Physical and thermal characteristics of amaranth (Amaranthus hypochondriacus) protein nanoparticles affected by ultrasound time and microbial transglutaminase
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The same protein can form very different colloidal states depending on processing severity and chemical association.
“These results illustrate that the same protein can form very different colloidal states depending on processing severity and chemical associ ation”
From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Alimi et al., 2024
Nanoparticle formation or fibrillation further strengthens β-sheet signatures and fluorescence perturbations, consistent with more extensive aggregation and tighter intermolecular packing.
“Nanoparticle for mation or fibrillation further strengthens β -sheet signatures and fluo rescence perturbations, consistent with more extensive aggregation and tighter intermolecular packing”
From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Alimi et al., 2024
Further structuring routes can drive proteins toward distinct results, including compact particles in the nano-to submicron range or extended fibrillar/amyloid-like assemblies.
“Further structuring routes can drive proteins toward distinct results, including compact particles in the nano-to submicron range or extended fibrillar/amyloid-like assemblies.”
From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Alimi et al., 2024
Extending sonication or adding microbial transglutaminase further shifts the system toward either compact nanoparticles or larger crosslinked clusters depending on energy input and crosslink density.
“Extending sonication or adding microbial transglutaminase further shifts the system toward either compact nanoparticles or larger crosslinked clusters depending on energy input and crosslink density”
From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Alimi et al., 2024
Cited by
Sorted by citations
Yan, X., & Zhu, F. (2027) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.113137
- Authors
- Alimi, S., Fadavi, A., Sayyed-Alangi, S. Z., & Delouee, S. A.
- ORCID
- Fadavi, Abolfazl
- Venue
- Journal of Food Measurement and Characterization
- Published
- 2024-03-12
- Volume
- 18
- Issue
- 5
- Pages
- 3391-3404
- ISSN
- 2193-4126
- 2193-4134
- Cited by
- 4
- References
- 0
- Language
- en
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