Protease-Amylase Liquid Detergent Storage Stability

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Solution Overview

Problem

Existing liquid washing and cleaning agents containing proteases and amylases suffer from insufficient storage stability, leading to a loss of amylolytic activity over time, which reduces their cleaning power.

Innovation Solution

A liquid washing or cleaning agent comprising a protease with an amino acid sequence at least 80% identical to a specific sequence (SEQ ID NO: 1) and having glutamic acid, aspartic acid, asparagine, glutamine, alanine, glycine, or serine at position 99, combined with an amylase, which reduces the inactivation of the amylase and maintains higher amylolytic activity during storage.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Productivity

If protease and amylase are combined in liquid washing agents, then cleaning power is improved, but storage stability deteriorates due to protease-induced amylase inactivation

Engineering Contradiction:
Improvecleaning powerVSAvoidstorage stability
Core Design Contradiction:
ProductivityVSReliability

Solution Approach 1:

The patent applies parameter changes by modifying the amino acid sequence of the protease at position 99 to specific amino acids (glutamic acid, aspartic acid, asparagine, glutamine, alanine, glycine, or serine) to reduce its inactivating effect on amylase, thereby improving storage stability while maintaining cleaning effectiveness

Inventive Principle:
Principle #35Parameter changes

Solution Approach 2:

The patent creates a composite enzyme system combining a specifically modified protease with amylase, where the protease has been engineered with specific amino acid substitutions to be compatible with amylase, forming a stable multi-enzyme formulation that maintains both cleaning power and storage stability

Inventive Principle:
Principle #40Composite materials

2Quantity of substance

If amylase is added to protease-containing washing agents, then amylolytic activity is improved, but residual activity after storage deteriorates

Engineering Contradiction:
Improveamylolytic activityVSAvoidresidual activity after storage
Core Design Contradiction:
Quantity of substanceVSDuration of action of moving object

Solution Approach 1:

The patent modifies the protease parameters through specific amino acid substitutions at position 99, changing its biochemical properties to reduce interaction with amylase that leads to inactivation, thereby preserving amylolytic activity during storage periods

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 specific protease and amylase in the washing agent enhances storage stability and cleaning power, particularly on protease-sensitive soils, even at low temperatures, by minimizing amylase inactivation and maintaining residual activity after extended storage periods.

Implementation Method 1

Proteases of the subtilisin type are preferably employed in washing and cleaning agents

Methodology Applied
Scientific EffectHydrolysis: Hydrolysis

Implementation Method 2

an amylase is an enzyme that catalyzes the hydrolysis of glycosidic bonds, especially in polysaccharides such as starch

Methodology Applied
Scientific EffectHydrolysis: Hydrolysis

Data Source

PatentUS20230365898A1Washing or cleaning agent comprising a protease and an amylase
Publication Date: 2023.11.16 BASF SE

AI summary

According to the invention, storage stability in terms of amylolytic activity is to be improved in a liquid washing or cleaning agent which comprises a protease and amylase. This is achieved by the use of a protease which comprises an amino acid sequence which is at least 80% identical to the amino acid sequence specified in SEQ ID NO. 1 and which has the amino acid glutamic acid (E) or aspartic acid (D) or the amino acid asparagine (N) or glutamine (Q) or the amino acid alanine (A) or glycine (G) or serine (S) at position 99 in the count according to SEQ ID NO. 1.