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The thermodynamic stability of lipases and proteases from psychrotrophic bacteria

Owusu, RK, MAKHZOUM, A and KNAPP, J (1991) The thermodynamic stability of lipases and proteases from psychrotrophic bacteria. Food Chemistry, 39 (2). p. 187. [Journal article]

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URL: http://dx.doi.org/10.1016/0308-8146(91)90159-L

DOI: doi:10.1016/0308-8146(91)90159-L


The thermodynamic or conformational stability of psychrotroph lipases and proteases, measured as the Gibbs free energy difference (ΔG) between the native and denatured enzymes, were estimated from enzyme temperature-activity profile data. ΔG estimates of 8–10 kJ/mol and 16–17 kJ/mol were obtained for psychrotroph-derived lipases and proteases, respectively. Pseudomonas fluorescens strain AR-11 protease was unusually thermolabile (ΔG = 3·0–7·6 kJ/mol). These values were compared with values for some mesophilic and thermophilic enzymes and the possible relationship of ΔG to psychrotrophic enzyme heat-resistance is discussed.

Item Type:Journal article
Faculties and Schools:Faculty of Life and Health Sciences
Faculty of Life and Health Sciences > School of Biomedical Sciences
Research Institutes and Groups:Biomedical Sciences Research Institute
Biomedical Sciences Research Institute > Nutrition Innovation Centre for Food and Health (NICHE)
ID Code:16959
Deposited By: Dr Richard Owusu-Apenten
Deposited On:01 Feb 2011 13:26
Last Modified:01 Feb 2011 13:26

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