Proteomic datasets of three

Over the past few decades, black soldier fly (BSF) larvae have emerged as a promising alternative protein source for animal feed. In addition to providing essential amino acids that support animal performance, BSF larvae also contain certain bioactive components that may contribute to maintaining intestinal health of animals. However, it is assumed that depending on the process used to obtain these larvae, their composition in proteins and bioactive molecules may vary. In this context, we analyzed the proteomes of live BSF larvae (BSFL), dehydrated BSFL, and a protein concentrate prepared from the dehydrated BSFL (all from the same commercial source). The larvae samples were frozen, freeze-dried, and ground before protein extraction. Proteins from each form were solubilized using a high concentration of sodium chloride and subsequently analyzed by mass spectrometry. The resulting protein lists were compared to identify shared proteins, sample-specific proteoforms, and gene identifiers. Venn diagrams showed that the three samples shared 888 proteins. Notably, live larvae exhibited the highest protein complexity, with 814 unique proteins, compared to none in dehydrated larvae, and 36 in the protein concentrate. The compilation of all the data enabled the identification of 2232 unique gene identifiers. Gene ontology analysis using EnsemblMetazoa database revealed numerous proteins associated with metabolism (amino acids, lipids, carbohydrates), while 57 proteins were assigned to innate defense and detoxification processes. Approximately 30 antimicrobial proteins/peptides were identified (peptidoglycan-binding proteins, lysozymes, cecropins, defensins, and attacin-like peptides). These data highlight that BSF larvae are a natural source of potential bioactive compounds, including antimicrobial proteins and peptides.