Improved Decomposition Efficiency of Cutinase from Thielavia terrestris via Random Mutagenesis

초록

Cutinase , an enzyme found in fungi, bacteria, and plants, is crucial for breaking down cutin , a major component of plant cuticles. Beyond this natural role, cutinase has great potential as an eco friendly agent for degrading plastics like PCL, PLA, and PET. The fungus Thielavia terrestris , known for thriving at high temperatures, is a promising source of cutinase for efficient plastic breakdown in hot conditions. However, to enhance the thermal stability and efficiency of cutinase from Thielavia terrestris , further research is needed. This study focused on creating mutant cutinases by incorporating sequences from similar fungal cutinases and expressing them in Escherichia coli . The pelB gene was used to encode a signal peptide for extracellular expression, and PCL on agar plates was utilized for screening. The T124A mutant showed improved enzyme activity and thermal stability at both optimal and elevated temperatures, effectively degrading PCL films. This research supports the development of sustainable plastic degradation strategies, with significant implications for waste management and environmental protection.