Purification and Partial characterization of manganese peroxidase from Bacillus pumilus AND Paenibacillus sp

Area of Science:

• Biotechnology
• Enzymology
• Microbial Physiology

Background:

• Manganese peroxidase (MnP) is a key enzyme in lignin biodegradation.
• Investigating MnP production in Bacillus pumilus and Paenibacillus sp. is essential for understanding their enzymatic capabilities.
• Optimizing MnP production requires identifying effective inducers and optimal reaction conditions.

Purpose of the Study:

• To evaluate the effect of various inducers on MnP production by Bacillus pumilus and Paenibacillus sp.
• To characterize the purified MnP enzymes from both bacterial species.
• To determine the optimal pH and temperature for MnP activity.

Main Methods:

• Enzyme production was induced using indulin AT, guayacol, veratryl alcohol, and lignosulfonic acids.
• Purification of MnP was performed using phenyl sepharose chromatography.
• Enzyme activity was measured across a range of pH (5.0-10.0) and temperatures (30-60 °C).
• Molar masses were determined using SDS-PAGE electrophoresis.

Main Results:

• Indulin AT significantly increased Bacillus pumilus MnP activity to 31.66 U/L within 8 hours.
• Paenibacillus sp. reached maximum MnP activity of 12.22 U/L after 20 hours without significant improvement from indulin AT.
• Purified MnPs exhibited maximum activities of 4.3 U/L at pH 8.0 and 25 °C (B. pumilus) and 11.74 U/L at pH 9.0 and 35 °C (Paenibacillus sp.).
• Molar masses of the purified enzymes were 25 kDa for B. pumilus and 40 kDa for Paenibacillus sp.

Conclusions:

• Indulin AT is an effective inducer for Bacillus pumilus MnP production.
• Optimal conditions for MnP activity vary between Bacillus pumilus and Paenibacillus sp.
• The characterized MnPs possess distinct properties, suggesting potential for specific biotechnological applications in lignin degradation.