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

Polysaccharide lyases from gellan-producing Sphingomonas spp

Lynn Kennedy1, Ian W Sutherland1

  • 1Institute of Cell and Molecular Biology, Edinburgh University, Mayfield Road, Edinburgh EH9 3JH, UK.

Microbiology (Reading, England)
|April 1, 1996
PubMed
Summary

Sphingomonas bacteria produce gellanase enzymes that degrade deacylated gellan and rhamsan. These extracellular lyases cleave specific sugar sequences, with some periplasmic glucosidase and glucuronidase activity also observed.

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

Molecular detection of insecticide resistance markers in Aedes aegypti (Diptera: Culicidae) populations from Haiti.

Journal of medical entomology·2026
Same author

Correction: The changing meaning of "no" in Canadian sex work.

PloS one·2024
Same author

The changing meaning of "no" in Canadian sex work.

PloS one·2024
Same author

Estimating turnover and industry longevity of Canadian sex workers.

PloS one·2024
Same author

Etiology and risk factors for diarrheal disease amongst rural and peri-urban populations in Cambodia, 2012-2018.

PloS one·2023
Same author

Clinical and epidemiologic evaluation of a 2020 chikungunya outbreak in Cambodia.

BMC infectious diseases·2022

Area of Science:

  • Microbiology
  • Biochemistry
  • Enzymology

Background:

  • Sphingomonas strains synthesize gellan and related polysaccharides.
  • Gellan and rhamsan are bacterial exopolysaccharides with distinct structures.
  • Enzymatic degradation pathways for these polymers are not fully elucidated.

Purpose of the Study:

  • To investigate the gellanase activity in Sphingomonas strains.
  • To characterize the enzymes responsible for gellan and rhamsan degradation.
  • To determine the substrate specificity of these enzymes.

Main Methods:

  • Enzyme assays on deacylated gellan and rhamsan.
  • Analysis of degradation products using chromatography.
  • Characterization of enzyme location (extracellular vs. periplasmic).

Related Experiment Videos

Main Results:

  • Sphingomonas strains exhibit constitutive extracellular gellanase activity.
  • The enzymes are eliminase-type lyases, cleaving specific glycosidic linkages.
  • Deacetylated rhamsan is an alternative substrate; acylated forms are resistant.
  • Associated beta-D-glucosidase and beta-D-glucuronidase activities are found in the periplasm.

Conclusions:

  • Sphingomonas gellanases are extracellular lyases specific for deacylated polysaccharides.
  • Enzyme activity is generally low, with variations between strains.
  • The degradation products are consistent with enzymatic cleavage of the polysaccharide backbone.