Study on Functional, Structural, Thermal properties of Insect protein source extracted from black soldier fly pre-pupae (Hermetia illucens)

Edible insect’s specifically black soldier fly is hailed as a naturally profitable source of alternative protein source that can be used to replace existing food and feed sources. The functional, thermal, crystallinity and structural properties of black soldier fly prepupae (BSFP) protein were investigated in this study. The protein content in BSFP flour before and after defatting was found to be increased from 37.7% to 46.97%. The functional properties of BSFP protein such as WAC (75.53%), OBC (83.78%), FC (112.78%), and EC (46.32%) shows a huge viability to use as a functional ingredient in food sectors. The endothermic peak at 170℃ in DSC reveals the high thermal stability of modified BSFP protein due to strong pH shift (Iso-electric) method. The electrostatic modification and hydrophobic interaction triggers the modified protein with enhanced physical, functional, thermal properties. The morphology of the BSFP flour sample in SEM was found to be agglomerated together due to high temperature prevailed during defatting process. The smooth globules structure depicts the protein embedded on the surface with porous structure due to freeze drying. The XRD image with 2 peaks at 2θ = 8.28° and 2θ = 19.44° depicts the BSFP protein is in crystallinity structure and the particle size was found to be 8.3434 nm. The insect protein from black soldier fly prepupae was found to have better functional and thermal properties which paved path as a commercial functional ingredient and novel protein alternate in food industry.