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Physicochemical and functional properties of buckwheat (Fagpopyrum esculentum Moench) albumin

Ninomiya, Kazumi, Yamaguchi, Yusuke, Kumagai, Hitoshi, Kumagai, Hitomi·2022·Future Foods
DOI 10.1016/j.fufo.2022.100178
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  • Albumin-rich fractions remain comparatively soluble even at mildly acidic pH, indicating that fraction composition is a key confounder when buckwheat protein is treated as a single ingredient.

    “In contrast, albumin-rich fractions remain compara­ tively soluble even at mildly acidic pH, indicating that fraction composition is a key confounder when buckwheat protein is treated as a single ingredient”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Ninomiya et al., 2022

    Section 3.2 (Solubility; page unavailable) reports that buckwheat albumin remained highly soluble across pH 3–6, supporting the acidic-pH portion of the claim. The paper compares it with egg albumin and casein, but does not establish that differences among buckwheat protein fractions make fraction composition a key confounder when buckwheat protein is treated as a single ingredient. (LLM, conf=0.84)

    Experimental — accuracy not yet measured

  • Common buckwheat 2S albumins contain established allergenic proteins, including Fag e 1 and Fag e 2.

    “Common buckwheat 2S albumins contain established allergenic proteins, including Fag e 1 and Fag e 2.”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Ninomiya et al., 2022

    The Introduction discusses buckwheat albumin and its functional properties, but does not identify 2S albumins or allergenic proteins. Searches for Fag e 1, Fag e 2, 2S albumin, and allergy found no passage addressing the claim in our copy; page numbers were unavailable. (LLM, conf=0.74)

    Experimental — accuracy not yet measured

  • The major 13S globulins are typically resolved as high-order oligomers (340 kDa) with fewer intermediate SEC peaks than amaranth, consistent with a stronger native oligomeric structure under mild conditions.

    “The major 13S globulins are typically resolved as high-order oligomers (340 kDa) with fewer intermediate SEC peaks than amaranth, consistent with a stronger native oligomeric structure under mild conditions”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Ninomiya et al., 2022

  • The presence of allergenic 2S albumins in common buckwheat complicates fraction selection for emulsion applications and supports fraction-processing rather than treating buckwheat protein as a single ingredient.

    “This finding complicates fraction selection for emulsion applications and supports fraction-processing rather than treating buckwheat protein as a single ingredient”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Ninomiya et al., 2022

  • For buckwheat, albumins foam better (especially under mildly acidic conditions) than globulins, whereas strong globulin self-association can slow adsorption and weaken foam stability.

    “For buckwheat, foaming is strongly dependent on protein fractions. Albumins foam better (espe­ cially under mildly acidic conditions) than globulins, whereas strong globulin self-association can slow adsorption and weaken foam stability (Ninomiya et al., 2022).”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Ninomiya et al., 2022

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Research works printed but not linked: 40

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Cited by

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Authors
Ninomiya, K., Yamaguchi, Y., Kumagai, H., & Kumagai, H.
ORCID
Kumagai, Hitomi
Venue
Future Foods
Publisher
Elsevier BV
Published
2022-12
Volume
6
Pages
100178
ISSN
2666-8335
DOI
10.1016/j.fufo.2022.100178
Cited by
11
References
0
Language
en
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