Buffalo worm (Alphitobius diaperinus) proteins: Structural properties, proteomics and nutritional benefits
Zidan Ma, Martin Mondor, Adam Dowle, Francisco M. Goycoolea, Alan Javier Hernández‐Álvarez
Abstract
Biophysical methods such as circular dichroism (CD) and differential scanning calorimetry (DSC) have been minimally used to characterize insect-derived proteins. This study examines the insect Alphitobius diaperinus as a potential protein source. Techniques such as alkaline solubilization coupled to isoelectric precipitation and Osborne fractionation were used to obtain protein concentrates and fractions (albumins, globulins, prolamins, glutelins). SDS-PAGE results showed dominant protein bands at 78.3, 73.3, 49.3, 34.5, 32.0, and 10.3 kDa. All fractions had over 60 % α-helix and β-sheet structures, indicating stable conformations. Prolamins showed high surface hydrophobicity and thermal stability. Nutritionally, glutelins exhibited the highest concentration of essential amino acids (68.75 g/100 g protein), and demonstrated superior In vitro protein-digestibility (84.04 %) as well as the highest In vitro protein-digestibility corrected amino acid score (73.11 %). Therefore, this study characterized the structural-function relationship of A. diaperinus proteins and collectively assessed their suitability and safety for human consumption. • A. diaperinus Osborne fractions are mainly composed of α-helix, β-sheet and β-turn. • Glutelin-rich protein fraction showed the best protein quality parameters. • Osborne fractionation effectively removes arginine kinase allergen from protein extracts.