Protease Variants Hydrophobic Cluster Stability
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Solution Overview
Problem
Current protease variants used in detergents face challenges in maintaining stability and performance, particularly in the presence of detergent ingredients like bleach and surfactants, and have limitations in activity at low temperatures and varying pH levels.
Innovation Solution
Development of protease variants with specific substitutions at positions 121, 124, 137, and 162 in the hydrophobic cluster, enhancing stability and wash performance by improving detergent stability and activity profiles.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If current protease variants are used in detergents, then they provide protease activity, but they fail to maintain stability in the presence of detergent ingredients like bleach and surfactants
Solution Approach 1:
The patent applies parameter changes by introducing specific amino acid substitutions at positions 121, 124, 137, and 162 in the hydrophobic cluster of the protease variant. These substitutions alter the physical-chemical parameters of the enzyme structure, specifically enhancing hydrophobic interactions and structural stability. The variants show improved stability in detergent solutions containing bleach and surfactants while maintaining protease activity, directly resolving the contradiction between reliability and resistance to harmful detergent ingredients.
2Reliability
If protease variants are designed for enhanced stability, then they show improved detergent stability, but they have limitations in activity at low temperatures and varying pH levels
Solution Approach 1:
The patent applies local quality by making targeted amino acid substitutions specifically in the hydrophobic cluster region (positions 121, 124, 137, and 162) of the protease variant. This localized modification enhances detergent stability through improved hydrophobic interactions and structural rigidity in the core region, while the rest of the enzyme structure remains flexible enough to maintain catalytic activity across varying temperatures and pH levels. The specific substitutions include I121S, I121V, V124A, I137E, I137M, and V162W, which locally optimize stability without compromising overall adaptability.
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 variants exhibit improved stability and wash performance compared to parent proteases, maintaining activity in detergent solutions and enhancing catalytic efficiency across a range of temperatures and pH levels.
Implementation Method 1
Proteases are from a commercial perspective the most relevant enzyme in such formulations... The variants exhibit improved stability and wash performance compared to parent proteases, maintaining activity in detergent solutions and enhancing catalytic efficiency
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.