CaLB Catalyzed Conversion of ε-Caprolactone in Aqueous Medium. Part 1: Immobilization of CaLB to Microgels
The enzymatic ring-opening polymerization of lactones is a method of increasing interest for the synthesis of biodegradable and biocompatible polymers. In the past it was shown that immobilization of Candida antarctica lipase B (CaLB) and the reaction medium play an important role in the polymerizat...
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fttibhannoverren:oai:oa.tib.eu:123456789/8644 2024-09-15T17:42:17+00:00 CaLB Catalyzed Conversion of ε-Caprolactone in Aqueous Medium. Part 1: Immobilization of CaLB to Microgels Engel, Stefan Höck, Heidi Bocola, Marco Keul, Helmut Schwaneberg, Ulrich Möller, Martin 2016 application/pdf https://oa.tib.eu/renate/handle/123456789/8644 https://doi.org/10.34657/7682 eng eng Basel : MDPI ESSN:2073-4360 DOI:https://doi.org/10.3390/polym8100372 https://oa.tib.eu/renate/handle/123456789/8644 https://doi.org/10.34657/7682 CC BY 4.0 Unported https://creativecommons.org/licenses/by/4.0/ frei zugänglich ddc:540 Candida antarctica lipase B enzyme immobilization Microgel Novozym® 435 Polyesterification ε-Caprolactone status-type:publishedVersion doc-type:Article doc-type:Text 2016 fttibhannoverren https://doi.org/10.34657/768210.3390/polym8100372 2024-07-03T23:33:53Z The enzymatic ring-opening polymerization of lactones is a method of increasing interest for the synthesis of biodegradable and biocompatible polymers. In the past it was shown that immobilization of Candida antarctica lipase B (CaLB) and the reaction medium play an important role in the polymerization ability especially of medium ring size lactones like ε-caprolactone (ε-CL). We investigated a route for the preparation of compartmentalized microgels based on poly(glycidol) in which CaLB was immobilized to increase its esterification ability. To find the ideal environment for CaLB, we investigated the acceptable water concentration and the accessibility for the monomer in model polymerizations in toluene and analyzed the obtained oligomers/polymers by NMR and SEC. We observed a sufficient accessibility for ε-CL to a toluene like hydrophobic phase imitating a hydrophobic microgel. Comparing free CaLB and Novozym® 435 we found that not the monomer concentration but rather the solubility of the enzyme, as well as the water concentration, strongly influences the equilibrium of esterification and hydrolysis. On the basis of these investigations, microgels of different polarity were prepared and successfully loaded with CaLB by physical entrapment. By comparison of immobilized and free CaLB, we demonstrated an effect of the hydrophobicity of the microenvironment of CaLB on its enzymatic activity. Article in Journal/Newspaper Antarc* Antarctica Renate - Repositorium für Naturwissenschaften und Technik (TIB Hannover) |
institution |
Open Polar |
collection |
Renate - Repositorium für Naturwissenschaften und Technik (TIB Hannover) |
op_collection_id |
fttibhannoverren |
language |
English |
topic |
ddc:540 Candida antarctica lipase B enzyme immobilization Microgel Novozym® 435 Polyesterification ε-Caprolactone |
spellingShingle |
ddc:540 Candida antarctica lipase B enzyme immobilization Microgel Novozym® 435 Polyesterification ε-Caprolactone Engel, Stefan Höck, Heidi Bocola, Marco Keul, Helmut Schwaneberg, Ulrich Möller, Martin CaLB Catalyzed Conversion of ε-Caprolactone in Aqueous Medium. Part 1: Immobilization of CaLB to Microgels |
topic_facet |
ddc:540 Candida antarctica lipase B enzyme immobilization Microgel Novozym® 435 Polyesterification ε-Caprolactone |
description |
The enzymatic ring-opening polymerization of lactones is a method of increasing interest for the synthesis of biodegradable and biocompatible polymers. In the past it was shown that immobilization of Candida antarctica lipase B (CaLB) and the reaction medium play an important role in the polymerization ability especially of medium ring size lactones like ε-caprolactone (ε-CL). We investigated a route for the preparation of compartmentalized microgels based on poly(glycidol) in which CaLB was immobilized to increase its esterification ability. To find the ideal environment for CaLB, we investigated the acceptable water concentration and the accessibility for the monomer in model polymerizations in toluene and analyzed the obtained oligomers/polymers by NMR and SEC. We observed a sufficient accessibility for ε-CL to a toluene like hydrophobic phase imitating a hydrophobic microgel. Comparing free CaLB and Novozym® 435 we found that not the monomer concentration but rather the solubility of the enzyme, as well as the water concentration, strongly influences the equilibrium of esterification and hydrolysis. On the basis of these investigations, microgels of different polarity were prepared and successfully loaded with CaLB by physical entrapment. By comparison of immobilized and free CaLB, we demonstrated an effect of the hydrophobicity of the microenvironment of CaLB on its enzymatic activity. |
format |
Article in Journal/Newspaper |
author |
Engel, Stefan Höck, Heidi Bocola, Marco Keul, Helmut Schwaneberg, Ulrich Möller, Martin |
author_facet |
Engel, Stefan Höck, Heidi Bocola, Marco Keul, Helmut Schwaneberg, Ulrich Möller, Martin |
author_sort |
Engel, Stefan |
title |
CaLB Catalyzed Conversion of ε-Caprolactone in Aqueous Medium. Part 1: Immobilization of CaLB to Microgels |
title_short |
CaLB Catalyzed Conversion of ε-Caprolactone in Aqueous Medium. Part 1: Immobilization of CaLB to Microgels |
title_full |
CaLB Catalyzed Conversion of ε-Caprolactone in Aqueous Medium. Part 1: Immobilization of CaLB to Microgels |
title_fullStr |
CaLB Catalyzed Conversion of ε-Caprolactone in Aqueous Medium. Part 1: Immobilization of CaLB to Microgels |
title_full_unstemmed |
CaLB Catalyzed Conversion of ε-Caprolactone in Aqueous Medium. Part 1: Immobilization of CaLB to Microgels |
title_sort |
calb catalyzed conversion of ε-caprolactone in aqueous medium. part 1: immobilization of calb to microgels |
publisher |
Basel : MDPI |
publishDate |
2016 |
url |
https://oa.tib.eu/renate/handle/123456789/8644 https://doi.org/10.34657/7682 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
ESSN:2073-4360 DOI:https://doi.org/10.3390/polym8100372 https://oa.tib.eu/renate/handle/123456789/8644 https://doi.org/10.34657/7682 |
op_rights |
CC BY 4.0 Unported https://creativecommons.org/licenses/by/4.0/ frei zugänglich |
op_doi |
https://doi.org/10.34657/768210.3390/polym8100372 |
_version_ |
1810488799335022592 |