Fungal Cellulase Variants With Improved Stability

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Solution Overview

Problem

Current cellulases used in industrial applications, such as textile treatment and detergents, lack improved stability and performance, particularly in the presence of proteases, which affects their long-term effectiveness.

Innovation Solution

Development of novel variants of GH45 cellulases with specific amino acid substitutions at positions 167, 210, 215, 220, and 225, which enhance stability and performance, including improved color revival and color maintenance in detergents containing proteases.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Reliability

If conventional cellulases are used in detergent applications, then basic cleaning function is provided, but stability in the presence of proteases deteriorates

Engineering Contradiction:
ImprovestabilityVSAvoidperformance in varying industrial applications
Core Design Contradiction:
ReliabilityVSAdaptability or versatility

Solution Approach 1:

The patent applies parameter changes by modifying amino acid residues at specific positions (167, 210, 215, 220, and 225) in the GH45 cellulase sequence. These sequence parameter changes result in variants with improved stability in protease-containing detergents while maintaining cellulolytic activity, directly resolving the contradiction between stability and adaptability

Inventive Principle:
Principle #35Parameter changes

2Duration of action of moving object

If parental cellulase is used, then initial activity is achieved, but long-term effectiveness deteriorates

Engineering Contradiction:
Improvelong-term effectivenessVSAvoidstability
Core Design Contradiction:
Duration of action of moving objectVSReliability

Solution Approach 1:

The patent introduces amino acid substitutions at positions 167, 210, 215, 220, and 225 to create cellulase variants that maintain their catalytic activity and structural integrity over extended periods in detergent formulations, thereby improving both long-term effectiveness and stability

Inventive Principle:
Principle #35Parameter changes

3Productivity

If standard cellulase variants are used, then basic color revival is achieved, but enhanced color maintenance and antigreying properties are not obtained

Engineering Contradiction:
Improvecolor revival performanceVSAvoidcolor maintenance stability
Core Design Contradiction:
ProductivityVSReliability

Solution Approach 1:

The patent modifies the cellulase sequence at specific positions to enhance color maintenance and antigreying properties while maintaining color revival performance, achieving improved productivity in textile treatment applications without sacrificing reliability

Inventive Principle:
Principle #35Parameter changes

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 novel variants demonstrate significantly improved stability and performance compared to parental enzymes, maintaining activity and effectiveness over time, even in protease-containing detergents, with enhanced color revival and antigreying properties.

Implementation Method 1

cellulases are enzymes having cellulolytic activity, which means that they are capable of hydrolysing cellulosic substrates or derivatives thereof into smaller saccharides

Methodology Applied
Scientific EffectEnzymatic hydrolysis: Enzyme

Data Source

PatentUS20220002697A1Fungal Cellulase Variants With Improved Stability
Publication Date: 2022.01.06 SESAM BIOTECH
  • US20220002697A1 patent drawing
  • US20220002697A1 patent drawing
  • US20220002697A1 patent drawing

AI summary

The invention relates to novel variants of fungal endoglucanases. The invention further relates to enzyme preparations and detergent compositions comprising the variant as well as to processes for treating cellulosic material with the variant. The variants have depilling, antipilling and/or antigreying performance, and improved stability in the presence of proteases.