Compartmentalized cross-linked enzymatic nano-aggregates (c-CLEnA) for efficient in-flow biocatalysis
Nano-sized enzyme aggregates, which preserve their catalytic activity are of great interest for flow processes, as these catalytic species show minimal diffusional issues, and are still sizeable enough to be effectively separated from the formed product. The realization of such catalysts is however...
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ftpubmed:oai:pubmedcentral.nih.gov:8157641 2023-05-15T13:58:05+02:00 Compartmentalized cross-linked enzymatic nano-aggregates (c-CLEnA) for efficient in-flow biocatalysis De Martino, M. Teresa Tonin, Fabio Yewdall, N. Amy Abdelghani, Mona Williams, David S. Hanefeld, Ulf Rutjes, Floris P. J. T. Abdelmohsen, Loai K. E. A. van Hest, Jan C. M. 2020-02-07 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8157641/ https://doi.org/10.1039/c9sc05420k en eng The Royal Society of Chemistry http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8157641/ http://dx.doi.org/10.1039/c9sc05420k This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/ CC-BY-NC Chem Sci Chemistry Text 2020 ftpubmed https://doi.org/10.1039/c9sc05420k 2021-06-06T00:41:18Z Nano-sized enzyme aggregates, which preserve their catalytic activity are of great interest for flow processes, as these catalytic species show minimal diffusional issues, and are still sizeable enough to be effectively separated from the formed product. The realization of such catalysts is however far from trivial. The stable formation of a micro-to millimeter-sized enzyme aggregate is feasible via the formation of a cross-linked enzyme aggregate (CLEA); however, such a process leads to a rather broad size distribution, which is not always compatible with microflow conditions. Here, we present the design of a compartmentalized templated CLEA (c-CLEnA), inside the nano-cavity of bowl-shaped polymer vesicles, coined stomatocytes. Due to the enzyme preorganization and concentration in the cavity, cross-linking could be performed with substantially lower amount of cross-linking agents, which was highly beneficial for the residual enzyme activity. Our methodology is generally applicable, as demonstrated by using two different cross-linkers (glutaraldehyde and genipin). Moreover, c-CLEnA nanoreactors were designed with Candida antarctica Lipase B (CalB) and Porcine Liver Esterase (PLE), as well as a mixture of glucose oxidase (GOx) and horseradish peroxidase (HRP). Interestingly, when genipin was used as cross-linker, all enzymes preserved their initial activity. Furthermore, as proof of principle, we demonstrated the successful implementation of different c-CLEnAs in a flow reactor in which the c-CLEnA nanoreactors retained their full catalytic function even after ten runs. Such a c-CLEnA nanoreactor represents a significant step forward in the area of in-flow biocatalysis. Text Antarc* Antarctica PubMed Central (PMC) Chemical Science 11 10 2765 2769 |
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English |
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Chemistry |
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Chemistry De Martino, M. Teresa Tonin, Fabio Yewdall, N. Amy Abdelghani, Mona Williams, David S. Hanefeld, Ulf Rutjes, Floris P. J. T. Abdelmohsen, Loai K. E. A. van Hest, Jan C. M. Compartmentalized cross-linked enzymatic nano-aggregates (c-CLEnA) for efficient in-flow biocatalysis |
topic_facet |
Chemistry |
description |
Nano-sized enzyme aggregates, which preserve their catalytic activity are of great interest for flow processes, as these catalytic species show minimal diffusional issues, and are still sizeable enough to be effectively separated from the formed product. The realization of such catalysts is however far from trivial. The stable formation of a micro-to millimeter-sized enzyme aggregate is feasible via the formation of a cross-linked enzyme aggregate (CLEA); however, such a process leads to a rather broad size distribution, which is not always compatible with microflow conditions. Here, we present the design of a compartmentalized templated CLEA (c-CLEnA), inside the nano-cavity of bowl-shaped polymer vesicles, coined stomatocytes. Due to the enzyme preorganization and concentration in the cavity, cross-linking could be performed with substantially lower amount of cross-linking agents, which was highly beneficial for the residual enzyme activity. Our methodology is generally applicable, as demonstrated by using two different cross-linkers (glutaraldehyde and genipin). Moreover, c-CLEnA nanoreactors were designed with Candida antarctica Lipase B (CalB) and Porcine Liver Esterase (PLE), as well as a mixture of glucose oxidase (GOx) and horseradish peroxidase (HRP). Interestingly, when genipin was used as cross-linker, all enzymes preserved their initial activity. Furthermore, as proof of principle, we demonstrated the successful implementation of different c-CLEnAs in a flow reactor in which the c-CLEnA nanoreactors retained their full catalytic function even after ten runs. Such a c-CLEnA nanoreactor represents a significant step forward in the area of in-flow biocatalysis. |
format |
Text |
author |
De Martino, M. Teresa Tonin, Fabio Yewdall, N. Amy Abdelghani, Mona Williams, David S. Hanefeld, Ulf Rutjes, Floris P. J. T. Abdelmohsen, Loai K. E. A. van Hest, Jan C. M. |
author_facet |
De Martino, M. Teresa Tonin, Fabio Yewdall, N. Amy Abdelghani, Mona Williams, David S. Hanefeld, Ulf Rutjes, Floris P. J. T. Abdelmohsen, Loai K. E. A. van Hest, Jan C. M. |
author_sort |
De Martino, M. Teresa |
title |
Compartmentalized cross-linked enzymatic nano-aggregates (c-CLEnA) for efficient in-flow biocatalysis |
title_short |
Compartmentalized cross-linked enzymatic nano-aggregates (c-CLEnA) for efficient in-flow biocatalysis |
title_full |
Compartmentalized cross-linked enzymatic nano-aggregates (c-CLEnA) for efficient in-flow biocatalysis |
title_fullStr |
Compartmentalized cross-linked enzymatic nano-aggregates (c-CLEnA) for efficient in-flow biocatalysis |
title_full_unstemmed |
Compartmentalized cross-linked enzymatic nano-aggregates (c-CLEnA) for efficient in-flow biocatalysis |
title_sort |
compartmentalized cross-linked enzymatic nano-aggregates (c-clena) for efficient in-flow biocatalysis |
publisher |
The Royal Society of Chemistry |
publishDate |
2020 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8157641/ https://doi.org/10.1039/c9sc05420k |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Chem Sci |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8157641/ http://dx.doi.org/10.1039/c9sc05420k |
op_rights |
This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/ |
op_rightsnorm |
CC-BY-NC |
op_doi |
https://doi.org/10.1039/c9sc05420k |
container_title |
Chemical Science |
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11 |
container_issue |
10 |
container_start_page |
2765 |
op_container_end_page |
2769 |
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1766266104585388032 |