Protection by sucrose against heat-induced lethal and sublethal injury of Lactococcus lactis: An FT-IR study

Klaus V. Kilimann, Wolfgang Doster, Rudi F. Vogel, Christoph Hartmann, Michael G. Gänzle

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38 Scopus citations

Abstract

The heat inactivation of Lactococcus lactis was studied by determination of cell counts, and by FT-IR spectroscopy recording the average structure of cell proteins. Cell counts were measured after incubation milk buffer or milk buffer with 1. 5 M sucrose, and FT-IR spectra were recorded in 2H2O or 2H2O with 1. 5 M sucrose in the range of 6-75 °C. Sucrose protected L. lactis against heat inactivation. The cell counts differed by up to 6-log cycles after treatment in milk buffer as compared to milk buffer with sucrose. The 1H/2H exchange in proteins, and secondary structure elements were detected by the analysis of amide I′, amide II and amide II′ bands. A reduced 1H/2H exchange as well as a lower content of disordered structural elements was observed when sucrose was present. Conformational fluctuations of native proteins as indicated by the 1H/2H exchange were apparent already at sublethal temperatures. The loss of viability of L. lactis occurred in the same temperature range as the loss of the protein secondary structure. These results demonstrate that sucrose protects L. lactis against heat inactivation, and that the increased heat stability of proteins in the presence of sucrose contributed to this enhanced heat resistance.

Original languageEnglish
Pages (from-to)1188-1197
Number of pages10
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1764
Issue number7
DOIs
StatePublished - Jul 2006

Keywords

  • Bacterial inactivation
  • FT-IR spectroscopy
  • Heat resistance
  • Protein denaturation

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