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

Substrate and binding specificities of bacterial polyhydroxybutyrate depolymerases.

K Kasuya1, T Ohura, K Masuda

  • 1Polymer Chemistry Laboratory, The Institute of Physical and Chemical Research (RIKEN), Saitama, Japan.

International Journal of Biological Macromolecules
|July 17, 1999
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

Multifocal granulomatous jejunitis associated with an argyrophilic gram-positive segmented filamentous bacterium in a Holstein cow.

Journal of comparative pathology·2011
Same author

Lawsonia intracellularis and virulent Rhodococcus equi infection in a thoroughbred colt.

Journal of comparative pathology·2010
Same author

Magnetic compression anastomosis: a novel technique for canalization of severe hilar bile duct strictures.

Endoscopy·2005
Same author

Experimental study of plasma recycling system by off-line bioartificial liver in rats.

Transplantation proceedings·2002
Same author

Is frozen section effective for diagnosis of unsuspected gallbladder cancer during laparoscopic cholecystectomy?

Surgical endoscopy·2002
Same author

Enzymatic degradation of atactic poly(R,S-3-hydroxybutyrate) induced by amorphous polymers and the enzymatic degradation temperature window of an amorphous polymer system.

Biomacromolecules·2001
Same journal

Marek's disease virus-encoded microRNA-M6-5p suppresses viral replication by targeting UL42.

International journal of biological macromolecules·2026
Same journal

Pioneering the formation of 2-carboxylic anthraquinone: CRISPR/Cas9-mediated functional validation of Octaketide synthase and Polyketide reductase genes in Aloe vera.

International journal of biological macromolecules·2026
Same journal

Characterization of the blueberry AUXIN RESISTANT 1/LIKE-AUX1 gene family and regulatory roles of VcAUX1/LAX12 in flower bud burst.

International journal of biological macromolecules·2026
Same journal

Structural and biochemical insights into an anthocyanin-related glutathione transferase from bilberry and its inhibition by quercetin.

International journal of biological macromolecules·2026
Same journal

Hydrolases enzymes for oral biofilm reduction: Lipase, lysozyme, and amylase as promising candidates for canine oral health applications.

International journal of biological macromolecules·2026
Same journal

Dietary chitosan alleviates Enterohemorrhagic Escherichia coli induced intestinal injury by reducing bacterial colonization and restoring mucosal immune homeostasis in weaned piglets.

International journal of biological macromolecules·2026
See all related articles

Three bacterial polyhydroxybutyrate (PHB) depolymerases showed broad substrate specificity, hydrolyzing five aliphatic polyesters. Their binding domains strongly adsorbed onto polyester granules, suggesting specific interactions for PHB degradation.

Area of Science:

  • Biochemistry
  • Polymer Science
  • Microbiology

Background:

  • Extracellular polyhydroxybutyrate (PHB) depolymerases are key enzymes for PHB biodegradation.
  • These enzymes are classified into types A and B based on lipase box positioning in their catalytic domains.
  • Understanding their substrate specificity and binding mechanisms is crucial for developing effective biodegradation strategies.

Purpose of the Study:

  • To investigate the substrate specificities of PHB depolymerases from Alcaligenes faecalis, Pseudomonas stutzeri, and Comamonas acidovorans.
  • To analyze the binding characteristics of substrate binding domains of PHB depolymerases from C. faecalis, C. acidovorans, and C. testosteroni.
  • To elucidate the interactions between PHB depolymerases and various aliphatic polyesters.

Main Methods:

Related Experiment Videos

  • Enzymatic hydrolysis assays using films of 12 different aliphatic polyesters.
  • Construction and purification of glutathione S-transferase (GST) fusion proteins of substrate binding domains.
  • Analysis of fusion protein adsorption onto polyester granules and determination of adsorption kinetics (Langmuir isotherm).

Main Results:

  • PHB depolymerases hydrolyzed poly(3-hydroxybutyrate) (P(3HB)), poly(3-hydroxypropionate) (P(3HP)), poly(4-hydroxybutyrate) (P(4HB)), poly(ethylene succinate) (PESU), and poly(ethylene adipate) (PEA).
  • GST-fusion proteins strongly adsorbed onto P(3HB), P(3HP), and poly(2-hydroxypropionate) (P(2HP)) granules, but not on Avicel or chitin.
  • Adsorption kinetics followed the Langmuir isotherm, with an estimated cross-sectional area of 12+/-4 nm²/molecule on P(3HB) granules.

Conclusions:

  • PHB depolymerases exhibit broad substrate specificity towards certain aliphatic polyesters.
  • Specific amino acid interactions in the substrate-binding domains are responsible for strong adsorption onto polyester surfaces.
  • The findings suggest a conserved conformational structure in the active sites of PHB depolymerases, facilitating polyester hydrolysis.