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Production and characterization of poly(3-hyroxybutyrate) depolymerases from Aspergillus sp. isolated from soil that could degrade poly(3-hydroxybutyrate)

Research Paper | August 1, 2015

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Akhtar Nadhman, Fariha Hasan, Aamer Ali Shah

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Int. J. Biosci.7( 2), 25-28, August 2015

DOI: http://dx.doi.org/10.12692/ijb/7.2.25-28


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The degradation ability of Aspergillus sp. strain NA-25 was determined against poly (3-hydroxybutyrate) (PHB), since it was previously tested against co-polymer poly(3-hydroxybutyrate-co-3-hydroxyvalerate). PHB depolymerase enzymes were produced from strain NA-25 at 45oC and pH 7.0 after 96h of incubation. The enzymes were purified to homogeneity through column chromatography using Sephadex G-75 gel, as indicated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Four bands of different molecular sizes, approximately 48, 75, 80 and 85 kDa, were found which revealed that strain NA-25 was producing 4 types of PHB depolymerases. The enzymes utilized p-nitrophenyl caproate (C6) as preferred substrate among various p-NP-acyl esters, indicating that these are a type of esterases, therefore, designated as Aest and numbered as Aest-1–4, respectively. The enzymes were stable at wide range of temperature (37–60°C) and pH (6–9). All the PHB depolymerases were stable in the presence of different metal ions except enzyme Aest-4. Ethylenediamine teteracetic acid (EDTA), β-mercaptoethanol and sodium dodecyl sulphate (SDS) inhibited the activity of all depolymerases. PHB depolymerases were related to the serine group of hydrolases, as indicated by the inhibitory effect of phenylmethyl sulphonyl fluoride (PMSF) against all the depolymerases. The enzymes from Aspergillus sp. strain NA-25 could degrade aliphatic polyesters; therefore, it might be applied for bioremediation in the polyesters-contaminated environments.


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Production and characterization of poly(3-hyroxybutyrate) depolymerases from Aspergillus sp. isolated from soil that could degrade poly(3-hydroxybutyrate)

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