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Use of edible insects in thermal-induced protein gels containing porcine myofibrillar protein

  • T. K. Kim
  • , M. H. Lee
  • , J. Y. Cha
  • , J. Kim
  • , M. C. Kang
  • , H. I. Yong
  • , S. Jung
  • , Y. S. Choi

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)

Abstract

Edible insects are considered an environmentally friendly source of protein; however, products containing only edible insects are associated with poor quality and processing properties. Therefore, we examined and compared the thermal stability and rheological properties among thermal-induced myofibrillar protein gels prepared using porcine myofibril protein and five different edible insect species: larvae: Tenebrio molitor L., Protaetia brevitarsis, and Allomyrina dichotoma and adult insects: Gryllus bimaculatus and Oxyachinensis sinuosa. The myofibrillar protein gels containing edible insects had a higher pH than that of the control. The water-holding capacity of the myofibrillar gel containing G. bimaculatus (T4) was higher than that of the other samples. The hardness, cohesiveness, gumminess, and chewiness of the thermal-induced myofibrillar gel containing T4 were the highest. The myofibrillar gel containing edible insects had a higher peak temperature than that of the control, except for T4, as well as a similar or lower enthalpy, which is required for denaturation. All myofibrillar gels with/without edible insects exhibited Hershel-Bulkley fluid properties, and rigid structures were developed during heating. The myofibrillar protein gels containing T4 revealed excellent processing properties. Therefore, myofibrillar protein gels containing T4 may be used for producing protein-rich foods.

Original languageEnglish
Pages (from-to)803-811
Number of pages9
JournalJournal of Insects as Food and Feed
Volume8
Issue number7
DOIs
Publication statusPublished - 2022

Bibliographical note

Publisher Copyright:
© 2022. Wageningen Academic Publishers

Keywords

  • Edible insect
  • Myofibrillar protein
  • Rheological property
  • Thermal stability
  • Thermal-induced gel

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