Protease-Stable Cellulase Variants for Detergent Formulations

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Solution Overview

Problem

Existing cellulases are not stable in the presence of proteases and other detergent components, leading to degradation and loss of laundering benefits in detergent compositions.

Innovation Solution

Development of cellulase variants with specific mutations that enhance thermostability and stability in the presence of proteases and other detergent components, such as surfactants, maintaining endoglucanase activity.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Reliability

If cellulase is added to detergent compositions containing proteases and other enzymes, then soil removal and fabric care benefits are improved, but the cellulase is degraded by proteases over time, negating the benefits

Engineering Contradiction:
Improvecellulase stabilityVSAvoidprotease degradation
Core Design Contradiction:
ReliabilityVSObject-generated harmful factors

Solution Approach 1:

The patent applies parameter changes by introducing specific amino acid substitutions at defined positions in the cellulase polypeptide sequence. These molecular-level parameter changes modify the enzyme's structural properties to enhance its resistance to proteolytic degradation while preserving its catalytic activity in detergent formulations.

Inventive Principle:
Principle #35Parameter changes

Solution Approach 2:

The patent creates a composite enzyme system by designing cellulase variants with modified amino acid compositions that combine enhanced protease resistance with maintained endoglucanase activity. The engineered cellulase represents a composite structure integrating stability features with functional catalytic domains.

Inventive Principle:
Principle #40Composite materials

2Reliability

If cellulase variants with improved protease stability are developed through amino acid substitutions, then enzyme stability is improved, but the complexity of enzyme design and characterization increases

Engineering Contradiction:
Improveenzyme stabilityVSAvoidenzyme design complexity
Core Design Contradiction:
ReliabilityVSDevice complexity

Solution Approach 1:

The patent systematically modifies specific parameters of the cellulase molecule by substituting amino acids at predetermined positions. This structured approach to parameter change enables improved stability while managing design complexity through focused modifications rather than comprehensive redesign.

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 cellulase variants exhibit improved stability and activity under detergent conditions, effectively removing soil, preventing pill formation, and enhancing fabric softness and appearance.

Implementation Method 1

cellulase enzymes that catalyze the hydrolysis of beta-1,4glycosidic linkages in cellulose to break it down into monosaccharides or shorter polysaccharides and oligosaccharides

Methodology Applied
Scientific EffectHydrolysis: Hydrolysis

Data Source

PatentEP3555279B1Polypeptides with endoglucanase activity and uses thereof
Publication Date: 2025.07.23 DANISCO US INC
  • EP3555279B1 patent drawingFigure 1
  • EP3555279B1 patent drawingFigure 2A
  • EP3555279B1 patent drawingFigure 2B

AI summary

Disclosed herein are cellulase variants, or active fragments thereof, and polynucleotides encoding same, wherein the cellulase variants, or active fragments thereof, hav endoglucanase activity. Also disclosed herein are compositions comprising said cellulase variants, or active fragments thereof; vectors and/or host cells comprising the polynucleotides encoding said cellulase variants, or active fragments thereof; and methods for making and/or using said cellulase variants, or active fragments thereof and/or compositions containing same; wherein said cellulase variants, or active fragments thereof, have endoglucanase activity.