This study investigated the non-covalent interactions between phloretin (PHL) and perilla seed protein isolate (PSPI) using multispectral analyses and computational simulations. Intrinsic and time-resolved fluorescence confirmed that PHL bound spontaneously to PSPI via static quenching with strong affinity (Kₐ = 2.0 × 1010 L/mol at 298 K) and 1:1 stoichiometry. FTIR and CD spectra revealed secondary structure rearrangement, with random coil content increasing from 37.30% to 40.14%. Molecular docking and molecular dynamics simulations corroborated that the PSPI binding was primarily governed by hydrogen bonds and van der Waals forces, which elicited modest conformational rearrangements. Functionally, this remodeling increased water solubility and antioxidant capacity (54.27 mg AAE/g protein). Particle size and zeta-potential analyses further supported the modulation of emulsifying behavior, characterized by decreased emulsifying activity and enhanced emulsion stability. These findings provide mechanistic insights into plant protein-polyphenol co-assembly for functional ingredient design.
The bioactivity of plant proteins is often limited by the compact and aggregated structures. In this study, the walnut protein-whey protein isolate (WP-WPIp) complex was constructed via pH cycling. This treatment appeared to induce conformational changes characterized by a disordering of secondary structures and a disr...
Jing-Jing Ma, Wei-Jun Wang, Yu-Meng Chen et al.· International Journal of Bio...· 0 citations
The molecular mechanisms governing interactions between casein (CS) and key yogurt aromas remain insufficiently elucidated. This study systematically investigated the interactions of CS with acetoin, diacetyl, and acetaldehyde through multispectroscopic techniques and integrated molecular simulations. Fluorescence quen...
Can Tang, Chang Yang, Hui Li et al.· International Journal of Bio...· 0 citations
High-pressure homogenization (HPH) was investigated as a strategy to modify sesame protein isolate (SMPI) combined with pH shifting. SMPI was adjusted to pH 2.0, 7.0, and 11.0 and processed at 50, 100, or 150 MPa (1 cycle, 25 °C). HPH induced pH-dependent structural rearrangements that affected the techno-functional pr...
B. Valente, I. A. de Moraes, D. Barbin et al.· Food Chemistry· 0 citations
Protein coacervates are aqueous colloidal compartments, and their formation and interfacial organization depend on electrostatic and non-electrostatic interactions. In this study, we investigated how truncation of the acidic domain affects the apparent coacervation behavior and cationic protein-induced morphological re...
Jaemin Han, Hyunsuk Choi, Y. Choi· Colloids and Surfaces B: Bio...· 0 citations
Regenerated silk fibroin (RSF) is a protein biomaterial whose molecular conformation, aggregation behavior, and functional properties are strongly influenced by processing conditions. The current study investigated the structural response of RSF to thermal treatment following incubation at 50–100 °C for 3 h. Intrinsic...
S. Basha, Darshan Chikkanayakanahalli Mukunda, A. K et al.· RSC Advances· 0 citations
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