Stabilized Protease-Amylase Liquid Detergent

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Solution Overview

Problem

Prior art protease- and amylase-containing liquid washing agents have inadequate storage stability, leading to a significant loss of enzymatic activity, particularly amylolytic and proteolytic activity, due to the inactivation of amylase by protease, resulting in suboptimal cleaning performance.

Innovation Solution

A liquid washing agent comprising a protease with an amino acid sequence at least 70% identical to a specific sequence (SEQ ID no. 1) and featuring amino acid substitutions R99E or R99D in combination with S3T, V4I, and V199I, used in conjunction with an amylase, which stabilizes the enzymatic activity and maintains improved cleaning performance during storage.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Reliability

If prior art protease and amylase are combined in liquid washing agents, then cleaning performance is improved, but storage stability deteriorates due to protease inactivating amylase

Engineering Contradiction:
Improvestorage stabilityVSAvoidprotease inactivation of amylase
Core Design Contradiction:
ReliabilityVSObject-generated harmful factors

Solution Approach 1:

The invention applies parameter changes by modifying the amino acid sequence of the protease at specific positions (99, 213, 217, 222) to create variant proteases that do not inactivate amylase. These sequence modifications change the protease's properties to eliminate the harmful interaction while preserving its cleaning function, thereby resolving the contradiction between cleaning performance and storage stability.

Inventive Principle:
Principle #35Parameter changes

2Productivity

If liquid washing agents contain protease and amylase, then enzymatic cleaning capability is enhanced, but enzyme activity is lost during storage

Engineering Contradiction:
Improveenzymatic cleaning capabilityVSAvoidenzyme activity retention
Core Design Contradiction:
ProductivityVSDuration of action of moving object

Solution Approach 1:

The invention modifies the protease's amino acid parameters at positions 99, 213, 217, and 222 to create stable variants that maintain their activity over extended storage periods. This parameter modification approach allows the washing agent to retain full enzymatic cleaning capability throughout its shelf life, resolving the contradiction between initial productivity and duration of action.

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 combination of the modified protease and amylase in the washing agent enhances storage stability, maintaining effective amylolytic and proteolytic cleaning performance after storage, even at low temperatures, and ensures better removal of protease-sensitive soiling on textiles and hard surfaces.

Implementation Method 1

a protease which comprises an amino acid sequence which, over the entire length thereof, is at least 70% identical to the amino acid sequence stated in SEQ ID no. 1

Methodology Applied
Scientific EffectHydrolysis: Hydrolysis

Implementation Method 2

an amylase. Amylases consequently in particular act against starch-containing residues on laundry and catalyze the hydrolysis thereof

Methodology Applied
Scientific EffectHydrolysis: Hydrolysis

Data Source

PatentUS9752102B2Liquid washing or cleaning agent containing protease and amylase
Publication Date: 2017.09.05 HENKEL KGAA

AI summary

The intention is to improve storage stability in a liquid washing or cleaning agent which contains a protease and amylase. This is achieved by using a protease which comprises an amino acid sequence which, over the entire length thereof, is at least 70% identical to the amino acid sequence stated in SEQ ID no. 1 and, in the numbering according to SEQ ID no. 1, has the amino acid substitution R99E or R99D in combination with at least two further amino acid substitutions which are selected from the group consisting of S3T, V4I and V199I.