Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Rheological properties of modified lupin proteins.

J P Krause1, C Bagger, K D Schwenke

  • 1Institut für Angewandte Proteinchemie e. V. Potsdam, Stahnsdorfer Damm 81, D-14532 Kleinmacnow, Germany. krause@prochem-potsdam.de

Die Nahrung
|November 20, 2001
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Comparative studies on thermodynamic characteristics of pea legumin and legumin-T thermal denaturation.

International journal of biological macromolecules·2001
Same author

Exploitation of the functional potential of legume proteins.

Die Nahrung·2001
Same author

Reflections about the functional potential of legume proteins. A review.

Die Nahrung·2001
Same author

Plant protein interactions with polysaccharides and their influence on legume protein functionality. A review.

Die Nahrung·2001
Same author

Outcome of children identified as anemic by routine screening in an inner-city clinic.

Archives of pediatrics & adolescent medicine·2001
Same author

Changes in interfacial behaviour, emulsifying and foaming properties of faba bean legumin after modification with dimethylsuberimidate.

Die Nahrung·2001

Chemical modifications like succinylation, acetylation, and phosphorylation significantly alter yellow lupin protein isolate (LPI) properties. Succinylation boosted viscosity and lowered gelation temperature, while acetylation and phosphorylation affected flow behavior and gel strength.

Area of Science:

  • Food Science
  • Protein Chemistry
  • Rheology

Background:

  • Yellow lupin protein isolate (LPI) is a potential food ingredient.
  • Understanding its modification properties is crucial for food applications.
  • Chemical modifications can alter protein functionality.

Purpose of the Study:

  • To investigate the impact of acetylation, succinylation, and phosphorylation on LPI properties.
  • To analyze the rheological behavior of modified LPI dispersions and gels.
  • To determine how these modifications affect viscosity, gel point, and gel texture.

Main Methods:

  • Extraction of protein isolates from yellow lupin (L. luteus) flour.
  • Chemical modifications: acetylation, succinylation, and phosphorylation.

Related Experiment Videos

  • Oscillatory rheology to study dispersions (15% w/w) and thermotropic gels.
  • Main Results:

    • Succinylation increased LPI dispersion viscosity from 99 to 515 mPas and yielded the lowest gel point (30.5°C).
    • Acetylation and phosphorylation enhanced pseudoplastic flow behavior in LPI dispersions.
    • Acetylated lupin formed strong gels with a narrow visco-elastic range; phosphorylated lupin formed weak, "rubber-like" gels.

    Conclusions:

    • Chemical modifications distinctly influence the rheological properties and gelation behavior of yellow lupin protein isolates.
    • Succinylation offers a route to increase viscosity and reduce gelation temperature.
    • Acetylation and phosphorylation provide different textural outcomes, impacting gel strength and elasticity for tailored food applications.