Subject area	Chemistry
More specific subject area	Proteomics, protein purification, protein precipitation, trichloroacetic acid
Type of data	Tables, Figures
How data was acquired	Raman (LabRAM HR800UV confocal microspectrometer, Horiba Jobin Yvon, Kyoto, Japan)
	Bradford assay (DC Protein Assay, Biorad)
	Electrophoresis (ImageJ software)
	UPLC-HRMS (Accela LC pumps, Q-Exactive Hybrid Quadrupole-Orbitrap mass spectrometer equipped of an ESI source, Thermo Fisher Scientific, Waltham, MA, USA)
	MASCOT search engine (Matrix Science, London, UK; version 2.6.0) and Skyline software (MacCoss Lab, Washington, US; version 3.7.0.10940)
	ProteomeXchange Consortium with identifier PXD008110
Data format	Raw, analyzed and processed data
Experimental factors
Experimental features	Proteins extraction was performed on 500 mg of soil, 10 mg of biofilm and 15 mg of mouse liver as starting material according to protocols of Chourey et al.[2], Huang et al.[3]and Song et al.[4]respectively.
	Proteins were precipitated with 25% (w/v) trichloroacetic acid (TCA).
	The washing of protein pellet was performed with three different agents (acetone, ethanol, or ethanol/HCl). The mixture was vortexed and kept at −20 °C for 1 h, centrifuged at 16,600 g for 15 min at 4 °C. The resulting pellets were dried in a SpeedVac concentrator, solubilized in a 50 mM of ammonium bicarbonate buffer containing 10 mM of Tris. Proteins were subjected to trypsin digestion for 24 h at 37 °C. Digestion was stopped with formic acid before gel, bradford and mass analysis.
Data source location	Poitiers, France
Data accessibility	data are with this article