Traditional discovery of bioactive peptides usually involves bioactivity experiments, but an estimate can be proposed through the application of bioinformatics tools. The detection of bioactive peptides comprises several experimental steps including in vitro screening for the targeted bioactivity. However, the development of bioinformatics has led to an accumulation of systematic biological data which might result in reliable predictions of the bioactivity displayed by peptides of known sequence. The present work aimed to evaluate the different bioactivities of peptides obtained through the hydrolysis of soy protein concentrate by the LC-MS identification of the peptide sequences and their comparison to available information in bioactive peptides databases. For this purpose, commercial soy protein concentrate was hydrolyzed with papain, the hydrolyzate was ultra filtrated through a 3 kDa membrane and the filtrate was subjected to analysis in a nanoUPLC-RPxRP SYNAPT G2-S HDMS instrument. The spectra were analyzed through different approaches: applying comparison to the “soybean” databank from UNIPROT, the PatternLab platform identified 3 peptides and the Peaks software 1 (FDR 2%, Delta Mass of 5 ppm; Min Pri Score of 2.50). Applying the de novo sequencing methodology (Peaks software) other 6 peptides were identified (% Confidence > 70; error < 20 ppm). The peptide sequences identified were matched against the following peptide databases: APD; Pepbank and SDAP. All 10 sequences were found similar to existing antimicrobial peptides with similarity ranging from 34.6% to 50%. Higher similarity was displayed by the sequence VVPPA with the antibacterial and antifungal Fusaricidin B. All sequences were found to be present in allergenic proteins, with PD index values ranging from 0.00 to 9.99, which was expected since soy proteins are regarded as allergenic. None of the peptide sequences showed similarity to antioxidant peptides in the researched databanks. The in silico evaluation indicated that soy hydrolizate may present antimicrobial activity.