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Physicochemical, conformational and functional changes of quinoa protein affected by high-pressure homogenization

Zhao, Yanyan, Yuan, Yibo, Yuan, Xiaorui, Zhao, Shengming, Kang, Zhuangli, Zhu, Mingming, He, Hongju, Ma, Hanjun·2023·LWT
DOI 10.1016/j.lwt.2022.114343
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  • Specific routes such as pH-shift combined with heating or ultrasound, HPH and ultrasound-assisted enzymatic extraction often reduce floc size from 0.8-1.2 μm to 0.15-0.5 μm.

    “By contrast, specific routes such as pH-shift combined with heating or ultrasound, HPH and ultrasound-assisted enzymatic extraction often reduce floc size from 0.8-1.2 μ m to 0.15-0.5 μ m.”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Zhao et al., 2023b

    Section 3.1 reports that high-pressure homogenization reduced the mean particle size of quinoa protein from 4093 nm to as little as 252 nm. The paper does not support the claimed starting range of 0.8–1.2 μm or address the other named routes, including pH-shift combinations and ultrasound-assisted enzymatic extraction. Page numbers were not available in our copy. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

  • pH-shift combined with heat or ultrasound, high-pressure homogenization, and ultrasound-assisted enzymatic routes commonly reduce the mean particle size to 0.15-0.5 μm and narrow the size distribution.

    “However, pH-shift combined with heat or ultrasound, high-pressure homogenization, and ultrasound-assisted enzymatic routes commonly reduce the mean particle size to 0.15-0.5 μ m and narrow the size distribution”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Zhao et al., 2023b

  • The mechanism that increased conformational flexibility and hydrophobic exposure leads to faster interfacial adsorption remains inferential unless direct interfacial measurements are available.

    “However, this mechanism remains inferential unless direct interfacial measurements are available”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Zhao et al., 2023b

  • Treatments that reduce aggregate size and increase ζ-potential magnitude (pH-shift combined with heating or ultrasound, high-pressure homogenization) commonly accelerate interfacial coverage and improve stability for quinoa.

    “Treatments that reduce aggregate size and increase ζ -potential magnitude (pH-shift combined with heating or ul­ trasound, high-pressure homogenization) commonly accelerate interfa­ cial coverage and improve stability (Wang et al., 2025a; Zhao et al., 2023b).”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Zhao et al., 2023b

  • Extraction treatments (pH-shift with heating or ultrasound, high-pressure homogenization) can increase the magnitude of ζ-potential and reduce particle size, shifting quinoa dispersions from micron flocs toward submicron particles and improving neutral-pH dispersibility and solubility.

    “Extraction treatments (pH-shift with heating or ultra­ sound, high-pressure homogenization) can increase the magnitude of ζ -potential and reduce particle size, shifting quinoa dispersions from micron flocs toward submicron particles and improving neutral-pH dispersibility and solubility”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Zhao et al., 2023b

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Cited by

Sorted by citations

Authors
Zhao, Y., Yuan, Y., Yuan, X., Zhao, S., Kang, Z., Zhu, M., He, H., & Ma, H.
ORCID
Zhao, Shengming
Venue
LWT
Publisher
Elsevier BV
Published
2023-01
Volume
173
Pages
114343
ISSN
0023-6438
DOI
10.1016/j.lwt.2022.114343
Cited by
78
References
1
Language
en
Licence

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