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Kobayashi, T; Sugiyama, Akinori; Kawase, Yoshiyuki; Saito, Terumi; Mergaert, Joris; Swings, Jean

doi:10.1023/a:1021885901119

Cited by 59 publications

(12 citation statements)

References 20 publications

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“…The activity of P(3HB) depolymerase enzyme was measured according to the method of Kobayashi et al (1999) with slight modification. Standard enzyme assay mixture contained a stable suspension of 0.16% P(3HB) granules in 0.1 M phosphate buffer at pH 6.0.…”

Section: Enzyme Activity Assaymentioning

confidence: 99%

Enhanced degradation of polyhydroxyalkanoates (PHAs) by newly isolated Burkholderia cepacia DP1 with high depolymerase activity

Azami

Wirjon²,

Shantini

et al. 2017

3 Biotech

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The contribution of microbial depolymerase has received much attention because of its potential in biopolymer degradation. In this study, the P(3HB) depolymerase enzyme of a newly isolated Burkholderia cepacia DP1 from soil in Penang, Malaysia, was optimized using response surface methodology (RSM). The factors affecting P(3HB) depolymerase enzyme production were studied using one-variable-at-a-time approach prior to optimization. Preliminary experiments revealed that the concentration of nitrogen source, concentration of carbon source, initial pH and incubation time were among the main factors influencing the enzyme productivity. An increase of 9.4 folds in enzyme production with an activity of 5.66 U/mL was obtained using optimal medium containing 0.028% N of di-ammonium hydrogen phosphate and 0.31% P(3HB-co-21%4HB) as carbon source at the initial pH of 6.8 for 38 h of incubation. Moreover, the RSM model showed great similarity between predicted and actual enzyme production indicating a successful model validation. This study warrants the ability of P(3HB) degradation by B. cepacia DP1 in producing higher enzyme activity as compared to other P(3HB) degraders being reported. Interestingly, the production of P(3HB) depolymerase was rarely reported within genus Burkholderia. Therefore, this is considered to be a new discovery in the field of P(3HB) depolymerase production.

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Section: Enzyme Activity Assaymentioning

confidence: 99%

Enhanced degradation of polyhydroxyalkanoates (PHAs) by newly isolated Burkholderia cepacia DP1 with high depolymerase activity

Azami

Wirjon²,

Shantini

et al. 2017

3 Biotech

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“…TP4 according to the method of Kobayashi et al Considering the optimum P(3HB) degradation conditions for the PhaZ aci depolymerase 5 was different from those for PhaZ ral depolymerase, the degradation experiment by the PhaZ aci depolymerase was carried out in 50 mM Tris buffer (pH 8.0) at 30 °C, while that by PhaZ ral has been carried out in 0.1 M potassium phosphate buffer (pH 7.5) at 37 °C . The activity of PHA depolymerase was measured by the decrease in turbidity of a P(3HB) suspension in aqueous buffer solutions . The aqueous solution of PhaZ aci depolymerase prepared had a P(3HB) degradation activity of 50 U/mg.…”

Section: Experimental Partmentioning

confidence: 99%

“…The extracellular PHA depolymerase of Acidovorax Sp. Strain TP4 ( PhaZ aci ) has been purified, and the DNA sequence has been determined . The sequence of this depolymerase is very similar to that of PHA depolymerase of Comamonas acidovorans YM1609 ( PhaZ com ), both of which belong to the type II PHA depolymerase.…”

Section: Introductionmentioning

confidence: 99%

“…Many extracellular poly(3-hydroxyalkanoate) (PHA) depolymerases have been purified from various microorganisms and characterized . More than 10 bacterial PHA depolymerase genes ( PhaZ ) have been cloned and analyzed since 1989. − All PHA depolymerase proteins have composite domain structures and consist of a signal peptide segment, a large catalytic domain at the N terminus, a C-terminal substrate-binding domain, and a linking domain between catalytic and binding domains. Three strictly conserved amino acids, serine, aspartate, and histidine, constitute the active center of the catalytic domain …”

Section: Introductionmentioning

confidence: 99%

“…Considering that the PhaZ aci depolymerase from AcidoVorax Sp. TP4 belongs to the type II, and degrades P(3HP) easier than P(3HB), 5 we wondered whether it would show different degradation behavior with the PhaZ ral PHA depolymerase. The study described in the present report utilized bacterial P(3HB), comonomer-compositionally fractionated P(3HB-co-3HP)s with varied degree of crystallinity and chemosynthesized P(3HP) to provide evidence for similarity and difference between the enzymatic hydrolysis behavior of the extracellular depolymerases PhaZ ral and PhaZ aci , defined as type I and type II, respectively.…”

Section: Introductionmentioning

confidence: 99%

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Enzymatic Hydrolysis of Bacterial Poly(3-hydroxybutyrate-co-3-hydroxypropionate)s by Poly(3-hydroxyalkanoate) Depolymerase from Acidovorax Sp. TP4

et al. 2002

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Enzymatic degradability has been investigated for a series of bacterial poly(3-hydroxybutyrate-co-3-hydroxypropionate)s (P(3HB-co-3HP)s) with 3-hydroxypropionate (3HP) unit contents from 11 to 86 mol % as well as poly(3-hydroxybutyrate) (P(3HB)) and chemosynthesized poly(3-hydroxypropionate) (P(3HP)). The behavior of degradation by two types of extracellular poly(3-hydroxyalkanoate) (PHA) depolymerases purified from Ralstonia pikettii T1 and Acidovorax Sp. TP4, defined respectively as PHA depolymerase types I and II according to the position of the lipase box in the catalytic domain, were compared in relation to the thermal properties and crystalline structures of the PHA samples elucidated by differential scanning calorimetry and wide-angle X-ray diffraction. The degradation products were characterized by high-performance liquid chromatography and one- (1D) and two-dimension (2D) (1)H NMR spectroscopy. It was found that the PHA depolymerase of Acidovorax Sp. TP4 showed degradation behavior different from that shown by depolymerase of R. pikettii T1. PHA depolymerase from Acidovorax Sp. TP4 degraded the P(3HB-co-3HP) films with lower crystallinity in higher rates than those with higher crystallinity, no matter what kinds of crystalline structures they formed. In contrast, PHA depolymerase from R. pikettii T1 degraded P(3HB-co-3HP) films forming P(3HB) crystalline structure in higher rates than those forming P(3HP)s. The increase in amorphous nature of the P(3HB-co-3HP) films with P(3HB)-homopolymer-like crystalline structure increases and then decreases the rate of degradation by depolymerase from R. pikettii T1. The 3-hydroxybutyrate (3HB) monomer was produced as a major product by the hydrolysis of P(3HB) film by PHA depolymerase from Acidovorax Sp. TP4. The P(3HB-co-3HP) films could be degraded into 3HB and 3-hydroxypropionate (3HP) monomer at last, indicating that the catalytic domain of the enzyme recognized at least two monomeric units as substrates. While the PHA depolymerase from R. pikettii T1 hydrolyzed P(3HB) film into 3HB dimer as a major product, and the catalytic domain recognized at least three monomeric units. The degradation behavior of P(3HB-co-3HP) films by the PHA depolymerase of Acidovorax Sp. TP4 could be distinguished from that by the depolymerase of R. pikettii T1.

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Extracellular Polyhydroxyalkanoate (PHA) Depolymerases: The Key Enzymes of PHA Degradation

Jendrossek

2002

Biopolymers Online

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Introduction Historical Outline Identification and Isolation of Extracellular d‐Poly(HA)‐Degrading Microorganisms Characterization of Poly(HA)‐Degrading Microorganisms Biochemical Properties of Extracellular d‐Poly(HA) Depolymerases Molecular Biology and Functional Analysis of d‐Poly(3HA SCL ) Depolymerases PhaZ7, a new Type of Thermoalkalophilic Hydrolase of P. lemoignei with high Specificity for Amorphous Poly(HA SCL ) Molecular Biology and Functional Analysis of d‐Poly(HA MCL ) Depolymerases Enantioselectivity and Hydrolysis Products of Poly(HA) Depolymerases Regulation of Poly(HA) Depolymerase Synthesis Influence of Physico‐chemical Properties of the Polymer on its Biodegradability Outlook and Perspectives Patents Acknowledgments

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Untitled

Cited by 59 publications

References 20 publications

Enhanced degradation of polyhydroxyalkanoates (PHAs) by newly isolated Burkholderia cepacia DP1 with high depolymerase activity

Enhanced degradation of polyhydroxyalkanoates (PHAs) by newly isolated Burkholderia cepacia DP1 with high depolymerase activity

Enzymatic Hydrolysis of Bacterial Poly(3-hydroxybutyrate-co-3-hydroxypropionate)s by Poly(3-hydroxyalkanoate) Depolymerase from Acidovorax Sp. TP4

Extracellular Polyhydroxyalkanoate (PHA) Depolymerases: The Key Enzymes of PHA Degradation

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