Details

Autor(en) / Beteiligte

• Ding, Yuxin
• Zhao, Lingling
• Liu, Yanqun
• Sun, Jingxin
• Pi, Yuzhen
• Shao, Jun-Hua

Titel

Effects of protein aggregation induced by NaCl and temperature on gelation of silkworm (Antheraea pernyi) pupa raw powder

Ist Teil von

• International journal of biological macromolecules, 2023-12, Vol.253, p.126679-126679, Article 126679

Ort / Verlag

Elsevier B.V

Erscheinungsjahr

2023

Quelle

Alma/SFX Local Collection

Beschreibungen/Notizen

• Edible insects have great potential for producing protein-rich ingredients. This study aimed to investigate the effects of protein aggregation induced by NaCl (0–1 M) and temperature (65–95 °C) on gelation of Antheraea pernyi (A. pernyi) pupa raw powder. No thermal aggregates were observed at low temperature (65 °C), on the basis of there being no significant enhancement in turbidity and particle size (P > 0.05), regardless of NaCl concentrations. At elevated temperatures (75–95 °C), protein solutions exhibited significantly higher turbidity and particle size (P < 0.05), accompanied by an initial rise in surface hydrophobicity followed by a decline, alongside declining sulfhydryl. This marks the beginning of massive thermal aggregation driven by molecular forces. In addition, covalent (disulfide bonds) and non-covalent (hydrogen bonding, electrostatic interactions, and hydrophobicity) forces were influenced by NaCl, leading to variability in the protein aggregation and gelation. Correlation analysis indicates that the higher protein aggregation induced by ions was beneficial to the construction of more compact three-dimensional structures, as well as to the rheology, texture, and water-holding capacity of A. pernyi pupa gels. However, excessive salt ions destroyed the gel structure. Our findings will aid the use of A. pernyi pupae as textural ingredients in formula foods. [Display omitted] •Thermal aggregation of A. pernyi pupa protein is regulated by temperature and NaCl.•Heat and NaCl change the interaction forces (covalent and non-covalent) of proteins.•A pupa gel with ideal properties is induced by higher protein thermal aggregation.•NaCl improves the texture, WHC and microstructure of the gel from pupa powder.•Gelation ability of pupa powder with NaCl is equal to some traditional gel agents.