Curtin University Homepage
  • Library
  • Help
    • Admin

    espace - Curtin’s institutional repository

    JavaScript is disabled for your browser. Some features of this site may not work without it.
    View Item 
    • espace Home
    • espace
    • Curtin Theses
    • View Item
    • espace Home
    • espace
    • Curtin Theses
    • View Item

    Increasing the Gelling Functionality of Lupin Protein Using Ultrasound Treatment

    AlAli H 2020.pdf (5.291Mb)
    Access Status
    Open access
    Authors
    Al-Ali, Hayder A.
    Date
    2020
    Supervisor
    Stuart Johnson
    Type
    Thesis
    Award
    PhD
    
    Metadata
    Show full item record
    Faculty
    Health Sciences
    School
    School of Molecular and Life Sciences
    URI
    http://hdl.handle.net/20.500.11937/83446
    Collection
    • Curtin Theses
    Abstract

    Protein concentrate from the legume seed lupin has great potential in human nutrition however it use as a food ingredient is limited by its lack of gelling properties. The use of ultrasound to increase the gelling ability of the protein was optimised using statistical modelling and associated molecular changes were identified. The resulting modified protein with strong gelling ability has great potential as a texturising ingredient in a wide range of plant-based foods.

    Related items

    Showing items related by title, author, creator and subject.

    • Ion-transfer electrochemistry of rat amylin at the water–organogel microinterface array and its selective detection in a protein mixture
      De Eulate, Eva; O'Sullivan, Shane; Fletcher, Sharon; Newsholme, Philip; Arrigan, Damien (2013)
      The behaviour of proteins and polypeptides at electrified aqueous-organic interfaces is of benefit in label-free detection strategies. In this work, rat amylin (or islet amyloid polypeptide) was studied at the interface ...
    • Gelation properties of myofibrillar protein under malondialdehyde-induced oxidative stress
      Wang, L.; Zhang, M.; Fang, Zhongxiang; Bhandari, B. (2017)
      Background: The structure of myofibrillar protein (MP) can be readily altered by oxidation, leading to the unfolding of MP structure, which further promotes protein–protein interactions, and thus influences the MP gelling ...
    • Evaluation of protease resistance and toxicity of amyloid-like food fibrils from whey, soy, kidney bean, and egg white
      Lassé, M.; Ulluwishewa, Dulantha; Healy, J.; Thompson, D.; Miller, A.; Roy, N.; Chitcholtan, K.; Gerrard, J. (2016)
      © 2015 Elsevier Ltd. Abstract The structural properties of amyloid fibrils combined with their highly functional surface chemistry make them an attractive new food ingredient, for example as highly effective gelling agents. ...
    Advanced search

    Browse

    Communities & CollectionsIssue DateAuthorTitleSubjectDocument TypeThis CollectionIssue DateAuthorTitleSubjectDocument Type

    My Account

    Admin

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular Authors

    Follow Curtin

    • 
    • 
    • 
    • 
    • 

    CRICOS Provider Code: 00301JABN: 99 143 842 569TEQSA: PRV12158

    Copyright | Disclaimer | Privacy statement | Accessibility

    Curtin would like to pay respect to the Aboriginal and Torres Strait Islander members of our community by acknowledging the traditional owners of the land on which the Perth campus is located, the Whadjuk people of the Nyungar Nation; and on our Kalgoorlie campus, the Wongutha people of the North-Eastern Goldfields.