Owusu, Richard and Doble, C (1994) Heat-stability of a proteinase from psychrotrophic Pseudomonas fluorescens P38, chymotrypsin and thermolysin. Food Chemistry, 51 (2). p. 137. [Journal article]
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The heat-stabilities of proteinases from a psychrotrophic Psuedomonas fluorescens strain P38 (P38 proteinase), chymotypsin, succinyl-chymotrypsin and thermolysin are compared on the basis of their respective thermoinactivation-rate constants and Arrhenius plots (40–145°C). The Arrhenius plots for P38 proteinase and succinyl-chymotrypsin showed an inversion at 80–90°C characteristic of enzymes showing low-temperature inactivation (LTI). Thermolysin showed a biphasic log k versus 1/T plot consistent with the two-state model for protein and enzyme denaturation. The results are discussed in terms of the kinetics of proteinase autolysis and possible physico-chemical features necessary for LTI.
|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 > Northern Ireland Centre for Food and Health (NICHE)
|Deposited By:||Dr Richard Owusu-Apenten|
|Deposited On:||01 Feb 2011 13:27|
|Last Modified:||01 Feb 2011 13:27|
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