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Heat-stability of a proteinase from psychrotrophic Pseudomonas fluorescens P38, chymotrypsin and thermolysin

Biomedical Sciences Research Institute Computer Science Research Institute Environmental Sciences Research Institute Nanotechnology & Advanced Materials Research Institute

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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URL: http://dx.doi.org/10.1016/0308-8146(94)90247-X

DOI: doi:10.1016/0308-8146(94)90247-X

Abstract

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)
ID Code:16900
Deposited By:Dr Richard Owusu-Apenten
Deposited On:01 Feb 2011 13:27
Last Modified:01 Feb 2011 13:27

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