Characterization of the technofunctional properties and three-dimensional structure prediction of 11S globulins from amaranth (Amaranthus hypochondriacus L.) seeds
Abstract
Amaranth 11S globulins (Ah11Sn) are an excellent source of essential amino acids; however, there have been no investigations on the characterization of their techno-functional properties at different pH conditions and NaCl concentrations, which are necessary for food formulations. In this work, we report a new two-step purification method for native Ah11Sn with purity levels of ~95%. LC–MS/MS analysis revealed the presence of three different Ah11Sn paralogs named Ah11SB, A11SC, and Ah11SHMW, and their structures were predicted with Alphafold2. We carried out an experimental evaluation of Ah11Sn surface hydrophobicity, solubility, emulsifying properties, and assembly capacity to provide an alternative application of these proteins in food formulations. Ah11Sn showed good surface hydrophobicity, solubility, and emulsifying properties at pH values of 2 and 3. However, the emulsions became unstable at 60 min. The assembly capacity of Ah11Sn evaluated by DLS analysis showed mainly the trimeric assembly (~150–170 kDa). This information is beneficial to exploit and utilize Ah11Sn rationally in food systems.
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For amaranth, purified 11S globulin typically shows α-helices (10-15%) and β-sheets (35-40%), with the remainder β-turns and unordered structures.
“For amaranth, purified 11S globulin typically shows α -helices (10-15%) and β -sheets (35-40%), with the remainder β -turns and unordered structures”
From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Aguilar-Padilla et al., 2023
Isolation can bias recovery toward globulins while reducing low-MW species that adsorb rapidly and are disproportionately important for foaming and interfacial coverage.
“This pattern suggests that isolation can bias recovery toward globulins while reducing low-MW species that adsorb rapidly and are disproportionately important for foaming and interfacial coverage”
From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Aguilar-Padilla et al., 2023
For amaranth, SEC of purified 11S globulins typically resolves a dominant oligomeric peak consistent with trimeric assemblies (150-170 kDa), with smaller dimeric (90-100 kDa) and monomeric (50 kDa) species.
“For amaranth, SEC of purified 11S globulins typically resolves a dominant oligomeric peak consistent with trimeric assemblies (150-170 kDa), with smaller dimeric (90-100 kDa) and monomeric (50 kDa) species”
From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Aguilar-Padilla et al., 2023
Albumin-rich extracts often show stronger low-MW bands than isolates obtained by alkaline extraction.
“Importantly, albumin-rich extracts often show stronger low-MW bands than isolates obtained by alkaline extraction.”
From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Aguilar-Padilla et al., 2023
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
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Cited by
Sorted by citations
Yan, X., & Zhu, F. (2027) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.113137
- Authors
- Aguilar-Padilla, J., Centeno-Leija, S., Bojórquez-Velázquez, E., Elizalde-Contreras, J. M., Ruiz-May, E., Serrano-Posada, H., & Osuna-Castro, J. A.
- Affiliations
- Facultad de Ciencias Químicas, Universidad de Colima, Carr. Colima-Coquimatlán km. 9, Coquimatlán 28400, Colima, Mexico
- Consejo Nacional de Ciencia y Tecnología, Laboratorio de Biología Sintética, Estructural y Molecular, Laboratorio de Agrobiotecnología, Tecnoparque CLQ, Universidad de Colima, Carretera Los Limones-Loma de Juárez, Colima 28629, Colima, Mexico
- Red de Estudios Moleculares Avanzados, Instituto de Ecología A.C., Cluster BioMimic®, Carretera Antigua a Coatepec 351, El Haya, Xalapa 91073, Veracruz, Mexico
- Facultad de Ciencias Biológicas y Agropecuarias, Universidad de Colima, Carr. Colima-Manzanillo km. 40, Tecomàn 28100, Colima, Mexico
- ORCID
- Venue
- Foods
- Publisher
- MDPI AG
- Published
- 2023-01-19
- Volume
- 12
- Issue
- 3
- Pages
- 461
- ISSN
- 2304-8158
- PMC
- PMC9914310
- Cited by
- 9
- References
- 1
- Language
- en
- Funders
- CONACyT grants (CB-2016-01-285001, INFR-2017-01-280608, CB-2018-A1-S-18011, CF-2019-33-5494771, INFR-2021-17-316456)
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