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A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes

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Published on: November 7, 2012

Engineering hyperthermostability into a GH11 xylanase is mediated by subtle changes to protein structure.

Claire Dumon¹, Alexander Varvak, Mark A Wall

¹Institute for Cell and Molecular Biosciences, Newcastle University, The Medical School, Newcastle Upon Tyne NE2 4HH, United Kingdom.

The Journal of Biological Chemistry

|June 3, 2008

Summary

Researchers engineered a hyperthermostable xylanase enzyme using directed evolution. This enhanced enzyme shows a significant increase in thermal stability with subtle structural changes, crucial for industrial applications.

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Area of Science:

Biochemistry
Protein Engineering
Enzymology

Background:

Protein thermostability is vital for industrial enzymes like xylanases used in high-temperature processes.
Understanding the structural basis of thermostability can lead to improved enzyme applications.

Purpose of the Study:

To generate hyperthermostable variants of the thermophilic GH11 xylanase, EvXyn11, using directed protein evolution.
To investigate the structural and molecular basis for enhanced protein thermostability.

Main Methods:

Directed protein evolution using Gene Site Saturation Mutagenesis (GSSM) to identify thermostable mutations.
Screening of single mutants and combinatorial libraries to isolate hyperthermostable variants.
Crystal structure determination of the parent and hyperthermostable xylanase variants.

Main Results:

Identified 15 thermostable mutants with melting temperatures (Tm) 1-8°C higher than the parent enzyme.
Developed a hyperthermostable variant, EvXyn11TS, with seven mutations, exhibiting a Tm ~25°C higher than the parent.
Observed subtle structural changes, primarily T13F and S9P mutations, contributing to increased thermostability without significantly altering catalytic properties.

Conclusions:

The molecular basis for enhanced thermostability in EvXyn11TS is subtle, involving minor changes in hydrophobic interactions and loop conformation.
Directed evolution is effective in generating hyperthermostable enzymes with industrially relevant properties.
Further research with advanced tools is needed to fully elucidate protein folding mechanisms at non-ambient temperatures.