Information on taste-active components of porcine meat was provided based on an in-silico analysis using tools available in the BIOPEP database. The role of proteins as crucial nonvolatile components of muscle tissue was defined to develop the sensory profile of meat products. Among them, myofibrillar proteins, particularly myosin-2, proved to be a good precursor for taste-active peptides and amino acids; bitter, umami, and sour compounds were the most numerous among them. The role of peptides in suppressing (sourness and sweetness) and enhancing (salty and umami) the taste was also highlighted, which was not observed for amino acids. Troponin T, fast skeletal muscle, was the only source of components suppressing the sour taste. Practical applications The properties of dry-cured meats may result from the presence of bioactive peptides released by protein hydrolysis during fermentation and aging. However, protein hydrolysates sometimes have a bitter taste, which is unwanted by consumers, thus it is necessary to look for a way to combine functionality with consumer acceptability of food products undergoing proteolytic changes, such as dry-cured meat products. So far, there is insufficient knowledge regarding the protein factors directly related to porcine raw meat influencing the taste that affects consumer acceptability, commercialization, and validation of functional peptide-rich products. This analysis is a thorough and useful data source on taste-active protein compounds in porcine meat that can be used to show what taste can be expected if this particular material is applied to produce some specific meat-derived product (e.g., dry-cured meat).