
Research Square (Research Square), Journal Year: 2024, Volume and Issue: unknown
Published: June 26, 2024
Language: Английский
Research Square (Research Square), Journal Year: 2024, Volume and Issue: unknown
Published: June 26, 2024
Language: Английский
Advances in Colloid and Interface Science, Journal Year: 2025, Volume and Issue: unknown, P. 103494 - 103494
Published: March 1, 2025
Language: Английский
Citations
0International Journal of Biological Macromolecules, Journal Year: 2025, Volume and Issue: unknown, P. 142614 - 142614
Published: March 1, 2025
Language: Английский
Citations
0Innovative Food Science & Emerging Technologies, Journal Year: 2025, Volume and Issue: 102, P. 104018 - 104018
Published: April 8, 2025
Language: Английский
Citations
0International Journal of Biological Macromolecules, Journal Year: 2025, Volume and Issue: unknown, P. 143321 - 143321
Published: April 1, 2025
Language: Английский
Citations
0Food Chemistry X, Journal Year: 2025, Volume and Issue: 27, P. 102508 - 102508
Published: April 1, 2025
Language: Английский
Citations
0Foods, Journal Year: 2025, Volume and Issue: 14(10), P. 1699 - 1699
Published: May 11, 2025
Reducing the allergenicity of food components through processing is attracting great attention in industry. This study investigated structure and complexes formed from peanut protein (PP) rice (RP) using pH-driven method. The properties PP–RP were morphological analysis, multi-spectroscopic characterization, IgE binding capacity vitro digestibility studies. Morphological analysis showed that lost their particulate structures after treatment. Spectroscopic treatment promoted structural changes, making them more susceptible to degradation. There also changes tertiary proteins following studies suggested reduced potential PP by altering its under gastrointestinal conditions. provides a promising approach for producing hypoallergenic ingredients use
Language: Английский
Citations
0Journal of the Science of Food and Agriculture, Journal Year: 2024, Volume and Issue: 104(11), P. 6778 - 6786
Published: April 3, 2024
This study explored the denaturation of 11S globulin, a protein known for its diverse functional properties in soy applications, at pH 3.0 and 10.0, followed by gradual return to 7.0 facilitate renaturation. It investigated structural changes during renaturation induced change pH, revealing stabilization mechanism globulin.
Language: Английский
Citations
3Food Chemistry, Journal Year: 2024, Volume and Issue: 460, P. 140578 - 140578
Published: July 24, 2024
Language: Английский
Citations
3Food and Bioprocess Technology, Journal Year: 2024, Volume and Issue: unknown
Published: Aug. 12, 2024
Abstract Nowadays , lupin seeds have emerged as a novel and valuable source of proteins representing sustainable alternative to current raw materials plant-based proteins, such soybean. In this regard, demonstrates superior adaptation the Mediterranean climate with improved tolerance water stress. However, its suitability for human consumption is limited due presence anti-nutritional anti-technological factors, including alkaloids, polyphenols, tannins, lipids, which can adverse nutritional consequences and/or impact on purity yield protein extraction. study, Lupinus luteus were germinated 1, 2, 3, 6 days effect germination factors flours derived isolates was analyzed. Additionally, changes techno-functional properties also studied. Results showed that prolonged decreased fat content whereas antioxidant activity, saponin, alkaloid increased. alkaloids completely removed during Furthermore, from exhibited higher oil absorption capacities, well foaming emulsifying capabilities in comparison non-germinated seeds. Nevertheless, periods associated diminished foam emulsion stability. Therefore, no longer than 3 should be recommended order minimize levels while enhancing isolate.
Language: Английский
Citations
3Food Hydrocolloids, Journal Year: 2024, Volume and Issue: 160, P. 110796 - 110796
Published: Nov. 2, 2024
Language: Английский
Citations
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