Catalytic capsids: the art of confinement
In the cell, enzymes are almost always spatially confined in crowded and tightly controlled cellular compartments. The entrapment of enzymes in artificial nanoreactors as biomimetic systems can be expected to contribute to the understanding of the activity and the interactions of enzymes in confined...
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Royal Society of Chemistry
2011
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ftunivqespace:oai:espace.library.uq.edu.au:UQ:596707 2023-05-15T13:51:28+02:00 Catalytic capsids: the art of confinement Minten, Inge J. Claessen, Victor I. Blank, Kerstin Rowan, Alan E. Nolte, Roeland J. M. Cornelissen, Jeroen J. L. M. 2011-02-01 https://espace.library.uq.edu.au/view/UQ:596707 eng eng Royal Society of Chemistry doi:10.1039/c0sc00407c issn:2041-6520 issn:2041-6539 orcid:0000-0003-0728-3851 Chemistry Multidisciplinary 1600 Chemistry Journal Article 2011 ftunivqespace https://doi.org/10.1039/c0sc00407c 2020-12-29T00:25:58Z In the cell, enzymes are almost always spatially confined in crowded and tightly controlled cellular compartments. The entrapment of enzymes in artificial nanoreactors as biomimetic systems can be expected to contribute to the understanding of the activity and the interactions of enzymes in confined spaces. The capsid of the Cowpea Chlorotic Mottle virus (CCMV) represents such an artificial nanoreactor that can be used to encapsulate multiple proteins in its interior. Employing a controlled encapsulation process we are able to load a precise number of proteins (Pseudozyma antarctica lipase B and EGFP) into the CCMV capsid and to study their activity. In the case of the enzyme, our results indicate that the apparent overall reaction rate increases upon encapsulation and is almost independent of the number of enzymes in the capsid. These observation are the result of the extremely high confinement molarity of the enzyme inside the capsid (Mconf-~1 mM) leading to very rapid formation of the enzyme-substrate complex. These results highlight the importance of small volumes for efficient multi-enzyme cascade catalysis. Article in Journal/Newspaper Antarc* Antarctica The University of Queensland: UQ eSpace Chem. Sci. 2 2 358 362 |
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Open Polar |
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The University of Queensland: UQ eSpace |
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ftunivqespace |
language |
English |
topic |
Chemistry Multidisciplinary 1600 Chemistry |
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Chemistry Multidisciplinary 1600 Chemistry Minten, Inge J. Claessen, Victor I. Blank, Kerstin Rowan, Alan E. Nolte, Roeland J. M. Cornelissen, Jeroen J. L. M. Catalytic capsids: the art of confinement |
topic_facet |
Chemistry Multidisciplinary 1600 Chemistry |
description |
In the cell, enzymes are almost always spatially confined in crowded and tightly controlled cellular compartments. The entrapment of enzymes in artificial nanoreactors as biomimetic systems can be expected to contribute to the understanding of the activity and the interactions of enzymes in confined spaces. The capsid of the Cowpea Chlorotic Mottle virus (CCMV) represents such an artificial nanoreactor that can be used to encapsulate multiple proteins in its interior. Employing a controlled encapsulation process we are able to load a precise number of proteins (Pseudozyma antarctica lipase B and EGFP) into the CCMV capsid and to study their activity. In the case of the enzyme, our results indicate that the apparent overall reaction rate increases upon encapsulation and is almost independent of the number of enzymes in the capsid. These observation are the result of the extremely high confinement molarity of the enzyme inside the capsid (Mconf-~1 mM) leading to very rapid formation of the enzyme-substrate complex. These results highlight the importance of small volumes for efficient multi-enzyme cascade catalysis. |
format |
Article in Journal/Newspaper |
author |
Minten, Inge J. Claessen, Victor I. Blank, Kerstin Rowan, Alan E. Nolte, Roeland J. M. Cornelissen, Jeroen J. L. M. |
author_facet |
Minten, Inge J. Claessen, Victor I. Blank, Kerstin Rowan, Alan E. Nolte, Roeland J. M. Cornelissen, Jeroen J. L. M. |
author_sort |
Minten, Inge J. |
title |
Catalytic capsids: the art of confinement |
title_short |
Catalytic capsids: the art of confinement |
title_full |
Catalytic capsids: the art of confinement |
title_fullStr |
Catalytic capsids: the art of confinement |
title_full_unstemmed |
Catalytic capsids: the art of confinement |
title_sort |
catalytic capsids: the art of confinement |
publisher |
Royal Society of Chemistry |
publishDate |
2011 |
url |
https://espace.library.uq.edu.au/view/UQ:596707 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
doi:10.1039/c0sc00407c issn:2041-6520 issn:2041-6539 orcid:0000-0003-0728-3851 |
op_doi |
https://doi.org/10.1039/c0sc00407c |
container_title |
Chem. Sci. |
container_volume |
2 |
container_issue |
2 |
container_start_page |
358 |
op_container_end_page |
362 |
_version_ |
1766255350034464768 |