PET-Degrading Esterase Variants With Targeted Amino Acid Changes

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Solution Overview

Problem

There is a need for esterases with improved activity to enhance the efficiency of plastic waste degradation processes, particularly for polyethylene terephthalate (PET), as existing esterases are not sufficiently effective in degrading plastics and recycling their components.

Innovation Solution

Development of novel esterase variants with specific amino acid modifications, such as substitutions at positions F208, T157, T176, S65, A62, N85, T86, R89, A178, P179, S206, or N211, which exhibit increased activity and thermostability, allowing for more efficient degradation of PET and other polyesters.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Productivity

If conventional esterases are used for PET degradation, then the process can proceed with existing enzyme technology, but the degradation efficiency is insufficient and the process competitiveness is reduced

Engineering Contradiction:
Improvepolyester degradation efficiencyVSAvoidprocess competitiveness
Core Design Contradiction:
ProductivityVSReliability

Solution Approach 1:

The patent applies parameter changes by modifying amino acid residues at specific positions (F208, T157, T176, S65, A62, N85, T86, R89, A178, P179, S206, N211) in the esterase protein structure. These molecular-level parameter changes result in enhanced catalytic activity and thermostability, directly improving polyester degradation efficiency and process competitiveness

Inventive Principle:
Principle #35Parameter changes

2Productivity

If esterase variants with amino acid substitutions are developed, then polyester degrading activity and thermostability are enhanced, but the enzyme structure becomes more complex

Engineering Contradiction:
Improvespecific activityVSAvoidenzyme structure complexity
Core Design Contradiction:
ProductivityVSDevice complexity

Solution Approach 1:

The patent applies local quality by introducing specific amino acid substitutions at targeted positions (F208, T157, T176, S65, etc.) within the esterase molecule rather than redesigning the entire enzyme structure. This localized modification approach enhances catalytic activity and thermostability while maintaining the overall protein architecture and minimizing structural complexity

Inventive Principle:
Principle #3Local quality

Applied Scientific Principles

This section explains which scientific principles are used to turn an abstract innovation direction into a practical engineering solution.

Function Achieved in This Case

The modified esterase variants demonstrate enhanced polyester degrading activity, with increased specific activity and thermostability, enabling more effective plastic degradation and recycling of PET materials.

Implementation Method 1

enzymes may accelerate hydrolysis of polyester containing material, and more particularly of plastic products

Methodology Applied
Scientific EffectHydrolysis: Hydrolysis

Implementation Method 2

Esterases are able to catalyze the hydrolysis of a variety of polymers, including polyesters

Methodology Applied
Scientific EffectCatalysis: Catalysis

Data Source

PatentEP3485006B1Novel esterases and uses thereof
Publication Date: 2025.10.29 CARBIOS

AI summary

The present invention relates to novel esterase, more particularly to esterase variants having improved activity compared to the esterase of SEQ ID N° 1 and the uses thereof for degrading polyester containing material, such as plastic products. The esterases of the invention are particularly suited to degrade polyethylene terephthalate, and material containing polyethylene terephthalate.