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Deep eutectic system enhanced oat protein extraction.
J Food Sci
January 2025
Department of Chemistry, University of British Columbia, Vancouver, British Columbia, Canada.
Oats are a rich source of plant-based proteins owing to their nutritional value, diverse functions, and high abundance. However, traditional methods for extracting oat proteins (OPs), such as alkali solution acid precipitation (ASAP), can cause environmental pollution and potentially protein denaturation. In this work, we studied the use of deep eutectic solvents (DESs) and deep eutectic system (DESys)-based methods for OP extraction.
View Article and Find Full Text PDFSodiation of Enhanced Green Fluorescent Protein (EGFP) in Basic Solution Studied by Electrospray Mass Spectrometry.
J Mass Spectrom
January 2025
Graduate School of Medical Life Science, Yokohama City University, Yokohama, Kanagawa, Japan.
In our previous work, the sodiation of melittin, cytochrome c, and ubiquitin in a 1 mM NaOH water/methanol solution was studied by electrospray mass spectrometry. It was suggested that the α-helix is more resistant to sodiation than the β-sheet. In this study, sodiation of enhanced green fluorescent protein (EGFP) composed of a β-barrel was studied in 1% CHCOOH (AcOH) or 1 mM NaOH water/methanol solution by electrospray mass spectrometry.
View Article and Find Full Text PDFSupercritical fluid extrusion of pea flour and pea protein concentrate: Effects on functional and structural attributes.
J Food Sci
December 2024
Department of Food Science, Cornell University, Ithaca, New York, USA.
This research investigated the effectiveness of supercritical fluid extrusion (SCFX) to modify the functional and structural characteristics of pea protein concentrate (PPC) and pea flour (PF). The results indicate that the SCFX process favorably modified the hydration properties of PPC and PF needed for developments in the structural and textural qualities of the meat analogs and other similar products. The water-holding capacity of extruded PPC and PF improved significantly.
View Article and Find Full Text PDFpH-Dependent Conformational Plasticity of Monoclonal Antibodies at the SiO/Water Interface: Insights from Neutron Reflectivity and Molecular Dynamics.
ACS Appl Mater Interfaces
December 2024
Biological Physics Group, School of Physics and Astronomy, Faculty of Science and Engineering, The University of Manchester, Oxford Road, Manchester M13 9PL, United Kingdom.
Investigating the molecular conformations of monoclonal antibodies (mAbs) adsorbed at the solid/liquid interface is crucial for understanding mAb solution stability and advancing the development of mAb-based biosensors. This study examines the pH-dependent conformational plasticity of a human IgG1k mAb, COE-3, at the SiO/water interface under varying pH conditions (pH 5.5 and 9).
View Article and Find Full Text PDFUltrasonic assisted preparation of covalent bonding pea protein and polyphenol conjugate in emulsion delivery system.
Int J Biol Macromol
January 2025
State Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Key Laboratory of Animal Protein Deep Processing Technology of Zhejiang, School of Food and Pharmaceutical Sciences, Ningbo University, Ningbo, Zhejiang, China. Electronic address:
Article Synopsis
- Protein modification enhances the bioavailability of polyphenols, and polyphenols boost the functional properties of pea protein.
- Four polyphenols (gallic acid, ferulic acid, catechin, and kaempferol) were chemically bonded to pea protein using methods like ultrasonic grafting, and their interaction and structural changes were analyzed.
- The resulting conjugates displayed significantly improved antioxidant activity, thermal stability, and emulsifying properties compared to natural pea protein, making them promising for better polyphenol delivery in complex emulsions.
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