Monitoring the heat stress response of Escherichia coli via NiO nanoparticle assisted MALDI–TOF mass spectrometry

The heat stress response of Escherichia coli at various temperatures has been investigated using NiO nanoparticles assisted MALDI–TOF-MS. Significant numbers of protein peaks were obtained in the presence of NiO NPs when the samples were incubated at various temperatures in comparison with the control E. coli suspension (107 cfu/mL). The 10 kDa chaperonin (groES) is the principal protein operating both for the protection of proteins from denaturation and in the assembly of newly synthesized proteins. During the heat stress response with NiO NPs, 10 kDa chaperonin (grosES) proteins were detected using MALDI–TOF MS. The viability of E. coli was checked on LB agar plates at different temperatures and time treatments. In the presence of NiO NPs, viability decreases drastically; this has been explored and correlated with the MALDI–TOF MS results. Further, surface morphological changes of E. coli at different temperatures were investigated with NiO NPs by transmission electron microscopy (TEM). The response of heat stress toward E. coli for generating more stable protein ions can be applied for bacterial detection under high temperature conditions from biological, clinical and environmental samples.

► This study investigates and explores the heat stable proteins of E. coli by MALDI-TOF MS.
► Heat stress applied on E. coli with NiO NPs is checked by MALDI-TOF MS.
► 10 kDa chaperonin proteins have been observed by MALDI–TOF MS in the presence of NiO NPs.
► NiO NPs and E. coli interaction mechanism are explored in the heat stress system.