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Substrate and binding specificities of bacterial polyhydroxybutyrate depolymerases
Abstract
The substrate specificities of three extracellular polyhydroxybutyrate (PHB) depolymerases from Alcaligenes faecalis (PhaZ Afa), Pseudomonas stutzeri (PhaZ Pst), and Comamonas acidovorans (PhaZ Cac), which are grouped into types A and B based on the position of a lipase box sequence in the catalytic domain, were examined for films of 12 different aliphatic polyesters. Each of these PHB depolymerases used was capable of hydrolyzing poly(3-hydroxybutyrate) (P(3HB)), poly(3-hydroxypropionate) (P(3HP)), poly(4-hydroxybutyrate) (P(4HB)), poly(ethylene succinate) (PESU), and poly(ethylene adipate) (PEA) but could not hydrolyze another seven polyesters. In addition, the binding characteristics of substrate binding domains from PhaZ Afa, PhaZ Cac, and PHB depolymerase from Comamonas testosteroni (PhaZ Cte) were studied by using fusions with glutathione S-transferase (GST). All of fusion proteins adsorbed strongly on the surfaces of polyester granules of P(3HB), P(3HP), and poly(2-hydroxypropionate) (P(2HP)) which was not hydrolyzed by the PHB depolymerases used in this study, while they did not bind on Avicel and chitin granules. The adsorption kinetics of the fusion proteins to the surface of P(3HB) and P(2HP) granules were found to obey the Langmuir isotherm. The cross-area per molecule of fusion protein bound to P(3HB) granules was estimated to be 12+/-4 nm2/molecule. It has been suggested that the active sites in catalytic domains of PHB depolymerases have a similar conformational structure, and that several amino acids in substrate-binding domains of PHB depolymerases interact specifically with the surface of polyesters.
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“PHA depolymerases usually exhibit a catalytic domain containing an esterase sequence -often similar to lipase -and a substrate-binding domain (SBD) to enable adsorption of the enzyme at the surface of hydrophobic PHAs.493”
From Catalysis as an Enabling Science for Sustainable Polymers (2018) · cites this paper as [493]
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“The rates for the best depolymerase/polyester pairs were up to 0.28 g/h/cm 2 .”
From Catalysis as an Enabling Science for Sustainable Polymers (2018) · cites this paper as [493]
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Metadata
- Authors
- Kasuya, K.-I., Ohura, T., Masuda, K., & Doi, Y.
- Affiliations
- RIKEN (JP)
- Saitama University (JP)
- Corresponding author
- Doi, Yoshiharu
- Venue
- International Journal of Biological Macromolecules
- Publisher
- Elsevier BV
- Published
- 1999-05
- Volume
- 24
- Issue
- 4
- Pages
- 329-336
- ISSN
- 0141-8130 (ISSN-L)
- OpenAlex
- W2027297590
- Cited by
- 104
- References
- 38
- Citations by year
- 2026: 3 · 2025: 9 · 2024: 5 · 2023: 7 · 2022: 5 · 2021: 5 · 2020: 4 · 2019: 3 · 2018: 1 · 2017: 4 · 2016: 4 · 2015: 3 · 2014: 1 · 2013: 2 · 2012: 3
- FWCI
- 4.43
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- International Journal of Biological Macromolecules (publishedVersion)
- PubMed (publishedVersion)
- Tokyo Tech Research Repository (Tokyo Institute of Technology) (submittedVersion)
- Funders
- Japan Science and Technology Corporation
- Core Research for Evolutional Science and Technology
- Topics
- Physical Sciences › Materials Science › Biomaterials › biodegradable polymer synthesis and properties
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Physical Sciences › Environmental Science › Pollution › Microbial bioremediation and biosurfactants
- Keywords
- polyhydroxybutyrate depolymerase, substrate specificity, aliphatic polyesters, polyhydroxybutyrate, poly-4-hydroxybutyrate, poly(ethylene succinate), poly(ethylene adipate), substrate-binding domain, protein adsorption kinetics, Langmuir isotherm, Alcaligenes faecalis, Pseudomonas stutzeri, Comamonas acidovorans, Comamonas testosteroni, extracellular enzymes
- MeSH terms
- Polyhydroxybutyrates, Adsorption, Alcaligenes, Amino Acid Sequence, Binding Sites, Carboxylic Ester Hydrolases, Hydrolysis, Hydroxybutyrates, Molecular Sequence Data, Polyesters, Pseudomonas, Recombinant Fusion Proteins, Substrate Specificity, Gram-Negative Aerobic Rods and Cocci, Sequence Homology, Amino Acid
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