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

Thioglucosidase activity from Sphingobacterium sp. strain OTG1.

G H Meulenbeld1, S Hartmans

  • 1Department of Agrotechnology and Food Sciences, Wageningen University, The Netherlands. gerwin.meulenbeld@imb.ftns.wau.nl

Applied Microbiology and Biotechnology
|October 17, 2001
PubMed
Summary

Researchers discovered a novel thioglucosidase in Sphingobacterium sp. strain OTG1 that effectively hydrolyzes various thioglycosides, including sinigrin, offering potential for new enzymatic applications.

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

A cloned Bacillus halodurans multicopper oxidase exhibiting alkaline laccase activity.

Applied microbiology and biotechnology·2004
Same author

Membrane-aerated biofilm reactor for the removal of 1,2-dichloroethane by Pseudomonas sp. strain DCA1.

Applied microbiology and biotechnology·2004
Same author

Co-metabolic degradation of chlorinated hydrocarbons by Pseudomonas sp. strain DCA1.

Applied microbiology and biotechnology·2002
Same author

Plate screening methods for the detection of polysaccharase-producing microorganisms.

Applied microbiology and biotechnology·2001
Same author

Biodegradability of food-associated extracellular polysaccharides.

Current microbiology·2000
Same author

Transglycosylation by Streptococcus mutans GS-5 glucosyltransferase-D: acceptor specificity and engineering of reaction conditions.

Biotechnology and bioengineering·2000

Area of Science:

  • Microbiology
  • Enzymology
  • Biochemistry

Background:

  • Thioglycosides are sulfur-containing glycosides with diverse biological roles.
  • Enzymes capable of hydrolyzing thioglycosides are of interest for biotechnological applications.
  • Sphingobacterium species are known for their metabolic versatility.

Purpose of the Study:

  • To isolate and characterize microorganisms with novel thioglucoside hydrolase activity.
  • To investigate the substrate specificity of the identified enzyme.
  • To explore the potential of the isolated strain as a biocatalyst.

Main Methods:

  • Enrichment culture of Sphingobacterium sp. strain OTG1 using octylthioglucoside (OTG).
  • Enzymatic assays using cell-free extracts to determine hydrolase activity.

Related Experiment Videos

  • Use of beta-glucosidase inhibitors (ascorbic acid, D-gluconic acid lactone) to differentiate enzyme activities.
  • Testing hydrolysis of various thioglycosides and sinigrin.
  • Main Results:

    • Isolation of Sphingobacterium sp. strain OTG1 exhibiting thioglucoside hydrolase activity.
    • Hydrolysis of OTG into octanethiol and glucose by cell-free extracts.
    • Demonstration of broad substrate specificity for the novel thioglucosidase, including sinigrin.
    • Sinigrin utilization as a growth substrate by the strain, with limitations at higher concentrations.

    Conclusions:

    • Sphingobacterium sp. strain OTG1 possesses a novel thioglucosidase with broad substrate specificity.
    • The enzyme is distinct from typical beta-glucosidases.
    • The strain shows potential for the degradation of thioglycosides and glucosinolates.