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Iyer, Srividya; Shah, Ruchir; Sharma, Ashima; Jendrossek, Dieter; Desai, Anjana J.

doi:10.1023/a:1015249811314

Cited by 29 publications

(9 citation statements)

References 11 publications

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“…S2 (PhaZ Pen ) is distinct to other eukaryotic depolymerases in its M r , glycosylation and similar to other fungal depolymerases in terms of pH and temperature optima on activity. Production of 3HB monomer from PHB with PhaZ Pen as the main hydrolysis product is also comparable to that of the 3HB monomer produced by PhaZ Afu [9] and A. fumigatus Pdf1 [10]. The enzyme also shows distinct behaviour towards different inhibitors tested, which suggests the role of serine, serine residue, carboxyl group, tyrosine and sulfhydryl groups in its active site.…”

Section: Conclusion and Future Prospectssupporting

confidence: 54%

“…According to the literature, the yield of PHB depolymerase after purification was 66% from P. funiculosum [6], 27% from A. faecalis [19], 42% from Pseudomonas sp. [20], 66% from A. fumigatus [9], 73.5% from Aureobacterium saperdae [21], 61% from P. simplicissimum and 86.11% from A. fumigatus Pdf1 [8,10]. The purification fold was found to be 4.5 for P. funiculosum [6] The purity and homogeneity of the enzyme were confirmed by activity (Fig.…”

Section: Resultsmentioning

confidence: 98%

“…2 Time course production of PHB depolymerise by P. citrinum S2 Fig 1 a P. citrinum (stained with lactophenol cotton blue). b PHB clearance by P. citrinum S2; "Z" indicates zone of clearance P. funiculosum [6], P. pinophilum [7], P. simplicissimum [8], A. fumigatus Pdf1 [10], and bacterial PHB depolymerase [9,12,[19][20][21][22], all of which showed a single polypeptide of different molecular weights. Only the poly(3-hydroxyoctanoate) (PHO) depolymerase of Pseudomonas fluorescens GK13 is composed of two identical polypeptides (M r , 26,000) [23].…”

Section: Resultsmentioning

confidence: 99%

“…Carbohydrates were not detected in the PHB depolymerase either from A. fumigatus or from A. saperdae [9,21]. However, the fungal PHB depolymerase from P. funiculosum [6], P. simplicissimum [8] and A. fumigatus Pdf1 [10] were glycosylated.…”

Section: Resultsmentioning

confidence: 99%

“…PNP-acetate and PNP-butyrate were hydrolyzed efficiently by the PHB depolymerase of E. minima [11] and A. fumigatus Pdf1 [10].…”

Section: Resultsmentioning

confidence: 99%

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Purification, Characterization and Kinetic Studies of a Novel Poly(β) Hydroxybutyrate (PHB) Depolymerase PhaZ Pen from Penicillium citrinum S2

Shivakumar

Jani

Zatakia

et al. 2011

Appl Biochem Biotechnol

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A fungal isolate, identified as Penicillium citrinum S2, produced ≈1 U/mL of PHB depolymerase by 72 h when grown in BHM containing 0.2%, w/v PHB, pH 6.0 at 30 °C. Partial purification of an extracellular poly(-β-)hydroxybutyrate (PHB) depolymerase PhaZ( Pen ) from P. citrinum S2 by two steps using ammonium sulphate (80% saturation) and affinity chromatography using concanavalin A yielded 16.18-fold purity and 21.53% recovery of protein. The enzyme was composed of three polypeptide chains of 66, 43 and 20 kDa, respectively, as determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. All the three bands stained positive for glycoprotein by PAS staining. Optimum enzyme activity was detected at pH 6.0 and 50 °C. The enzyme was stable between pH 4.0 and 7.0 at 50 °C, 2 h. β-hydroxybutyrate monomer was detected as the major end product of PHB hydrolysis. The enzyme also showed distinct behaviour towards different inhibitors tested, which suggests the role of serine, serine residue, carboxyl group, tyrosine and sulfhydryl groups in its active site.

show abstract

Section: Conclusion and Future Prospectssupporting

confidence: 54%

Section: Resultsmentioning

confidence: 98%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

“…PNP-acetate and PNP-butyrate were hydrolyzed efficiently by the PHB depolymerase of E. minima [11] and A. fumigatus Pdf1 [10].…”

Section: Resultsmentioning

confidence: 99%

See 3 more Smart Citations

Purification, Characterization and Kinetic Studies of a Novel Poly(β) Hydroxybutyrate (PHB) Depolymerase PhaZ Pen from Penicillium citrinum S2

Shivakumar

Jani

Zatakia

et al. 2011

Appl Biochem Biotechnol

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Biodegradation of microbial and synthetic polyesters by fungi

Kim

Rhee

2003

Appl Microbiol Biotechnol

221

102

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A variety of biodegradable polyesters have been developed in order to obtain useful biomaterials and to reduce the impact of environmental pollution caused by the large-scale accumulation of non-degradable waste plastics. Polyhydroxyalkanoates, poly(epsilon-caprolactone), poly( l-lactide), and both aliphatic and aromatic polyalkylene dicarboxylic acids are examples of biodegradable polyesters. In general, most aliphatic polyesters are readily mineralized by a number of aerobic and anaerobic microorganisms that are widely distributed in nature. However, aromatic polyesters are more resistant to microbial attack than aliphatic polyesters. The fungal biomass in soils generally exceeds the bacterial biomass and thus it is likely that fungi may play a considerable role in degrading polyesters, just as they predominantly perform the decomposition of organic matter in the soil ecosystem. However, in contrast to bacterial polyester degradation, which has been extensively investigated, the microbiological and environmental aspects of fungal degradation of polyesters are unclear. This review reports recent advances in our knowledge of the fungal degradation of microbial and synthetic polyesters and discusses the ecological importance and contribution of fungi in the biological recycling of waste polymeric materials in the biosphere.

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An extracellular polyhydroxybutyrate depolymerase in Thermus thermophilus HB8

Papaneophytou

Pantazaki

Kyriakidis

2009

Appl Microbiol Biotechnol

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The thermophilic bacterium Thermus thermophilus HB8 has been characterized as a polyhydroxybutyrate (PHB)-degrading microorganism since it grows efficiently and forms clear zones on agar plates containing PHB as sole carbon source. T. thermophilus extracellular PHB depolymerase was purified to homogeneity using an affinity chromatography protocol. The purified enzyme was estimated to have an apparent molecular mass of 42 kDa. The extracellular PHB depolymerase gene was identified as the TTHA0199 gene product of T. thermophilus HB8. The amino acid sequence of the TTHA0199 gene product shared significant homologies to other carboxylesterases. A catalytic triad was identified consisting of S(183), E(310), and H(405). A pentapeptide sequence (GX(1)SX(2)G) exists within the molecule, characteristic for PHB depolymerases (lipase box) and for other serine hydrolases. Purified extracellular PHB depolymerase was stable at high temperatures with an optimum activity at pH 8.0. The apparent Km value of the purified enzyme for PHB was 53 microg/ml. As the main product of the enzymic hydrolysis of PHB, the monomer 3-hydroxybutyrate was identified, suggesting that the enzyme acts principally as an exo-type hydrolase.

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Untitled

Cited by 29 publications

References 11 publications

Purification, Characterization and Kinetic Studies of a Novel Poly(β) Hydroxybutyrate (PHB) Depolymerase PhaZ Pen from Penicillium citrinum S2

Purification, Characterization and Kinetic Studies of a Novel Poly(β) Hydroxybutyrate (PHB) Depolymerase PhaZ Pen from Penicillium citrinum S2

Biodegradation of microbial and synthetic polyesters by fungi

An extracellular polyhydroxybutyrate depolymerase in Thermus thermophilus HB8

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