ArticleFoods (Basel, Switzerland)2022
Effect of Hydrothermal Treatment on the Structure and Functional Properties of Quinoa Protein Isolate.
Article in Foods (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Preparation of Antioxidant Peptides Derived From Quinoa Protein and Evaluation of Their Antioxidant Activity Through a D-Galactose-Induced Aging Mice Model.Food science & nutrition · 2026Article
- Mild thermal unfolding of pea protein enhances curcumin binding and interfacial properties of the resulting complexes.Food chemistry: X · 2026Article
- Heat Treatment Modulates Structure, Functionality, and Digestion-Related Antioxidant Activity ofFoods (Basel, Switzerland) · 2026Article
- Enhancing the techno-functional properties of Quinoa protein isolate through cold plasma treatment: a comprehensive study on pH effects.Scientific reports · 2026Article
- Effects of pH and Temperature on the Structure and Function of Pea Albumin.Molecules (Basel, Switzerland) · 2026Article
- Effect of pH-Shifted Compound Heating Treatment on the Structure and Properties of Walnut Protein Isolate.Foods (Basel, Switzerland) · 2025Article
- Pre-Treatment Effects on Chemico-Physical Characteristics of Argan Press Cake Used for Bread Production.Foods (Basel, Switzerland) · 2025Article
- Studies on the Efficient Extraction of Ovotransferrin and the Effect of Heating Treatment on Its Structure and Activity.Foods (Basel, Switzerland) · 2025Article
- Optimization of ultrasound-assisted extraction of faba bean protein isolate: Structural, functional, and thermal properties. Part 2/2.Ultrasonics sonochemistry · 2024Article
- Modifying quinoa protein for enhanced functional properties and digestibility: A review.Current research in food science · 2023Review
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Authors and funding
6 authors.
Funding
Abstract
The aim of this study was to investigate the effects of hydrothermal treatment at different temperatures and times on the structure and functional properties of quinoa protein isolate (QPI). The structure of QPI was investigated by analyzing changes in the intrinsic fluorescence spectrum, ultra-violet (UV) spectrum, and Fourier transform infrared spectrum. The solubility, water/oil-holding capacity, emulsifying activity, and emulsion stability of QPI were studied, as were the particle size and the thermogravimetric properties of QPI. The results showed that the average particle size of QPI gradually increased with the increase in hydrothermal treatment time and temperature, and reached a maximum value of 121 °C for 30 min. The surface morphology also became rough and its thermal stability also increased. The endogenous fluorescence and UV spectral intensity at 280 nm decreased gradually with increasing hydrothermal treatment time and temperature, and reduced to the minimum values at 121 °C for 30 min, respectively. After hydrothermal treatment, the secondary structure of QPI tended to be disordered. The functional properties of QPI after treatment were all superior to those of the control. The results of this study might provide a basis for the processing and utilization of QPI.
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