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Methanol Independent Expression by Pichia Pastoris Employing De-repression Technologies

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An Inferred Ancestral CotA Laccase with Improved Expression and Kinetic Efficiency.

Lei Lei¹, Lijun Zhao¹, Yiqia Hou¹

¹School of Life Science and Technology, Wuhan Polytechnic University, Wuhan 430023, China.

International Journal of Molecular Sciences

|July 14, 2023

Summary

Researchers resurrected ancestral laccase sequences to improve enzyme stability and expression. The best variant, AncCotA2, showed enhanced catalytic rates and stability, offering potential for industrial applications.

Keywords:

ancestral sequence inferring dye decolorization heat-resistant laccase pH stability

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Area of Science:

Biotechnology
Enzyme Engineering
Industrial Microbiology

Background:

Laccases are vital industrial enzymes due to their eco-friendly nature and broad substrate range.
Challenges remain in enhancing laccase stability and expression for industrial demands.

Purpose of the Study:

To resurrect ancestral laccase sequences for improved stability and expression.
To engineer a superior laccase variant for industrial applications.

Main Methods:

Resurrection of five ancestral laccase BsCotA sequences and homologues.
Expression of variants in *Escherichia coli* to assess functionality and expression levels.
Characterization of catalytic rates, thermal stability, and acidic stability.

Main Results:

All five resurrected variants showed improved soluble and functional expression in *E. coli*.
Three variants demonstrated enhanced catalytic rates, thermal, and acidic stabilities.
AncCotA2 exhibited a 5.2-fold higher k/K value than wild-type BsCotA, with superior stability and dye decolorization.

Conclusions:

Ancestral sequence resurrection is a viable strategy for improving laccase properties.
AncCotA2 presents significant potential for industrial applications due to its enhanced performance.
This study provides a foundation for further enzyme engineering of laccases.