Journal
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
Volume 1764, Issue 7, Pages 1188-1197Publisher
ELSEVIER
DOI: 10.1016/j.bbapap.2006.04.016
Keywords
FT-IR spectroscopy; bacterial inactivation; protein denaturation; heat resistance
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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 (H2O)-H-2 or (H2O)-H-2 with 1.5 M sucrose in the range of 6-75 degrees 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 H-1/H-2 exchange in proteins, and secondary structure elements were detected by the analysis of amide I', amide II and amide II' bands. A reduced (HH)-H-1-H-2 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 H-1/H-2 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. (c) 2006 Elsevier B.V. All rights reserved.
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