Aug 2026
BACKGROUND
The increasing demand for sustainable dietary proteins has driven interest in alternative plant-derived ingredients beyond soy protein. Although soy protein isolate (SPI) remains widely used, its supply is affected by trade dependence and price fluctuations. Cyperus esculentus protein (CEP), recovered from underutilized tiger nut by-products after oil extraction, may improve resource efficiency and support value-added utilization. However, its techno-functional properties and gut microbial fermentation behavior remain insufficiently characterized under direct comparison with SPI.
RESULTS
Compared with SPI, CEP showed favorable emulsifying and foaming properties, a relatively small median particle size (D50 = 40.32 μm), and good thermal stability. CEP also exhibited a balanced amino acid profile, with hydrophobic amino acids accounting for 31.68% ± 0.83% of total amino acids. During in vitro gut microbial fermentation, CEP enriched genera including Agathobacter, Bacteroides, and Butyricicoccus. After 24 h, acetate, propionate, and butyrate concentrations reached 13.00 ± 0.27, 11.95 ± 0.18, and 10.20 ± 0.47 mmol L-1, respectively, all significantly higher than those in the control group.
CONCLUSION
CEP combines competitive techno-functional performance, favorable amino acid composition, and promising fermentability, indicating its potential as a sustainable and value-added plant-protein ingredient. © 2026 Society of Chemical Industry.
Huifang Wang, Hui Liu, Yunchuan Bai et al.
· The Journal of the Science o... · 0 citations
Review
Open access
Aug 2026
BACKGROUND
Cottonseed is an important byproduct of cottonseed processing and is rich in proteins. A literature review indicated that cottonseed protein isolate (CPI) demonstrated a compact structure because of its limited exposure of hydrophobic groups, leading to poor emulsifying performance. This limited the functional performance and practical application of CPI in food systems. This study aimed to enhance CPI interfacial functionality through laccase-induced structural remodeling and to evaluate its performance in curcumin (Cur)-loaded emulsions.
RESULTS
This study designed a control group (0%) and laccase-treated groups (0.3%, 0.5%, and 0.8%, w/w). It was found that protein aggregation and network formation became more pronounced following laccase treatment and followed a dose-dependent pattern. Importantly, this investigation revealed that free sulfhydryl and free amino groups decreased, whereas random coil content, hydrophobic residue exposure, surface hydrophobicity, emulsifying activity, foaming capacity and oil-holding capacity increased, in which surface hydrophobicity increased by 61.09%, and emulsifying activity, foaming capacity, and oil-holding capacity increased by 30.55%, 57.24%, and 10.94%, respectively. Pearson correlation analysis showed that surface hydrophobicity was closely related to functional improvement. Compared with the control, 0.8% laccase-modified CPI produced smaller, more uniform Cur-loaded droplets. Encapsulation efficiency increased from 74.04% to 81.97%, and Cur bioaccessibility increased from 26.84% to 40.88%.
CONCLUSION
These findings indicated that laccase modification improved the functional properties and interfacial characteristics of CPI by altering its molecular conformation, thereby enhancing the encapsulation and bioaccessibility of Cur. This study provided a promising strategy for improving the delivery of hydrophobic bioactive compounds through enzymatic modified proteins. © 2026 Society of Chemical Industry.
Junhan Zhang, Wan-Lu Liu, Xinyu Guo et al.
· The Journal of the Science o... · 0 citations
