View in EDS

Low- and intermediate-frequency ultrasound modification of millet protein: Implications for emulsifying and gelling properties.

Saved in:
Bibliographic Details
Title: Low- and intermediate-frequency ultrasound modification of millet protein: Implications for emulsifying and gelling properties.
Authors: Ma, Yan-Rong1 (AUTHOR), Manickam, Sivakumar2 (AUTHOR), Xu, Yong-Qiang1 (AUTHOR), Chen, Zhi-Gang1 (AUTHOR) zgchen@njau.edu.cn, Wu, Yue1,3 (AUTHOR) wu.yue@njau.edu.cn
Source: Food Chemistry. May2026, Vol. 511, pN.PAG-N.PAG. 1p.
Subjects: Protein structure, Gelation, Molecular dynamics, Three-dimensional printing, Plant proteins, Sonication, Emulsions, Functional foods
Abstract: Ultrasonic processing is increasingly being explored as a green strategy to tailor protein functionality, yet the mechanisms underlying frequency-dependent effects remain insufficiently understood. In this study, millet protein (MP) was subjected to low- and intermediate-frequency ultrasound (20 kHz and 207 kHz) and controlled power densities (48.70 W/L and 80.29 W/L) to elucidate structure-function-application relationships. Ultrasonic treatment induced pronounced conformational rearrangements, characterized by increased surface hydrophobicity and β -sheet content, accompanied by reduced free sulfhydryl groups and α -helix content. Molecular dynamics simulations supported these observations, revealing intensified residue-level fluctuations under intermediate-frequency ultrasound, indicative of enhanced structural flexibility. These molecular changes translated into markedly improved functional performance, including enhanced emulsifying stability and optimized rheological behavior, with ultrasound power identified as the dominant governing parameter. Notably, LUS-80.29 W/L emulsion gel exhibited superior 3D printability and effectively encapsulated curcumin, enabling intestinal-targeted release and improved micellization. This study provides mechanistic insight into frequency-regulated ultrasonic modification of MP and demonstrates its potential for designing functional, printable protein-based delivery systems in advanced food applications. [Display omitted] • LUS predominantly altered MP size and secondary structure through physical shearing. • IUS modified MP via sonochemical effects, exposing its internal hydrophobic groups. • MD simulations revealed that IUS-induced residue fluctuations were more obvious. • IUS-treated MP emulsions formed a more uniform and denser droplet distribution. • LUS-treated MP gels exhibited superior rheological properties compared to IUS. [ABSTRACT FROM AUTHOR]
Copyright of Food Chemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
FullText Text:
  Availability: 0
Header DbId: egs
DbLabel: Engineering Source
An: 193093235
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 0
IllustrationInfo
Items – Name: Title
  Label: Title
  Group: Ti
  Data: Low- and intermediate-frequency ultrasound modification of millet protein: Implications for emulsifying and gelling properties.
– Name: Author
  Label: Authors
  Group: Au
  Data: <searchLink fieldCode="AR" term="%22Ma%2C+Yan-Rong%22">Ma, Yan-Rong</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Manickam%2C+Sivakumar%22">Manickam, Sivakumar</searchLink><relatesTo>2</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Xu%2C+Yong-Qiang%22">Xu, Yong-Qiang</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Chen%2C+Zhi-Gang%22">Chen, Zhi-Gang</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> zgchen@njau.edu.cn</i><br /><searchLink fieldCode="AR" term="%22Wu%2C+Yue%22">Wu, Yue</searchLink><relatesTo>1,3</relatesTo> (AUTHOR)<i> wu.yue@njau.edu.cn</i>
– Name: TitleSource
  Label: Source
  Group: Src
  Data: <searchLink fieldCode="JN" term="%22Food+Chemistry%22">Food Chemistry</searchLink>. May2026, Vol. 511, pN.PAG-N.PAG. 1p.
– Name: Subject
  Label: Subjects
  Group: Su
  Data: <searchLink fieldCode="DE" term="%22Protein+structure%22">Protein structure</searchLink><br /><searchLink fieldCode="DE" term="%22Gelation%22">Gelation</searchLink><br /><searchLink fieldCode="DE" term="%22Molecular+dynamics%22">Molecular dynamics</searchLink><br /><searchLink fieldCode="DE" term="%22Three-dimensional+printing%22">Three-dimensional printing</searchLink><br /><searchLink fieldCode="DE" term="%22Plant+proteins%22">Plant proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Sonication%22">Sonication</searchLink><br /><searchLink fieldCode="DE" term="%22Emulsions%22">Emulsions</searchLink><br /><searchLink fieldCode="DE" term="%22Functional+foods%22">Functional foods</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Ultrasonic processing is increasingly being explored as a green strategy to tailor protein functionality, yet the mechanisms underlying frequency-dependent effects remain insufficiently understood. In this study, millet protein (MP) was subjected to low- and intermediate-frequency ultrasound (20 kHz and 207 kHz) and controlled power densities (48.70 W/L and 80.29 W/L) to elucidate structure-function-application relationships. Ultrasonic treatment induced pronounced conformational rearrangements, characterized by increased surface hydrophobicity and β -sheet content, accompanied by reduced free sulfhydryl groups and α -helix content. Molecular dynamics simulations supported these observations, revealing intensified residue-level fluctuations under intermediate-frequency ultrasound, indicative of enhanced structural flexibility. These molecular changes translated into markedly improved functional performance, including enhanced emulsifying stability and optimized rheological behavior, with ultrasound power identified as the dominant governing parameter. Notably, LUS-80.29 W/L emulsion gel exhibited superior 3D printability and effectively encapsulated curcumin, enabling intestinal-targeted release and improved micellization. This study provides mechanistic insight into frequency-regulated ultrasonic modification of MP and demonstrates its potential for designing functional, printable protein-based delivery systems in advanced food applications. [Display omitted] • LUS predominantly altered MP size and secondary structure through physical shearing. • IUS modified MP via sonochemical effects, exposing its internal hydrophobic groups. • MD simulations revealed that IUS-induced residue fluctuations were more obvious. • IUS-treated MP emulsions formed a more uniform and denser droplet distribution. • LUS-treated MP gels exhibited superior rheological properties compared to IUS. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Food Chemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=egs&AN=193093235
RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1016/j.foodchem.2026.148845
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        PageCount: 1
        StartPage: N.PAG
    Subjects:
      – SubjectFull: Protein structure
        Type: general
      – SubjectFull: Gelation
        Type: general
      – SubjectFull: Molecular dynamics
        Type: general
      – SubjectFull: Three-dimensional printing
        Type: general
      – SubjectFull: Plant proteins
        Type: general
      – SubjectFull: Sonication
        Type: general
      – SubjectFull: Emulsions
        Type: general
      – SubjectFull: Functional foods
        Type: general
    Titles:
      – TitleFull: Low- and intermediate-frequency ultrasound modification of millet protein: Implications for emulsifying and gelling properties.
        Type: main
  BibRelationships:
    HasContributorRelationships:
      – PersonEntity:
          Name:
            NameFull: Ma, Yan-Rong
      – PersonEntity:
          Name:
            NameFull: Manickam, Sivakumar
      – PersonEntity:
          Name:
            NameFull: Xu, Yong-Qiang
      – PersonEntity:
          Name:
            NameFull: Chen, Zhi-Gang
      – PersonEntity:
          Name:
            NameFull: Wu, Yue
    IsPartOfRelationships:
      – BibEntity:
          Dates:
            – D: 15
              M: 05
              Text: May2026
              Type: published
              Y: 2026
          Identifiers:
            – Type: issn-print
              Value: 03088146
          Numbering:
            – Type: volume
              Value: 511
          Titles:
            – TitleFull: Food Chemistry
              Type: main
ResultId 1