Oct 2026· Food and Bioprocess Technology· Vol 19· 0 citations· 68 references
Abstract
This study investigated the effects of cold atmospheric plasma (CAP) treatment (2–10 min) on the structural properties and functional performance of pequi almond protein (PAP). Structural changes were evaluated through spectroscopic and chemical analyses, including free sulfhydryl and carbonyl contents, as well as secondary and tertiary structural modifications. Techno-functional properties related to solubility, emulsification, water- and oil-holding capacities, and rheological behavior were also assessed. Short CAP exposure (2–4 min) improved PAP functionality. Solubility increased up to ~ 2.6-fold, the emulsifying activity increased nearly sevenfold after 2 min, emulsifying stability improved by ~ 2.7-fold, and water- and oil-holding capacities increased by ~ 2.0-fold. These improvements were associated with conformational rearrangements at secondary and tertiary structural levels, evidenced by increased fluorescence intensity, UV–Vis absorbance, changes in FTIR profiles, and enhanced surface hydrophobicity (~ 2.31-fold), indicating partial protein unfolding and improved interfacial activity. FTIR analysis confirmed time-dependent rearrangements in the secondary structure of PAP, with β-sheet content increasing from 46.07% to 51.06%, while α-helix content remained relatively stable (22.19–21.97%) and β-turn content decreased from 26.53% to 22.64%. CAP treatment also altered the colloidal and rheological behavior of PAP dispersions. At prolonged exposure, apparent viscosity at 50 s−1 increased from 2.0 ± 0.2 to 9.6 ± 0.1 mPa·s, accompanied by increases in particle size, polydispersity index, and rheological parameters, suggesting protein aggregation and network formation. These effects were accompanied by increased carbonyl content and reduced free sulfhydryl groups, indicating oxidative modifications induced by prolonged plasma exposure. Overall, CAP represents a promising strategy for tailoring PAP functionality under the processing conditions evaluated. These findings highlight the importance of controlling plasma exposure time to balance structural modification, oxidative reactions, and functional performance, and provide a basis for further evaluating CAP-treated PAP in food-relevant formulations.
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
Sacha inchi (
Plukenetia volubilis
L.) press cake is a protein-rich agro-industrial by-product whose functional utilization is constrained by antinutritional factors and suboptimal techno-functional properties. To improve its performance as a protein ingredient, the effect of chemical modification under acidic, neu...
Ruby Aracely Narváez Cadena, D. Roa-Acosta, H. S. Villada et al.· Frontiers in Sustainable Foo...· 0 citations
Findings establish PBCP as a stable, seaweed-derived protein pigment for food applications by leveraging the oxidative reactivity differences of hydrogen peroxide to induced interactions between proteins and saccharides in the water-soluble protein.
Jong-Bong Lee, Min Jae Kim, Si Hwan Kim et al.· Food Chemistry: X· 0 citations
Emerging technologies have been widely applied to modify complex protein systems; however, their effects are generally evaluated at the whole-protein level, limiting the understanding of the mechanisms governing individual protein fractions. Soy protein functionality is primarily determined by the β-conglycinin (7S) an...
Philippe Defáveri Bieler, B. D. de Souza, Vitor Emanuel Máximo Santos et al.· Food Research International· 0 citations
Lipid peroxidation products can induce oxidative modification of myofibrillar proteins (MPs), thereby compromising their water-holding capacity (WHC), but the underlying molecular mechanism remains unclear. This study systematically investigated the mechanism of MDA-induced WHC deterioration in bovine myofibrillar prot...
He Li, Zhen-Yu Fang, Qin Wu et al.· Foods· 0 citations
The heat-induced aggregation behavior of coconut globulin at pH 2.0 and 85 °C was investigated over a continuous heating period of 0–24 h, with a focus on the temporal evolution of protein structure and corresponding changes in techno-functional performance. The aggregation process exhibited three distinct stages: init...