Stable Alpha-Amylase Variants in Chelating Detergent Systems
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Solution Overview
Problem
Alpha-amylases used in detergents are often unstable in the presence of chelating agents, which are necessary for reducing water hardness and stain removal, leading to reduced enzyme activity and formulation challenges.
Innovation Solution
Development of a variant alpha-amylase with specific amino acid substitutions and deletions that maintains stability and activity in the presence of chelating agents, specifically capable of reducing free calcium ion concentrations, thereby enhancing wash performance and stability in detergent compositions.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Object-affected harmful factors
If chelating agents are added to reduce water hardness and protect bleaching agents, then stain removal and bleaching protection are improved, but alpha-amylase stability and activity are reduced
Solution Approach 1:
The patent applies parameter changes by modifying the amino acid sequence of alpha-amylase at specific positions (193, 195, 197, 198, 200, 203, 206, 210, 212, 213, and 243) to alter the enzyme's chemical properties. These sequence modifications enable the enzyme to maintain stability and activity in the presence of chelating agents, resolving the contradiction between chelating agent effectiveness and enzyme stability.
2Reliability
If calcium is added to improve enzyme stability, then alpha-amylase stability is improved, but stain removing effect is destroyed and formulation problems occur
Solution Approach 1:
The patent modifies the enzyme's amino acid sequence parameters to change its calcium dependence. The variant alpha-amylases are engineered to maintain stability without requiring high calcium concentrations, thereby preserving stain removal effectiveness while avoiding formulation issues associated with calcium addition.
Solution Approach 2:
The patent extracts the calcium dependence requirement from the enzyme system by creating variants that are less dependent on calcium ions. This is achieved through amino acid substitutions that reduce the enzyme's affinity for calcium or stabilize the structure through alternative mechanisms, allowing the enzyme to function without added calcium.
3Object-affected harmful factors
If strong chelating compounds are used for water hardness reduction, then water hardness reduction is improved, but enzyme activity is reduced
Solution Approach 1:
The patent changes the enzyme's amino acid sequence parameters to reduce its sensitivity to chelating agents. The variants maintain high amylolytic activity even in the presence of strong chelating compounds that effectively reduce water hardness, thus resolving the contradiction between water hardness reduction and enzyme activity maintenance.
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 variant alpha-amylase exhibits improved stability and wash performance compared to parent enzymes, retaining activity and effectiveness even in the presence of chelating agents, ensuring effective stain removal and detergent stability.
Implementation Method 1
Alpha-amylases (alpha-1,4-glucan-4-glucanohydrolases, E.C. 3.2.1.1) constitute a group of enzymes, which catalyse hydrolysis of starch and other linear and branched 1,4-glucosidic oligo- and polysaccharides.
Data Source
AI summary
The present invention relates to cleaning compositions comprising variants of an alpha-amylase having improved stability to chelating agents relative to its parent enzyme and cleaning processes comprising such compositions.