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Conformational, physiochemical, and functional properties of quinoa protein isolate influenced by thermal treatment

Chang, Jiaojiao, Zhao, Yong, Xu, Jingwen·2025·Journal of Food Science
DOI 10.1111/1750-3841.70051
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Abstract

This study investigated the effect of various thermal treatments, including atmospheric boiling (AB), high‐pressure boiling (HPB), and baking (B), on the conformational, physicochemical, and functional properties of quinoa protein isolate (QPI), as well as its in vitro digestibility. Thermal treatment resulted in QPI denaturation, unfolding, and more exposure of hydrophobic groups, which was reflected as the reduced content of α‐helix and increased contents of β‐sheet and β‐turn. The reduced content of free sulfhydryl (SH) groups and total SH groups in thermally treated QPI also indicated that thermal treatment promoted QPI denaturation and unfolding. The functionalities of QPI, such as solubility, oil‐holding capacity, emulsification index, emulsion stability, and gel strength, were improved by thermal treatment, wherein HPB‐QPI > AB‐QPI > B‐QPI > control QPI. Thermal treatment improved in vitro digestibility of QPI and the contents of essential amino acids and hydrophobic amino acids compared to those of control QPI. HPB‐QPI showed the highest digestibility in vitro up to 88.26%, and the highest content of essential amino acids and hydrophobic amino acids up to 497.17 mg/g and 344.45 mg/g, respectively. This study provided new insights into the conformational behaviors and functionalities of QPI through thermal processing for benefiting their applications in the food industry. Practical Application: Through thermal treatment, the functional properties of quinoa protein were significantly enhanced, leading to improvements in plant‐based beverages, emulsified foods, and baked goods, thereby expanding its range of applications in the food industry.

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  • These treatments also increase ζ-potential magnitude and hydrophobic exposure while maintaining recognizable globulin structures.

    “These treatments also increase ζ -potential magnitude and hydrophobic exposure while maintaining recognizable globulin struc­ tures”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Chang et al., 2025

    Section 3.2.5 reports that thermal treatment significantly increased surface hydrophobicity by exposing previously buried hydrophobic residues. The searched passages do not report an increase in ζ-potential magnitude. Section 3.4 identifies globulin subunits in QPI, but does not establish that the treatments maintained recognizable globulin structures; the Conclusion instead describes denaturation and unfolding. Page numbers were not available in our copy. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

  • Thermal and alkaline treatments tend to increase β-sheets, β-turns and decrease α-helix, consistent with enhanced β-aggregation and cross-linking.

    “Thermal and alkaline treatments tend to increase β -sheets, β -turns and decrease α -helix, consistent with enhanced β -aggregation and cross-linking”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Chang et al., 2025

    The Conclusion and §3.1.2 (FTIR analysis; page unavailable) support a heat-induced shift from α-helix toward β-sheet in quinoa protein isolate, but the FTIR results vary by treatment: atmospheric boiling decreased β-sheet, while baking increased α-helix. The paper studies thermal treatments, not alkaline treatment, and does not establish the claimed β-aggregation and cross-linking interpretation. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

  • Higher extraction pH, from 9 to 11, and thermal treatments tend to increase void-volume aggregates and β-associated aggregation.

    “Higher extraction pH, from 9 to 11, and thermal treatments tend to increase void-volume aggregates and β -associated aggregation.”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Chang et al., 2025

  • Across proteins, quinoa is generally the most adjustable because multiple modifications (pH-shift, homogenization, thermal pretreatment) can steer its aggregation without fully destroying interfacial mobility.

    “Across proteins, quinoa is generally the most adjustable because multiple modifications (pH-shift, homogenization, thermal pretreatment) can steer its aggregation without fully destroying inter­ facial mobility (Chang et al., 2025; Wang et al., 2025a).”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Chang et al., 2025

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Research works printed but not linked: 35

  1. Arise, A. K., Malomo, S. A., Ihuoma Cynthia, C., Aliyu, N. A., & Arise, R. O. (2022). Influence of processing methods on the antinutrients, morphology and in-vitro protein digestibility of jack bean. Food Chemistry Advances, 1, 100078. https://doi.org/10.1016/ j.focha.2022.100078 · DOI
  2. Bailey, H. M., Fanelli, N. S., & Stein, H. H. (2023). Effect of heat treatment on protein quality of rapeseed protein isolate compared with non-heated rapeseed isolate, soy and whey protein isolates, and rice and pea protein concentrates. Journal of the Science of Food and Agriculture, 103(14), 7251-7259. https://doi.org/10.1002/ jsfa.12809 · DOI
  3. Cao, H., Huang, Q., Shi, J., Guan, X., Song, H., Zhang, Y., Xie, J., & Fang, Y. (2023). Effect of conventional and microwave heating treatment on antioxidant activity of quinoa protein after simulated gastrointestinal digestion. Food Chemistry, 415, 135763. https://doi. org/10.1016/j.foodchem.2023.135763 · DOI
  4. Choe, U., Osorno, J. M., Ohm, J. B., Chen, B., & Rao, J. (2022). Modifi- cation of physicochemical, functional properties, and digestibility of macronutrients in common bean (Phaseolus vulgaris L.) flours by different thermally treated whole seeds. Food Chemistry, 382, 132570. https://doi.org/10.1016/j.foodchem.2022.132570 · DOI
  5. Cui, H., Li, S., Roy, D., Guo, Q., & Ye, A. (2023). Modifying quinoa pro- tein for enhanced functional properties and digestibility: A review. Current Research in Food Science, 7, 100604. https://doi.org/10. 1016/j.crfs.2023.100604 · DOI
  6. Deng, Y., Huang, L., Zhang, C., Xie, P., Cheng, J., Wang, X., & Li, S. (2019). Physicochemical and functional properties of Chinese quince seed protein isolate. Food Chemistry, 283, 539-548. https:// doi.org/10.1016/j.foodchem.2019.01.083 · DOI
  7. Dille, M. J., Knutsen, S. H., & Draget, K. I. (2022). Gels and gelled emulsions prepared by acid-induced gelation of mixtures of faba bean (Vicia faba) protein concentrate and λ-carrageenan. Applied Food Research, 2(2), 100174. https://doi.org/10.1016/j.afres.2022. 100174 · DOI
  8. Ge, J., Sun, C. X., Corke, H., Gui, K., Gan, R. Y., & Fang, Y. (2020). The health benefits, functional properties, modifications, and applications of pea (Pisum sativum L.) protein: Current status, challenges, and perspectives. Comprehensive Reviews in Food Sci- ence and Safety, 19(4), 1835-1876. https://doi.org/10.1111/1541-4337. 12573 · DOI · Paper page
  9. Guo, H., Hao, Y., Yang, X., Ren, G., & Richel, A. (2023). Exploration on bioactive properties of quinoa protein hydrolysate and peptides: A review. Critical Reviews in Food Science and Nutrition, 63(16), 2896-2909. https://doi.org/10.1080/10408398.2021.1982860 · DOI
  10. Hall, A. E., & Moraru, C. I. (2021). Structure and function of pea, lentil and faba bean proteins treated by high pressure processing and heat treatment. LWT-Food Science and Technology, 152, 112349. https://doi.org/10.1016/j.lwt.2021.112349 · DOI
  11. He, X., Wang, B., Zhao, B., Meng, Y., Chen, J., & Yang, F. (2022). Effect of hydrothermal treatment on the structure and functional prop- erties of quinoa protein isolate. Foods, 11(19), 2954. https://doi.org/ 10.3390/foods11192954 · DOI
  12. Hu, J., Yu, B., Yuan, C., Tao, H., Wu, Z., Dong, D., Lu, Y., Zhang, Z., Cao, Y., Zhao, H., Cheng, Y., & Cui, B. (2023). Influence of heat treatment before and/or after high-pressure homogenization on the structure and emulsification properties of soybean protein isolate. International Journal of Biological Macromolecules, 253, 127411. https://doi.org/10.1016/j.ijbiomac.2023.127411 · DOI
  13. Hu, S., Zhu, S., Luo, J., Ouyang, L., Feng, J., & Zhou, J. (2022). Effect of extrusion on physicochemical properties and antioxidant poten- tial of protein isolate derived from Baijiu vinasse. Food Chemistry, 384, 132527. https://doi.org/10.1016/j.foodchem.2022.132527 · DOI
  14. Huang, R., Pan, X., Lv, J., Zhong, W., Yan, F., Duan, F., & Jia, L. (2018). Effects of explosion puffing on the nutritional composition and digestibility of grains. International Journal of Food Properties, 21(1), 2193-2204. https://doi.org/10.1080/10942912.2018.1514634 · DOI
  15. Huang, K., Shi, J., Li, M., Sun, R., Guan, W., Cao, H., Guan, X., & Zhang, Y. (2022). Intervention of microwave irradiation on struc- ture and quality characteristics of quinoa protein aggregates. Food Hydrocolloids, 130, 107677. https://doi.org/10.1016/j.foodhyd.2022. 107677 · DOI
  16. Kaushik, P., Dowling, K., McKnight, S., Barrow, C. J., Wang, B., & Adhikari, B. (2016). Preparation, characterization and functional properties of flax seed protein isolate. Food Chemistry, 197, 212- 220. https://doi.org/10.1016/j.foodchem.2015.09.106 · DOI
  17. Li, C., Tian, Y., Liu, C., Dou, Z., & Diao, J. (2023). Effects of heat treatment on the structural and functional properties of Phaseo- lus vulgaris L. protein. Foods, 12(15), 2869. https://doi.org/10.3390/ foods12152869 · DOI
  18. Liu, Y., Li, X., Liu, J., Wei, L., Liu, Y., Lu, F., Wang, W., Li, Q., & Li, Y. (2022). Focusing on Hofmeister series: Composition, structure and functional properties of pea protein extracted with food-related anions. Food Hydrocolloids, 133, 107976. https://doi.org/10.1016/j. foodhyd.2022.107976 · DOI · Paper page
  19. Ma, J., Chen, H., Chen, W., Wu, J., Li, Z., Zhang, M., Zhong, Q., & Chen, W. (2022). Effects of heat treatment and pH on the physic- ochemical and emulsifying properties of coconut (Cocos nucifera L.) globulins. Food Chemistry, 388, 133031. https://doi.org/10.1016/ j.foodchem.2022.133031 · DOI
  20. Mesfin, N., Belay, A., & Amare, E. (2021). Effect of germination, roasting, and variety on physicochemical, techno-functional, and antioxidant properties of chickpea (Cicer arietinum L.) protein isolate powder. Heliyon, 7(9), e08081. https://doi.org/10.1016/j. heliyon.2021.e08081 · DOI
  21. Mir, N. A., Riar, C. S., & Singh, S. (2020). Structural modification in album (Chenopodium album) protein isolates due to controlled thermal modification and its relationship with protein digestibil- ity and functionality. Food Hydrocolloids, 103, 105708. https://doi. org/10.1016/j.foodhyd.2020.105708 · DOI
  22. Mir, N. A., Riar, C. S., & Singh, S. (2021). Improvement in the func- tional properties of quinoa (Chenopodium quinoa) protein isolates after the application of controlled heat-treatment: Effect on struc- tural properties. Food Structure, 28, 100189. https://doi.org/10. 1016/j.foostr.2021.100189 · DOI
  23. Nan, J., Zou, M., Wang, H., Xu, C., Zhang, J., Wei, B., He, L., & Xu, Y. (2018). Effect of ultra-high pressure on molecular structure and properties of bullfrog skin collagen. International Journal of Biological Macromolecules, 111, 200-207. https://doi.org/10.1016/j. ijbiomac.2017.12.163 · DOI
  24. Nowak, V., Du, J., & Charrondière, U. R. (2016). Assessment of the nutritional composition of quinoa (Chenopodium quinoa Willd.). Food Chemistry, 193, 47-54. https://doi.org/10.1016/j.foodchem. 2015.02.111 · DOI
  25. Peled, S., & Livney, Y. D. (2021). The role of dietary proteins and car- bohydrates in gut microbiome composition and activity: A review. Food Hydrocolloids, 120, 106911. https://doi.org/10.1016/j.foodhyd. 2021.106911 · DOI
  26. Peng, W., Kong, X., Chen, Y., Zhang, C., Yang, Y., & Hua, Y. (2016). Effects of heat treatment on the emulsifying properties of pea proteins. Food Hydrocolloids, 52, 301-310. https://doi.org/10.1016/ j.foodhyd.2015.06.025 · DOI
  27. Sezgin, A. C., & Sanlier, N. (2019). A new generation plant for the con- ventional cuisine: Quinoa (Chenopodium quinoa Willd.). Trends in Food Science & Technology, 86, 51-58. https://doi.org/10.1016/j. tifs.2019.02.039 · DOI
  28. Shen, Y., Tang, X., & Li, Y. (2021). Drying methods affect physic- ochemical and functional properties of quinoa protein isolate. Food Chemistry, 339, 127823. https://doi.org/10.1016/j.foodchem. 2020.127823 · DOI
  29. Tavano, O. L., Amistá, M. J. de. M., Del Ciello, G., Rodrigues, M. C. M., Bono Nishida, A. M., Valadares, L. A., Siqueira, B. M., Gomes, R. A. da. S., Parolini, M. T., & Silva Junio, S. I. d. (2022). Isolation and evaluation of quinoa (Chenpodium quinoa Willd.) protein fractions. A nutritional and bio-functional approach to the globulin fraction. Current Research in Food Science, 5, 1028-1037. https://doi.org/10.1016/j.crfs.2022.06.006 · DOI · Paper page
  30. Wang, L., Dong, J. I., Zhu, Y. Y., Shen, R. I., Wu, L. G., & Zhang, K. Y. (2020). Effects of microwave heating, steaming, boiling and baking on the structure and functional properties of quinoa (Chenopodium quinoa Willd.) protein isolates. International Jour- nal of Food Science & Technology, 56(2), 709-720. https://doi.org/ 10.1111/ijfs.14706 · DOI
  31. Wang, S., Miao, S., & Sun, D. W. (2024). Modifying structural and techno-functional properties of quinoa proteins through extrac- tion techniques and modification methods. Trends in Food Sci- ence & Technology, 143, 104285. https://doi.org/10.1016/j.tifs.2023. 104285 · DOI · Paper page
  32. Yang, X. Y., Shi, L. S., Gong, T., Hu, C. Y., Guo, Y. R., & Meng, Y. H. (2022). Structural modification induced by heat treat- ments improves the emulsifying attributes of lacquer seed protein isolate. International Journal of Biological Macromolecules, 222, 1700-1708. https://doi.org/10.1016/j.ijbiomac.2022.09.223 · DOI
  33. Zhang, D., Cai, Y., Lao, F., & Wu, J. (2024). Steam cooking drives alter- ations of proteomics, protein structural and functional properties in rice (Oryza sativa l.). Food Bioscience, 59, 103899. https://doi. org/10.1016/j.fbio.2024.103899 · DOI
  34. Zhao, Q., Xiong, H., Selomulya, C., Chen, X. D., Huang, S., Ruan, X., Qiang, Z., & Sun, W. (2013). Effects of spray drying and freeze drying on the properties of protein isolate from rice dreg protein. Food and Bioprocess Technology, 6(7), 1759-1769. https://doi.org/ 10.1007/s11947-012-0844-3 · DOI
  35. Zhao, Y., Yuan, Y., Yuan, X., Zhao, S., Kang, Z., Zhu, M., He, H., & Ma, H. (2023). Physicochemical, conformational and functional changes of quinoa protein affected by high-pressure homogeniza- tion. LWT-Food Science and Technology, 173, 114343. https://doi. org/10.1016/j.lwt.2022.114343 · DOI · Paper page

Cited by

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Authors
Chang, J., Zhao, Y., & Xu, J.
Affiliations
College of Food Science and Technology Shanghai Ocean University Shanghai China
ORCID
Venue
Journal of Food Science
Publisher
Wiley
Published
2025-02
Volume
90
Issue
2
ISSN
  • 0022-1147
  • 1750-3841
DOI
10.1111/1750-3841.70051
Cited by
14
References
1
Language
en
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor, 9 d)
Funders
Science and Technology Commission of Shanghai Municipality (23YF1416700)

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