zarevúcka, Marie 2008 pdf https://hdl.handle.net/20.500.14279/27523 https://doi.org/10.1515/znb-2008-0628 https://api.elsevier.com/content/abstract/scopus_id/46949104460 en eng Zeitschrift für Naturforschung B, 2008, vol. 63, no. 6, pp. 779-784 18657117 https://hdl.handle.net/20.500.14279/27523 doi:10.1515/znb-2008-0628 2-s2.0-46949104460 https://api.elsevier.com/content/abstract/scopus_id/46949104460 779 784 none Lipase activity Supercritical carbon dioxide Enantioselectivity Chemical Sciences Natural Sciences article 2008 ftcyprusunivt https://doi.org/20.500.14279/2752310.1515/znb-2008-0628 2024-03-27T01:20:00Z The activity of lipases from porcine pancreas, Candida antartica recombinant from Aspergillus oryzae, Candida cylindracea (immobilized), Penicilium roqueforti, Aspergillus niger, Rhizopus arrhizus, Mucor miehei (two types of immobilization), and Pseudomonas cepacia (two types of immobilization) was studied after using them as biocatalysts of blackcurrant oil hydrolysis under SC-CO2 conditions. The reaction was performed at 40°C and 15 MPa in a continuous-flow reactor. Increased relative activity of all used lipases after the hydrolytic reaction was observed. The most remarkable increase in the activity was noted for the lipase from Rhizopus arrhizus which was increased by more than 50 times. The highest activity was shown by Lipozyme®, lipase from Mucor miehei, immobilized on macroporous resin. Both treated and untreated Lipozyme® were used as biocatalysts in hydrolytic resolution of the racemic cis- or frani-isomers of 2-(4-methoxybenzyl) cyclIohexyl acetates. Satisfactory reaction yields (40 %) and excellent enantiomeric purity of the products (E = 472) were obtained when hydrolysis of the frans-isomer of 2-(4-methoxybenzyl)cyclohexyl acetate was catalyzed by Lipozyme® treated with SC-CO2. © 2008 Verlag der Zeitschrift für Naturforschung, Tübingen. Article in Journal/Newspaper antartic* Ktisis Cyprus University of Technology Zeitschrift für Naturforschung B 63 6 779 784 |
institution |
Open Polar |
collection |
Ktisis Cyprus University of Technology |
op_collection_id |
ftcyprusunivt |
language |
English |
topic |
Lipase activity Supercritical carbon dioxide Enantioselectivity Chemical Sciences Natural Sciences |
spellingShingle |
Lipase activity Supercritical carbon dioxide Enantioselectivity Chemical Sciences Natural Sciences Hlavsová, Klára Wimmer, Zdeněk Xanthakis, Epameinondas Bernášek, Prokop Sovová, Helena Zarevúcka, Marie Lipase activity enhancement by SC-CO2 treatment |
topic_facet |
Lipase activity Supercritical carbon dioxide Enantioselectivity Chemical Sciences Natural Sciences |
description |
The activity of lipases from porcine pancreas, Candida antartica recombinant from Aspergillus oryzae, Candida cylindracea (immobilized), Penicilium roqueforti, Aspergillus niger, Rhizopus arrhizus, Mucor miehei (two types of immobilization), and Pseudomonas cepacia (two types of immobilization) was studied after using them as biocatalysts of blackcurrant oil hydrolysis under SC-CO2 conditions. The reaction was performed at 40°C and 15 MPa in a continuous-flow reactor. Increased relative activity of all used lipases after the hydrolytic reaction was observed. The most remarkable increase in the activity was noted for the lipase from Rhizopus arrhizus which was increased by more than 50 times. The highest activity was shown by Lipozyme®, lipase from Mucor miehei, immobilized on macroporous resin. Both treated and untreated Lipozyme® were used as biocatalysts in hydrolytic resolution of the racemic cis- or frani-isomers of 2-(4-methoxybenzyl) cyclIohexyl acetates. Satisfactory reaction yields (40 %) and excellent enantiomeric purity of the products (E = 472) were obtained when hydrolysis of the frans-isomer of 2-(4-methoxybenzyl)cyclohexyl acetate was catalyzed by Lipozyme® treated with SC-CO2. © 2008 Verlag der Zeitschrift für Naturforschung, Tübingen. |
format |
Article in Journal/Newspaper |
author |
Hlavsová, Klára Wimmer, Zdeněk Xanthakis, Epameinondas Bernášek, Prokop Sovová, Helena Zarevúcka, Marie |
author_facet |
Hlavsová, Klára Wimmer, Zdeněk Xanthakis, Epameinondas Bernášek, Prokop Sovová, Helena Zarevúcka, Marie |
author_sort |
Hlavsová, Klára |
title |
Lipase activity enhancement by SC-CO2 treatment |
title_short |
Lipase activity enhancement by SC-CO2 treatment |
title_full |
Lipase activity enhancement by SC-CO2 treatment |
title_fullStr |
Lipase activity enhancement by SC-CO2 treatment |
title_full_unstemmed |
Lipase activity enhancement by SC-CO2 treatment |
title_sort |
lipase activity enhancement by sc-co2 treatment |
publishDate |
2008 |
url |
https://hdl.handle.net/20.500.14279/27523 https://doi.org/10.1515/znb-2008-0628 https://api.elsevier.com/content/abstract/scopus_id/46949104460 |
genre |
antartic* |
genre_facet |
antartic* |
op_relation |
Zeitschrift für Naturforschung B, 2008, vol. 63, no. 6, pp. 779-784 18657117 https://hdl.handle.net/20.500.14279/27523 doi:10.1515/znb-2008-0628 2-s2.0-46949104460 https://api.elsevier.com/content/abstract/scopus_id/46949104460 779 784 |
op_rights |
none |
op_doi |
https://doi.org/20.500.14279/2752310.1515/znb-2008-0628 |
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