Effects of sonication on the in vitro digestibility and structural properties of buckwheat protein isolates
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Reports on common buckwheat globulin typically show 16% of α-helices and 35% of β-sheets, with substantial β-turns and unordered fractions.
“Reports on common buckwheat globulin typically show 16% of α -helices and 35% of β -sheets, with substantial β -turns and unordered fractions”
From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Jin et al., 2021
High-moisture extrusion promotes aggregation and more rigid β-associated structures that co-evolve with texture and digestibility.
“In contrast, high-moisture extrusion promotes aggregation and more rigid β -associated structures that co-evolve with texture and digestibility”
From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Jin et al., 2021
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Plant Proteins for Future Foods: A Roadmap
Sim, S. Y. J., SRV, A., Chiang, J. H., & Henry, C. J. (2021) · Foods · doi:10.3390/foods10081967 · Cited by 352 · see citing works
Yan, X., & Zhu, F. (2027) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.113137
- Authors
- Jin, J., Okagu, O. D., Yagoub, A. E. A., & Udenigwe, C. C.
- Venue
- Ultrasonics Sonochemistry
- Publisher
- Elsevier BV
- Published
- 2021-01
- Volume
- 70
- Pages
- 105348
- ISSN
- 1350-4177
- PMC
- PMC7495248
- Cited by
- 173
- References
- 1
- Language
- en
- Licence
- Funders
- University of Ottawa
- Natural Sciences and Engineering Research Council of Canada
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