Subtilisin Variant Amino Acid Substitutions for Cold Water Detergency
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Solution Overview
Problem
Current laundry detergents face challenges in maintaining effective stain and soil removal at low temperatures and short wash times, as existing proteases exhibit reduced efficacy under these conditions.
Innovation Solution
A cleaning composition featuring a subtilisin variant with specific amino acid substitutions, such as X006W, X024K, X055P, X109Q, X162Q, X182Q, X183N, X204Q, X206Y, X222Q, or X248A, which provides improved stability and proteolytic activity, combined with a cleaning adjunct, to enhance cleaning performance in cold water and short wash cycles.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If conventional proteases are used in detergent compositions, then good proteolytic activity is achieved at normal washing conditions, but cleaning efficacy is reduced at low temperatures and short wash times
Solution Approach 1:
The patent applies parameter changes by modifying the amino acid sequence of the subtilisin enzyme through specific substitutions (e.g., at positions 6, 24, 55, 109, 162, 182, 183, 204, 206, 222, 248, or 254) to alter its thermal and kinetic properties. These sequence modifications enable the enzyme to maintain optimal proteolytic activity at low temperatures while preserving stability during storage and washing cycles.
2Productivity
If conventional proteases are used in detergent compositions, then good cleaning performance is achieved, but stability over time and in storage is insufficient
Solution Approach 1:
The patent modifies the enzyme's structural parameters through amino acid substitutions that enhance its stability. Specific changes in the enzyme's primary sequence improve its resistance to denaturation, aggregation, and autolysis during storage and throughout the washing process, ensuring consistent cleaning performance.
Solution Approach 2:
The patent creates a composite system combining the engineered subtilisin variant with detergent formulation components. This composite approach optimizes the interaction between the enzyme and detergent matrix, protecting the protease from deactivating factors while maintaining its catalytic activity.
3Loss of energy
If washing time is reduced for energy efficiency, then energy consumption is lowered, but stain and soil removal efficacy is reduced
Solution Approach 1:
The patent changes the kinetic parameters of the subtilisin enzyme through amino acid modifications that increase its catalytic efficiency. The engineered variant has enhanced turnover number and substrate affinity, allowing it to achieve effective stain removal in shorter timeframes, thus enabling reduced wash cycles without sacrificing cleaning performance.
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 subtilisin variant demonstrates enhanced stability and cleaning performance, maintaining residual activity and proteolytic efficacy even at low temperatures and in the presence of detergents, thereby improving stain and soil removal efficiency.
Implementation Method 1
proteases into their products to provide good cleaning of stains... analyze the respective protease's ability to hydrolyze a commercial substrate
Implementation Method 2
the protease will provide good levels of proteolytic cleaning even after addition to the other materials in the cleaning composition and/or in the conditions on storage and/or shipment of the cleaning composition, and/or in the conditions in the wash liquor
Data Source
AI summary
Cleaning compositions particularly for laundry, can include one or more subtilisin variant and cleaning adjunct. Methods of treating surfaces, particularly fabrics, can include contacting the surface with an aqueous wash liquor having the cleaning composition therein. The subtilisin variant may have improved stability and/or soil removal compared to one or more reference subtilisin.


