Study of PcpD Enzyme in Biodegradation of Pentachlorophenol
Author Information
Author(s): Chen Lifeng, Yang Jian
Primary Institution: University of Saskatchewan
Hypothesis
Can the tetrachlorobenzoquinone reductase (PcpD) effectively degrade pentachlorophenol (PCP) despite its expected resistance to biodegradation?
Conclusion
PcpD has low but statistically significant activity in reducing tetrachlorobenzoquinone, regulated by both tetrachlorohydroquinone and PCP.
Supporting Evidence
- PcpD exhibited low but statistically significant activity in reducing tetrachlorobenzoquinone.
- The optimal pH for PcpD activity was found to be 7.0.
- PcpD was inhibited by PCP in a concentration-dependent manner.
Takeaway
Scientists studied an enzyme that helps break down a harmful chemical in the environment, and found it works better under certain conditions.
Methodology
The study involved cloning, expressing, and purifying the PcpD enzyme from Sphingobium chlorophenolicum, followed by enzyme activity assays.
Limitations
The enzyme was purified from inclusion bodies, which may affect its activity.
Statistical Information
P-Value
p<0.0001
Statistical Significance
p<0.0001
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