Among a series of crucial parameters, those for the selection and fragmentation are paramount as they can significantly enhance the number of proteins identified and quantified. Compared to traditional DDA setups, recent advances in DIA mode have shown increased sensitivity and broader protein coverage. Additionally, the recent introduction of a new generation of tandem mass spectrometers, specifically well adapted to address the complexity of metaproteomes, has significantly improved throughput and dynamic range . These instruments offer exceptional protein coverage, including of microbial effectors, and allow for deep characterization of dozens of samples or high-throughput monitoring of hundreds of samples in shorter time frames. Typically, 120,000 peptides can be identified and quantified within 30 minutes . Interestingly, within this landscape 12 proteins were associated with toxins and 14 with phages. In contrast, a smaller number of proteins were linked to virulence (1 protein) and antibiotic-related function (2 proteins). The dynamic range observed in this dataset enables the identification and characterization of microorganisms comprising as little as 0.1% of the total biomass. Further fractionation of the samples can increase the dynamic range of this massive peptidome, allowing researchers to detect proteins from even low abundant organisms.