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Unifying temperature effects on the growth rate of bacteria and the stability of globular proteins


Ratkowsky, DA and Olley, J and Ross, T, Unifying temperature effects on the growth rate of bacteria and the stability of globular proteins, Journal of Theoretical Biology, 233, (3) pp. 351-362. ISSN 0022-5193 (2005) [Refereed Article]

DOI: doi:10.1016/j.jtbi.2004.10.016


The specific growth rate constant for bacterial growth does not obey the Arrhenius-type kinetics displayed by simple chemical reactions. Instead, for bacteria, steep convex curves are observed on an Arrhenius plot at the low- and high-temperature ends of the biokinetic range, with a region towards the middle of the growth range loosely approximating linearity. This central region has been considered by microbiologists to be the "normal physiological range" for bacterial growth, a concept whose meaningfulness we now question. We employ a kinetic model incorporating thermodynamic terms for temperature-induced enzyme denaturation, central to which is a term to account for the large positive heat capacity change during unfolding of the proteins within the bacteria. It is now widely believed by biophysicists that denaturation of complex proteins and/or other macromolecules is due to hydrophobic hydration of non-polar compounds. Denaturation is seen as the process by which enthalpic and entropic forces becomes imbalanced both at high and at low temperatures resulting in conformational changes in the enzyme structure that expose hydrophobic amino acid groups to the surrounding water molecules. The "thermodynamic" rate model, incorporating the heat capacity change and its effect on the enthalpy and entropy of the system, fitted 35 sets of data for psychrophilic, psychrotrophic, mesophilic and thermophilic bacteria well, resulting in biologically meaningful estimates for the important thermodynamic parameters. As these results mirror those obtained by biophysicists for globular proteins, it appears that the same or a similar mechanism applies to bacteria as applies to proteins. © 2004 Elsevier Ltd. All rights reserved.

Item Details

Item Type:Refereed Article
Research Division:Physical Sciences
Research Group:Classical physics
Research Field:Thermodynamics and statistical physics
Objective Division:Expanding Knowledge
Objective Group:Expanding knowledge
Objective Field:Expanding knowledge in the environmental sciences
UTAS Author:Ratkowsky, DA (Dr David Ratkowsky)
UTAS Author:Olley, J (Professor June Olley)
UTAS Author:Ross, T (Professor Tom Ross)
ID Code:30104
Year Published:2005
Web of Science® Times Cited:112
Deposited By:Agricultural Science
Deposited On:2005-08-01
Last Modified:2006-05-04

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