Physico-chemical and colloidal properties of protein extracted from black soldier fly (Hermetia illucens) larvae

Int J Biol Macromol. 2021 Sep 1:186:714-723. doi: 10.1016/j.ijbiomac.2021.07.081. Epub 2021 Jul 16.

Abstract

The black soldier fly larvae (BSFL), Hermetia illucens (Linnaeus), has been largely utilized for animal feed. Due to its interesting composition, BSFL has great potential to be further implemented in the human diet. Herein we compared the flour and protein extract composition based on their moisture, ash, amino acids, mineral, and protein content. To have wide knowledge on protein profile and behavior, SDS-page electrophoresis, Fourier-transform infrared spectroscopy (FTIR) and differential scanning calorimetry (DSC) were used to give information about protein structure and thermal stability, respectively. The flour and protein extract contained respectively 37.3% and 61.1% of protein. DSC graph reported a glass transition temperature around 30 °C, recognizable by a shift in the curve, and an endothermic peak for solid melting at around 200 °C. FTIR analysis showed the main amide bands (A, B, I, II, III) for the flour and protein extract. The foam properties of BSFL protein extract were explored under different temperatures treatment, and the best foam stability was reached at 85 °C with 15 min of treatment. The data highlight the promising techno-functional properties of BSFL protein extract, and that the nutritional composition might be suitable for further use of BSFL as food fortification system.

Keywords: BSFL flour; Black soldier fly larvae; Foaming properties; Protein extraction and characterization.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Colloids
  • Diptera / embryology
  • Diptera / metabolism*
  • Edible Insects / embryology
  • Edible Insects / metabolism*
  • Food Handling
  • Food, Fortified
  • Hot Temperature
  • Insect Proteins / chemistry*
  • Insect Proteins / isolation & purification
  • Larva / metabolism
  • Nutritive Value
  • Protein Stability

Substances

  • Colloids
  • Insect Proteins