Issue 2, 2011

Catalytic capsids: the art of confinement

Abstract

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.

Graphical abstract: Catalytic capsids: the art of confinement

Supplementary files

Article information

Article type
Edge Article
Submitted
03 Aug 2010
Accepted
12 Oct 2010
First published
09 Nov 2010

Chem. Sci., 2011,2, 358-362

Catalytic capsids: the art of confinement

I. J. Minten, V. I. Claessen, K. Blank, A. E. Rowan, R. J. M. Nolte and J. J. L. M. Cornelissen, Chem. Sci., 2011, 2, 358 DOI: 10.1039/C0SC00407C

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements