Protease Variants for Egg Stain Removal in Detergents
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Solution Overview
Problem
Current proteases used in detergents face challenges in effectively removing egg stains due to inhibition by substances like trypsin inhibitors, resulting in suboptimal wash performance, especially at low temperatures and in the presence of detergent ingredients.
Innovation Solution
Development of protease variants with specific alterations, such as those at position 142 (G142*, G142C, G142S, G142A, G142E), which exhibit improved wash performance on egg stains by maintaining activity and stability in the presence of detergents and low temperatures, as measured by increased sequence identity and specific activity.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If current proteases are used in detergents, then general proteolytic activity is maintained, but wash performance on egg stains is suboptimal due to inhibition by trypsin inhibitors
Solution Approach 1:
The patent applies parameter changes by modifying the amino acid sequence of the protease at specific positions (particularly position 142 and surrounding residues). These sequence changes alter the enzyme's properties to reduce sensitivity to trypsin inhibitors while maintaining proteolytic activity, thereby improving egg stain removal performance.
Solution Approach 2:
The invention applies local quality by making targeted amino acid substitutions at specific positions (e.g., position 142) rather than throughout the entire enzyme. These localized changes modify the enzyme's interaction with inhibitors without affecting its overall catalytic function, resolving the contradiction between inhibitor sensitivity and activity.
2Reliability
If protease variants with altered amino acid sequences are developed, then wash performance on egg stains is improved, but enzyme stability and activity in detergent compositions must be maintained
Solution Approach 1:
The patent systematically varies amino acid sequences at specific positions to optimize both performance and stability. By changing parameters like amino acid identity at position 142 and surrounding residues, the invention achieves improved egg stain removal while maintaining or enhancing stability in detergent compositions.
Solution Approach 2:
The invention employs feedback through iterative screening and characterization of protease variants. Activity and stability are measured under relevant detergent conditions, and this information feeds back into further optimization of amino acid sequences, ensuring both improved performance and maintained stability.
3Productivity
If protease activity is increased through variant development, then stain removal performance improves, but cost and complexity of enzyme production increase
Solution Approach 1:
The invention reduces complexity by making targeted local changes to the amino acid sequence rather than undertaking complete enzyme redesign. Specific position substitutions (e.g., position 142) provide the desired activity increase with minimal impact on production complexity.
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 protease variants demonstrate enhanced egg stain removal capabilities compared to parent proteases, with improved stability and activity in detergent compositions, effectively addressing the limitations of existing proteases in removing egg stains.
Implementation Method 1
The present invention relates to novel protease variants exhibiting alterations relative to the parent protease in one or more properties including: wash performance, detergent stability and/or storage stability. The protease variants demonstrate enhanced egg stain removal capabilities compared to parent proteases, with improved stability and activity in detergent compositions
Data Source
AI summary
The present invention relates to protease variants and methods for obtaining protease variants. The present invention also relates to polynucleotides encoding the variants; nucleic acid constructs, vectors, and host cells comprising the polynucleotides; and methods of using the variants.