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Updated: May 13, 2026

Directed Evolution Method in Saccharomyces cerevisiae: Mutant Library Creation and Screening

Directed Evolution Method in Saccharomyces cerevisiae: Mutant Library Creation and Screening

Published on: April 1, 2016

Blood tolerant laccase by directed evolution.

Diana M Mate¹, David Gonzalez-Perez, Magnus Falk

¹Department of Biocatalysis, Institute of Catalysis, CSIC, 28049 Madrid, Spain.

Chemistry & Biology

|February 27, 2013

Summary

This summary is machine-generated.

Researchers evolved a fungal laccase to tolerate human blood conditions. This blood-tolerant laccase maintains high redox potential, enabling new biotechnological applications like nanobiodevices and detoxification.

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Area of Science:

Biotechnology
Enzyme Engineering
Biocatalysis

Background:

High-redox potential laccases are versatile biocatalysts.
Adapting enzymes for biological fluids like blood is challenging due to pH and ionic composition.
Thermostable laccases offer a robust starting point for engineering.

Purpose of the Study:

To engineer a thermostable laccase for tolerance to human blood conditions.
To investigate mutations affecting laccase activity and stability in blood.
To demonstrate the feasibility of adapting laccases for extreme biological environments.

Main Methods:

Directed evolution of a thermostable laccase using a surrogate complex blood medium.
Testing evolved laccase activity in human plasma and whole blood.
Analyzing mutations in the second coordination sphere of the T1 copper site.

Main Results:

Successfully evolved a blood-tolerant laccase from a white-rot fungus.
The engineered laccase retained high redox potential at the T1 copper site.
Key mutations shifted the pH optimum and significantly reduced chloride inhibition.

Conclusions:

Laccases can be adapted to function effectively in challenging biological conditions like human blood.
This engineered laccase demonstrates potential for applications in implantable nanobiodevices, chemical synthesis, and detoxification.
Enzyme engineering offers a pathway to overcome limitations for in vivo biocatalysis.