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 Research Publications
    • View Item
    • espace Home
    • espace
    • Curtin Research Publications
    • View Item

    Encapsulation of lipase in mesoporous silica yolk-shell spheres with enhanced enzyme stability

    Access Status
    Fulltext not available
    Authors
    Zhao, Z.
    Liu, Jian
    Hahn, M.
    Qiao, S.
    Middelberg, A.
    He, L.
    Date
    2013
    Type
    Journal Article
    
    Metadata
    Show full item record
    Citation
    Zhao, Zheng Yang and Liu, Jian and Hahn, Mandy and Qiao, Shizhang and Middelberg, Anton P.J. and He, Lizhong. 2013. Encapsulation of lipase in mesoporous silica yolk-shell spheres with enhanced enzyme stability. RSC Advances. 3 (44): pp. 22008-22013.
    Source Title
    RSC Advances
    DOI
    10.1039/C3RA43382J
    ISSN
    20462069
    URI
    http://hdl.handle.net/20.500.11937/29037
    Collection
    • Curtin Research Publications
    Abstract

    Enzyme encapsulation is an attractive method among the different immobilization strategies to improve the reusability and stability of enzymes because it can separate enzymes from a hazardous external environment. However, current encapsulation methods have limitations including enzyme leakage. In this study, a new approach based on a two-step soft templating method has been proposed to encapsulate lipase within substrate permeable mesoporous silica yolk–shell spheres. In the first step, lipase was immobilized onto epoxy functionalized silica nanospheres that serve as the core materials. The core materials were mixed with a fluorocarbon surfactant, FC4, to form a core–vesicle complex. In the second step, a mesoporous silica shell was assembled surrounding the core–vesicle complex to form the yolk–shell structure with the lipase encapsulated. The mesoporous silica shell has a pore size of 2.1 nm, which is permeable to the reactant and product while isolating the enzymes from harmful external conditions. The encapsulated lipase retained 87.5% of its activity after thermal treatment at 70 °C for 2 hours while the free enzyme lost 99.5% of its activity under the same treatment. Importantly, the encapsulated lipase shows significantly enhanced resistance to degradation by proteases.

    Related items

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

    • Pretreatment of wastewater containing fats and oils using an immobilized enzyme.
      Jia, Huanfei (2002)
      This thesis investigates an application of immobilized lipase for pre-treating wastewater containing fats and oils, which is difficult to treat practically. The kinetics of soluble lipase was studied for establishing ...
    • Growing a hydrophilic nanoporous shell on a hydrophobic catalyst interface for aqueous reactions with high reaction efficiency and: In situ catalyst recycling
      Hao, Y.; Jiao, X.; Zou, H.; Yang, H.; Liu, Jian (2017)
      © 2017 The Royal Society of Chemistry. The structure of biological components such as enzymes with active centers buried in hydrophobic pockets has inspired the design of new nanoreactors for efficient chemical processes. ...
    • Advances in Multicompartment Mesoporous Silica Micro/Nanoparticles for Theranostic Applications.
      Liu, J.; Liu, T.; Pan, J.; Liu, Shaomin; Lu, G. (2018)
      Mesoporous silica nanoparticles (MSNs) are promising functional nanomaterials for a variety of biomedical applications, such as bioimaging, drug/gene delivery, and cancer therapy. This is due to their low density, low ...
    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.