Cited by 143biodegradable polymer synthesis and propertiesEnzyme Catalysis and ImmobilizationMicrobial bioremediation and biosurfactants

Kinetics and mechanism of heterogeneous hydrolysis of poly[(R)-3-hydroxybutyrate] film by PHA depolymerases

Mukai, Katsuyuki, Yamada, Kenji, Doi, Yoshiharu·1993·International Journal of Biological Macromolecules

Abstract

The kinetics and mechanism of enzymatic degradation on the surface of poly[(R)-3-hydroxybutyrate] (P[(R)-3HB]) film have been studied using three types of extracellular poly(hydroxyalkanoate) (PHA) depolymerases from Alcaligenes faecalis, Pseudomonas picketti and Comamonas testosteroni. The monomer and dimer of 3-hydroxybutyric acid were produced during the course of the enzymatic degradation of P[(R)-3HB] film, and the rate of production was determined by monitoring the increase in absorbance at 210 nm on a spectrophotometer. The rate of enzymatic degradation increased to a maximum value with the concentration of PHA depolymerase, followed by a gradual decrease. The kinetic data were accounted for in terms of a heterogeneous enzymatic reaction, involving enzymatic degradation on the surface of P[(R)-3HB] film via two steps of adsorption and hydrolysis by a PHA depolymerase with binding and catalytic domains. The kinetic results suggest that the properties of the catalytic domains are very similar among the three PHA depolymerases, but that those of the binding domains are strongly dependent on the type of depolymerase.

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Crossref · 10.1016/0141-8130(93)90054-p

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28 of 28 references verified0 citation errors · 0 not checkable

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Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • Adding a higher amount of enzyme increases the efficiency of degradation up to an inhibitory concentration that is detrimental to degradation rates, owing to saturation of the substrate that prevents the catalytic site from interacting with the polymer.

    “Because of this mechanism of action, adding a higher amount of enzyme increases the efficiency of the degradation up to an inhibitory concentration that is detrimental to the degradation rates, owing to saturation of the substrate that prevents the catalytic site from interacting with the polymer.497”

    From Catalysis as an Enabling Science for Sustainable Polymers (2018) · cites this paper as [497]

  • Depending on the provenance of the PHB depolymerase, either monomer and dimer of 3-hydroxybutyric acid or oligomers can be obtained.

    “Depending on the provenance of the PHB depolymerase, either monomer and dimer of 3-hydroxybutyric acid 497 or oligomers can be obtained.[498][499][500]”

    From Catalysis as an Enabling Science for Sustainable Polymers (2018) · cites this paper as [497]

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Authors
Mukai, K., Yamada, K., & Doi, Y.
Affiliations
RIKEN (JP)
Corresponding author
Doi, Yoshiharu
Venue
International Journal of Biological Macromolecules
Publisher
Elsevier BV
Published
1993-12
Volume
15
Issue
6
Pages
361-366
ISSN
0141-8130 (ISSN-L)
OpenAlex
W2019749929
Cited by
143
References
27
Citations by year
2026: 1 · 2025: 5 · 2024: 8 · 2023: 8 · 2022: 4 · 2021: 7 · 2020: 5 · 2019: 2 · 2018: 3 · 2017: 7 · 2016: 2 · 2015: 2 · 2014: 3 · 2013: 2 · 2012: 3
FWCI
4.18
Type
journal article
Language
en
Open access
closed
Locations
  • International Journal of Biological Macromolecules (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Physical Sciences › Materials Science › Biomaterials › biodegradable polymer synthesis and properties
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
  • Physical Sciences › Environmental Science › Pollution › Microbial bioremediation and biosurfactants
Keywords
poly[(R)-3-hydroxybutyrate], PHA depolymerase, enzyme kinetics, enzyme mechanism, Alcaligenes faecalis, Comamonas testosteroni, beta-hydroxybutyrate, enzyme adsorption, binding domain, catalytic domain, biodegradable plastics
MeSH terms
Polyhydroxybutyrates, Alcaligenes, Carboxylic Ester Hydrolases, Hydrolysis, Hydroxybutyrates, Kinetics, Polyesters, Pseudomonas, Solubility

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