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

Cyclization reaction catalyzed by branching enzyme

H Takata1, T Takaha, S Okada

  • 1Biochemical Research Laboratory, Ezaki Glico Co., Ltd., Nishiyodogawa-ku, Osaka, Japan.

Journal of Bacteriology
|March 1, 1996
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

Planned release of contaminated water from the Fukushima storage tanks into the ocean: Simulation scenarios of radiological impact for aquatic biota and human from seafood consumption.

Marine pollution bulletin·2021
Same author

Temporal and spatial variations of <sup>134</sup>Cs and <sup>137</sup>Cs levels in the Sea of Japan and Pacific coastal region: Implications for dispersion of FDNPP-derived radiocesium.

Journal of environmental radioactivity·2017
Same author

The IAEA handbook on radionuclide transfer to wildlife.

Journal of environmental radioactivity·2012
Same author

Protective effects of mineralocorticoid receptor blockade against neuropathy in experimental diabetic rats.

Diabetes, obesity & metabolism·2011
Same author

New insight into the mitotic chromosome structure: irregular folding of nucleosome fibers without 30-nm chromatin structure.

Cold Spring Harbor symposia on quantitative biology·2011
Same author

Concentration ratios of stable elements for selected biota in Japanese estuarine areas.

Radiation and environmental biophysics·2010

Bacillus stearothermophilus branching enzyme forms cyclic glucans from amylose, not typical branched structures. This novel cyclization mechanism challenges existing models of carbohydrate processing.

Area of Science:

  • Biochemistry
  • Enzymology
  • Carbohydrate Chemistry

Background:

  • Branching enzymes typically create alpha-1,6 linkages in alpha-1,4 glucans.
  • The standard model predicts increased reducing power upon branching.

Purpose of the Study:

  • To investigate the action of Bacillus stearothermophilus branching enzyme on amylose.
  • To elucidate the mechanism of enzyme-catalyzed modification of amylose.

Main Methods:

  • Enzymatic treatment of amylose with branching enzyme.
  • Analysis of molecular size and reducing power.
  • Treatment with glucoamylase and alpha-amylase.
  • Mass spectrometry.

Main Results:

Related Experiment Videos

  • Branching enzyme reduced amylose size without increasing reducing power.
  • A glucoamylase-resistant component was formed.
  • This component was susceptible to alpha-amylase and isoamylase.
  • Mass spectrometry confirmed a cyclic structure.

    • Conclusions:

    • The enzyme catalyzes cyclization of amylose, forming cyclic glucans.
    • This represents a novel mechanism distinct from typical branching.
    • The enzyme forms alpha-1,6 linkages, leading to cyclization rather than linear branching.