Detergent Protease Variants for Storage-Stable Cleaning Activity

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Solution Overview

Problem

Existing proteases in detergents and cleaning agents, particularly textile detergents, suffer from insufficient catalytic activity and stability under standard cleaning conditions and during storage, leading to inadequate cleaning performance on protease-sensitive soils.

Innovation Solution

A protease with specific amino acid substitutions, such as N121F, A194C, A209V, T218I, and N237P, is developed to enhance its storage stability and catalytic activity, maintaining higher residual activity even after storage in detergents.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Reliability

If conventional proteases are used in detergents, then cleaning function is provided, but storage stability is insufficient

Engineering Contradiction:
Improvestorage stabilityVSAvoidcatalytic activity
Core Design Contradiction:
ReliabilityVSProductivity

Solution Approach 1:

The patent applies parameter changes by modifying specific amino acid residues in the protease sequence (positions 121, 194, 209, 218, and 237) to alter the enzyme's physical and chemical properties. These sequence modifications change the protease's stability parameters without compromising its catalytic function, allowing it to maintain activity during storage while preserving cleaning effectiveness.

Inventive Principle:
Principle #35Parameter changes

Solution Approach 2:

The invention applies local quality by making targeted modifications at specific locations (amino acid positions) within the protease molecule rather than changing the entire enzyme. The substitutions at positions 121, 194, 209, 218, and 237 are strategically selected to improve storage stability while maintaining the overall catalytic structure and function of the protease.

Inventive Principle:
Principle #3Local quality

2Duration of action of stationary object

If proteases are stored in detergent formulations, then cleaning performance is maintained, but residual activity decreases over time

Engineering Contradiction:
Improveresidual activity during storageVSAvoidcleaning performance
Core Design Contradiction:
Duration of action of stationary objectVSReliability

Solution Approach 1:

The patent modifies kinetic and stability parameters of the protease through amino acid substitutions. These changes increase the enzyme's half-life and residual activity during storage periods, ensuring that sufficient catalytic activity remains after storage to deliver effective cleaning performance on protease-sensitive soils.

Inventive Principle:
Principle #35Parameter changes

Solution Approach 2:

The invention applies preliminary action by pre-modifying the protease sequence to enhance its storage stability before the detergent is used. The amino acid substitutions are designed in advance to prevent degradation and maintain activity during the storage period, so the enzyme is already optimized for long-term stability before encountering the cleaning task.

Inventive Principle:
Principle #10Preliminary action

3Productivity

If standard proteases are used, then detergent formulation is simple, but cleaning effectiveness on protease-sensitive soils is inadequate

Engineering Contradiction:
Improvecleaning effectivenessVSAvoidprotease structure
Core Design Contradiction:
ProductivityVSDevice complexity

Solution Approach 1:

The patent applies local quality by introducing specific amino acid substitutions at defined positions (121, 194, 209, 218, 237) in the protease sequence. These localized modifications improve cleaning effectiveness on protease-sensitive soils while maintaining relative simplicity in the overall protein structure and detergent formulation.

Inventive Principle:
Principle #3Local quality

Solution Approach 2:

The invention changes specific structural parameters of the protease at key positions to enhance its cleaning performance. The amino acid substitutions are designed to optimize catalytic efficiency and substrate binding while preserving the fundamental protease structure, thus improving effectiveness without excessive complexity.

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 modified protease exhibits improved stability and cleaning performance on protease-sensitive soils like egg yolk, blood, and milk, ensuring effective removal over extended periods.

Implementation Method 1

They act as non-specific endopeptidases and hydrolyze any amide bonds located within peptides or proteins

Methodology Applied
Scientific EffectEnzymatic hydrolysis: Hydrolysis

Implementation Method 2

Proteases are among the most technically important enzymes. They break down protein-based soils on the items being cleaned

Methodology Applied
Scientific EffectEnzyme catalysis: Catalysis

Data Source

PatentEP4685233A1Protease variants with improved storage stability
Publication Date: 2026.01.28 HENKEL KGAA
  • EP4685233A1 patent drawing
  • EP4685233A1 patent drawing

AI summary

The invention relates to proteases exhibiting proteolytic activity and comprising an amino acid sequence that is at least 70% identical over its total length to the amino acid sequence specified in SEQ ID NO:1, wherein the proteases, each with reference to the numbering according to SEQ ID NO:1, have at least one amino acid substitution selected from the group consisting of N121F, A194C, A209V, T218I, N237P, and N237W at at least one of the positions corresponding to positions 121, 194, 209, 218, and 237. Such proteases are suitable for use in detergents and cleaning agents, in particular textile detergents, and exhibit improved storage stability compared to a reference protease. The invention further relates to the use of these proteases and processes in which they are used, as well as detergents and cleaning agents containing them, in particular textile detergents.