Novel insights into the coagulation mechanism induced by Dregea sinensis protease: rheological properties, molecular and microstructural changes
Year: 2025
Type: article
Abstract: The study aimed to investigate the novel curdled milk mechanism in terms of rheological properties, microstructural changes, and molecular interactions. The results showed that the texture and water-holding capacity (WHC) of the milk gel at the curd stage were improved compared to pre-curd and post-curd. There was a strong electrostatic interaction between protease and milk proteins, with the smallest particle size being 209.793 ± 2.31 nm and the highest zeta potential being -41.07 ± 0.65 mV. The elasticity (G') and viscosity (G") of the milk gel were increased and the gel network structure of the milk gel was uniform and dense. In addition, it was shown that the milk gel formed a stable crystalline structure (2θ=19.98°). Finally, the molecular structure changes confirmed that the formation of a stable, firm milk gel was driven by hydrogen bonding and hydrophobic interactions between D. sinensis protease and the active amino acid residues Gln21, Gln94, and Arg142 of casein. This study helps to elucidate the mechanism of milk gel formation and provides potential application value for the development of novel plant chymosin foods.
Source: LWT
Institutions: Yunnan Agricultural University, Hainan University
Language: English
Topic: Proteins in Food Systems
Subfield: Food Science
Domain: Life Sciences
SDG: Zero hunger
Open Access status: gold
Estimated APC paid: $3,240
Award: G7866301563
OpenAlex ID: W4409761773