Protease Variants With Targeted Substitutions for Cleaning Activity
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Solution Overview
Problem
There is a need for engineered proteases with enhanced proteolytic and cleaning activities suitable for specific conditions and uses.
Innovation Solution
Development of protease variants with specific amino acid substitutions, such as S078N-G097A-G128S-Y217Q, that exhibit improved proteolytic and cleaning activities compared to the BPN' protease, along with methods for producing and using these variants in compositions for cleaning applications.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Productivity
If protease variants with specific amino acid substitutions (S078N-G097A-G128S-Y217Q) are developed, then proteolytic activity and cleaning activity are enhanced, but protein structure complexity increases
Solution Approach 1:
The patent applies parameter changes by modifying specific amino acid residues (S078N, G097A, G128S, Y217Q) in the protease sequence to enhance proteolytic and cleaning activities. This targeted substitution approach optimizes enzyme performance while maintaining structural feasibility through controlled parameter modification.
Solution Approach 2:
The invention implements local quality by introducing specific amino acid substitutions at particular positions (78, 97, 128, 217) within the protease sequence. These localized modifications enhance specific functional properties (proteolytic activity, cleaning activity) without altering the entire protein structure, thereby resolving the contradiction between enhanced functionality and structural complexity.
2Productivity
If protease variants with specific amino acid substitutions (S078N-G097A-G128S-Y217Q) are developed, then cleaning activity is enhanced, but manufacturing complexity increases
Solution Approach 1:
The patent modifies specific amino acid parameters (S078N, G097A, G128S, Y217Q) to enhance cleaning activity. These targeted changes allow for improved performance while maintaining relatively simple manufacturing processes through site-directed mutagenesis and standard recombinant expression techniques.
Solution Approach 2:
By applying localized amino acid substitutions at specific positions rather than global sequence modification, the invention achieves enhanced cleaning activity with minimal impact on manufacturing complexity. The local quality approach enables precise functional optimization using established protein engineering methods.
3Productivity
If multiple amino acid substitutions are introduced to enhance proteolytic activity, then enzyme performance improves, but sequence identity to original BPN' protease decreases
Solution Approach 1:
The patent introduces specific amino acid substitutions (S078N, G097A, G128S, Y217Q) to enhance proteolytic activity while maintaining at least 80% sequence identity to BPN' protease. This controlled parameter modification approach optimizes enzyme performance within acceptable sequence deviation limits.
Solution Approach 2:
The invention applies local quality by limiting modifications to specific amino acid positions (78, 97, 128, 217) while preserving the majority of the original BPN' sequence. This localized approach enhances proteolytic activity while maintaining sufficient sequence identity for structural integrity and manufacturability.
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 proteolytic and cleaning activities, making them suitable for various industrial and personal care applications, including cleaning compositions and methods.
Implementation Method 1
the variant has enhanced proteolytic activity and/or cleaning activity compared to the proteolytic activity and/or cleaning activity of the BPN' protease
Data Source
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AI summary
The present invention provides protease variants, compositions comprising protease variants, and methods of using such protease variants and compositions.