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Extra resources for Advances in High Pressure Bioscience and Biotechnology: Proceedings of the International Conference on High Pressure Bioscience and Biotechnology, Heidelberg, August 30 - September 3, 1998
Heat shock treatment of the parent strain resulted in transient induction of heat shock proteins, and enhanced its survival at moderate pressures (220 MPa). However, heat shock did not protect the parent strain from inactivation at higher pressures (500 MPa). Hence, overexpression of heat shock proteins seems not sufficient to explain the high level of pressure resistance in the mutants. 1 Introduction We previously reported the acqUlsloon of pressure resistance in E. coli by spontaneous mutation .
Therefore, overexpression of heat shock proteins seems not sufficient for the high level of pressure resistance in the mutants. It is relevant that pressure inactivation of the mutants was strongly enhanced in the presence of nisin or lysozyme. Combining pressure-processing with such antimicrobial peptides seems an appropriate means to increase the safety of pressure-treated foods. References [I] Hauben, K. et at. (1997); Escherichia coli mutants resistant to inactivation by high hydrostatic pressure; AppL Environ.
416, 1-5. Multiple Stress Resistance in Pressure Resistant Escherichia coli Mutants K. Hauben, T. Nystrom, A. Farewell and C. Michiels Laboratory of Food Microbiology, Katholieke Universiteit Leuven, Kard. be Abstract. The E. coli mutants LMMIOIO and LMM1030, which were previously isolated on the basis of their pressure resistance, are demonstrated here to show cross-resistance to acid, reactive oxygen and/or heat. Analysis of protein expression r,,:vealed derepression of common heat shock proteins in both mutants under non-stress conditions.