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Extracellular Polyhydroxyalkanoate Depolymerase by Acidovorax sp. DP5.

Vigneswari S, Lee TS, Bhubalan K, Amirul AA - Enzyme Res (2015)

Bottom Line: The highest degradation activity of P(3HB) was also observed with depolymerase enzyme of DP5 in mineral salt medium containing P(3HB).Based on biochemical characterization and 16S rRNA cloning and sequencing, isolate DP5 was found to belong to the genus Acidovorax and subsequently named as Acidovorax sp.The highest extracellular depolymerase enzyme activity was achieved when 0.25% (w/v) of P(3HB) and 1 g/L of urea were used as carbon and nitrogen source, respectively, in the culture media.

View Article: PubMed Central - PubMed

Affiliation: Malaysian Institute of Pharmaceuticals and Nutraceuticals, NIBM, MOSTI, 11700 Penang, Malaysia ; Institute of Marine Biotechnology, Universiti Malaysia Terengganu, 21030 Kuala Terengganu, Malaysia.

ABSTRACT
Bacteria capable of degrading polyhydroxyalkanoates (PHA) by secreting extracellular depolymerase enzymes were isolated from water and soil samples collected from various environments in Malaysia. A total of 8 potential degraders exhibited clear zones on poly(3-hydroxybutyrate) [P(3HB)] based agar, indicating the presence of extracellular PHA depolymerase. Among the isolates, DP5 exhibited the largest clearing zone with a degradation index of 6.0. The highest degradation activity of P(3HB) was also observed with depolymerase enzyme of DP5 in mineral salt medium containing P(3HB). Based on biochemical characterization and 16S rRNA cloning and sequencing, isolate DP5 was found to belong to the genus Acidovorax and subsequently named as Acidovorax sp. DP5. The highest extracellular depolymerase enzyme activity was achieved when 0.25% (w/v) of P(3HB) and 1 g/L of urea were used as carbon and nitrogen source, respectively, in the culture media. The most suitable assay condition of the depolymerase enzyme in response to pH and temperature was tested. The depolymerase produced by strain Acidovorax sp. DP5 showed high percentage of degradation with P(3HB) films in an alkaline condition with pH 9 and at a temperature of 40°C.

No MeSH data available.


Related in: MedlinePlus

Effect of P(3HB) concentration (w/v) on the (a) bacterial growth and (b) enzyme activity. Values are mean of two replicates.
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Related In: Results  -  Collection


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fig3: Effect of P(3HB) concentration (w/v) on the (a) bacterial growth and (b) enzyme activity. Values are mean of two replicates.

Mentions: Growth of Acidovorax sp. DP5 and its depolymerase enzyme activity was further evaluated by manipulating the concentration of P(3HB) and nitrogen source. DP5 was cultivated in MSM containing different concentration of P(3HB) [0.1%–0.75% w/v] as the sole carbon source. Based on the result obtained in Figure 3(a), maximum growth was obtained at the highest concentration of P(3HB). It was clearly observed that the growth of Acidovorax sp. DP5 was proportional with concentration of P(3HB). At P(3HB) concentration of 0.75%, the growth of cells increased almost 4-fold from 12 to 48 h of cultivation. The growth of DP5 was almost reaching stationary phase after 72 h. In contrary, it was found that feeding of a low concentration of P(3HB) as substrate favored the high activity of depolymerase enzyme (Figure 3(b)).


Extracellular Polyhydroxyalkanoate Depolymerase by Acidovorax sp. DP5.

Vigneswari S, Lee TS, Bhubalan K, Amirul AA - Enzyme Res (2015)

Effect of P(3HB) concentration (w/v) on the (a) bacterial growth and (b) enzyme activity. Values are mean of two replicates.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4664802&req=5

fig3: Effect of P(3HB) concentration (w/v) on the (a) bacterial growth and (b) enzyme activity. Values are mean of two replicates.
Mentions: Growth of Acidovorax sp. DP5 and its depolymerase enzyme activity was further evaluated by manipulating the concentration of P(3HB) and nitrogen source. DP5 was cultivated in MSM containing different concentration of P(3HB) [0.1%–0.75% w/v] as the sole carbon source. Based on the result obtained in Figure 3(a), maximum growth was obtained at the highest concentration of P(3HB). It was clearly observed that the growth of Acidovorax sp. DP5 was proportional with concentration of P(3HB). At P(3HB) concentration of 0.75%, the growth of cells increased almost 4-fold from 12 to 48 h of cultivation. The growth of DP5 was almost reaching stationary phase after 72 h. In contrary, it was found that feeding of a low concentration of P(3HB) as substrate favored the high activity of depolymerase enzyme (Figure 3(b)).

Bottom Line: The highest degradation activity of P(3HB) was also observed with depolymerase enzyme of DP5 in mineral salt medium containing P(3HB).Based on biochemical characterization and 16S rRNA cloning and sequencing, isolate DP5 was found to belong to the genus Acidovorax and subsequently named as Acidovorax sp.The highest extracellular depolymerase enzyme activity was achieved when 0.25% (w/v) of P(3HB) and 1 g/L of urea were used as carbon and nitrogen source, respectively, in the culture media.

View Article: PubMed Central - PubMed

Affiliation: Malaysian Institute of Pharmaceuticals and Nutraceuticals, NIBM, MOSTI, 11700 Penang, Malaysia ; Institute of Marine Biotechnology, Universiti Malaysia Terengganu, 21030 Kuala Terengganu, Malaysia.

ABSTRACT
Bacteria capable of degrading polyhydroxyalkanoates (PHA) by secreting extracellular depolymerase enzymes were isolated from water and soil samples collected from various environments in Malaysia. A total of 8 potential degraders exhibited clear zones on poly(3-hydroxybutyrate) [P(3HB)] based agar, indicating the presence of extracellular PHA depolymerase. Among the isolates, DP5 exhibited the largest clearing zone with a degradation index of 6.0. The highest degradation activity of P(3HB) was also observed with depolymerase enzyme of DP5 in mineral salt medium containing P(3HB). Based on biochemical characterization and 16S rRNA cloning and sequencing, isolate DP5 was found to belong to the genus Acidovorax and subsequently named as Acidovorax sp. DP5. The highest extracellular depolymerase enzyme activity was achieved when 0.25% (w/v) of P(3HB) and 1 g/L of urea were used as carbon and nitrogen source, respectively, in the culture media. The most suitable assay condition of the depolymerase enzyme in response to pH and temperature was tested. The depolymerase produced by strain Acidovorax sp. DP5 showed high percentage of degradation with P(3HB) films in an alkaline condition with pH 9 and at a temperature of 40°C.

No MeSH data available.


Related in: MedlinePlus