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A Model of Anomalous Enzyme-Catalyzed Gel Degradation Kinetics

Chatterjee, Debarati and Cherayil, Binny J (2010) A Model of Anomalous Enzyme-Catalyzed Gel Degradation Kinetics. In: Journal of Physical Chemistry B, 114 (15). pp. 5190-5195.

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Official URL: http://pubs.acs.org/doi/abs/10.1021/jp100212r


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 t(c) 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](-1) or 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 t(c) on [E] is explained in terms of a reaction-diffusion equation that is formulated in terms of fractional rather than ordinary time derivatives.

Item Type: Journal Article
Publication: Journal of Physical Chemistry B
Publisher: American Chemical Society
Additional Information: Copyright of this article belongs to American Chemical Society.
Department/Centre: Division of Chemical Sciences > Inorganic & Physical Chemistry
Date Deposited: 09 Jun 2010 05:06
Last Modified: 09 Jun 2010 05:06
URI: http://eprints.iisc.ac.in/id/eprint/27249

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