Heat Stability of Virulence-Associated Enzymes from Listeria monocytogenes SLCC 5764
Authors: Zemser, Rachel B.; Martin, Scott E.
Source: Journal of Food Protection®, Number 7, July 1998, 785-923 , pp. 899-902(4)
Abstract:The enzyme activities of listeriolysin O (LLO), phosphatidylinositol-specific phospholipase C (PI-PLC), catalase (CA), and superoxide dismutase (SOD) from Listeria monocytogenes SLCC 5764 were examined after heat treatment, growth at elevated temperatures, and anaerobic growth. Growth at elevated temperatures may influence virulence as expressed by virulence enzyme activity. The enzymes were heated for 0 and 10 min at temperatures ranging from 40 to 100°C. The production of LLO was examined when the bacterium was grown at elevated temperatures, and the production of LLO, CA, and SOD were examined after anaerobic growth. LLO was the most heat-labile factor, losing almost all activity when heated above 50°C. CA was more heat stable, showing no decrease in activity until it was heated at 55°C. The PI-PLC enzyme was most heat resistant: the activity decreased between 40 and 50°C and continued to decrease when heated between 65 and 100°C. When L. monocytogenes was grown at elevated temperatures, it produced less LLO than when grown at the optimum growth temperature of 37°C. When the organism was grown under anaerobic conditions, the levels of CA and LLO decreased, while the SOD level remained unchanged.
Document Type: Research Article
Affiliations: University of Illinois, Department of Food Science and Human Nutrition, 486 Animal Sciences Laboratory, 1207 West Gregory Drive, Urbana, Illinois 61801, USA
Publication date: July 1998
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