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A model of anomalous enzyme-catalyzed gel degradation kinetics
, B.J. Cherayil
Published in American Chemical Society
2010
PMID: 20345155
Volume: 114
   
Issue: 15
Pages: 5190 - 5195
Abstract
We show that a model of target location involving n noninteracting particles moving subdiffusively along a line segment (a generalization of a model introduced by Sokolov et al. [Biophys. J. 2005, 89, 895.]) provides a basis for understanding recent experiments by Pelta et al. [Phys. Rev. Lett. 2007, 98, 228302.] on the kinetics of diffusion-limited gel degradation. These experiments find that the time tc taken by the enzyme thermolysin to completely hydrolyze a gel varies inversely as roughly the 3/2 power of the initial enzyme concentration [E]. In general, however, this time would be expected to vary either as [E]-1or as[E]-2, depending on whether the Brownian diffusion of the enzyme to the site of cleavage took place along the network chains (1-d diffusion) or through the pore spaces (3-d diffusion). In our model, the unusual dependence of tc on [E] is explained in terms of a reaction-diffusion equation that is formulated in terms of fractional rather than ordinary time derivatives. © 2010 American Chemical Society.
About the journal
JournalData powered by TypesetJournal of Physical Chemistry B
PublisherData powered by TypesetAmerican Chemical Society
ISSN15206106