Jump to main content
Jump to site search

Issue 2, 2011
Previous Article Next Article

Catalytic capsids: the art of confinement

Author affiliations

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

Back to tab navigation

Supplementary files

Publication details

The article was received on 03 Aug 2010, accepted on 12 Oct 2010 and first published on 09 Nov 2010


Article type: Edge Article
DOI: 10.1039/C0SC00407C
Citation: Chem. Sci., 2011,2, 358-362
  •   Request permissions

    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

Search articles by author

Spotlight

Advertisements