Identification of protein in black soldier fly larvae (Hermetia illucens) through trans-proteomic pipeline

Abstract

The global demand for protein has kept increasing in recent years. Black soldier fly (BSF) larvae have been studied for their bioconversion capabilities and optimization of medium culture; however, comprehensive knowledge of their genetic and proteomic profile remains limited. This study aimed to explore the proteomic profile of BSF larvae and evaluate different hydrolysis methods based on the amount of protein produced and the number of unique proteins identified. The BSF larvae were hydrolyzed with four different treatments: using trypsin incubated for 3, 5, and 7 hours and using papain incubated for 5 hours. The resulting hydrolysates were analyzed using liquid chromatography-tandem mass spectrometry (LC-MS/MS), followed by trans-proteomic pipeline (TPP) analysis. The hydrolysis method yielding the highest number of identified proteins was papain 5-hour papain incubation (150 proteins), followed by 7-hour trypsin (127 proteins), 3-hour trypsin (95 proteins), and 5-hour trypsin (68 proteins). Several proteins identified in the BSF larval hydrolysates with potential biomedical application include Nazo protein, autophagy-related protein 13, coronin, yellow protein, cytochrome P450, and collagen. Interestingly, despite yielding a lower total protein count, the recommended hydrolysis method to produce the highest number of proteins with biomedical potential was 3-hour trypsin incubation.