Automatic dishwashing detergent composition comprising an amylase
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Solution Overview
Problem
Existing automatic dishwashing compositions using conventional amylases are not stable in the detergent matrix, do not perform well in both long hot and short cycles, and struggle with heavily soiled dishware.
Innovation Solution
An automatic dishwashing composition comprising a variant α-amylase with specific mutations at positions 91 and the base of the α-amylase TIM barrel structure, along with optional mutations in loops and other residues, enhancing stability and activity in various cycles.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If conventional amylases are used in automatic dishwashing compositions, then the composition can be manufactured with standard ingredients, but the composition lacks stability in the detergent matrix and performs poorly in hot and short cycles
Solution Approach 1:
The patent applies parameter changes by introducing specific amino acid substitutions at defined positions in the α-amylase sequence. These molecular-level parameter changes (residue substitutions) enhance the enzyme's stability in the detergent matrix while maintaining its catalytic activity during hot and short wash cycles, directly resolving the contradiction between reliability and structural simplicity.
2Productivity
If conventional amylases are used, then the composition can be produced with standard manufacturing processes, but the cleaning performance is insufficient for heavily soiled dishware in short cycles
Solution Approach 1:
The patent introduces specific amino acid substitutions that modify the enzyme's kinetic parameters and stability characteristics. These changes enable the amylase to maintain consistent activity across varying wash conditions (temperature, time, detergent matrix), thereby improving cleaning speed for heavily soiled dishware while ensuring reliable performance consistency.
3Productivity
If the amylase is designed for high activity in short cycles, then cleaning performance improves, but stability in the detergent matrix deteriorates
Solution Approach 1:
The patent simultaneously optimizes multiple parameters through coordinated amino acid substitutions. The specific residue changes enhance both the enzyme's catalytic efficiency (productivity) and its conformational stability in the detergent matrix, resolving the contradiction between cleaning efficiency and compositional stability.
4Temperature
If standard amylases are used, then the composition formulation is simpler, but the performance in hot cycles above 40°C is inadequate
Solution Approach 1:
The patent introduces amino acid substitutions that specifically enhance the enzyme's thermal stability and activity profile. These molecular parameter changes enable the amylase to maintain reliable performance across an expanded temperature range, particularly in hot cycles above 40°C, while preserving formulation simplicity.
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 α-amylase provides improved cleaning performance in hot and short cycles, even with heavily soiled dishware, maintaining stability and activity throughout the wash process.
Implementation Method 1
Amylases are important ingredients in automatic dishwashing compositions... The composition comprises a variant α-amylase wherein the variant α-amylase comprises amino acid substitution(s)... provides improved cleaning performance
Data Source
AI summary
An automatic dishwashing cleaning composition comprising a variant α-amylase wherein the variant α-amylase comprises amino acid substitution(s) selected from the group consisting of:i) a mutation at position 91 and one or more mutation(s) at an amino acid residue at the base of the α-amylase TIM barrel structure, defined as residues 6, 7, 40, 96, 98, 100, 229, 230, 231, 262, 263, 285, 286, 287, 288, 322, 323, 324, 325, 362, 363 and 364; and/orii) a mutation at position 172 and a mutation in position 288 or 324; and/oriii) Y364Lreferring to SEQ ID NO: 1 for numbering.