Protease Sequence Variants for Stable Protein Soil Cleaning
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Solution Overview
Problem
Existing proteases in washing and cleaning agents do not exhibit sufficient catalytic activity and storage stability under standard washing conditions, leading to suboptimal cleaning performance on protein-sensitive soilings.
Innovation Solution
A protease from Bacillus pumilus with specific amino acid substitutions, such as 9T, 133A, 144K, 252T, and 271E, and additional substitutions at positions 3, 4, 82, 156, 162, or 218, enhances cleaning performance and storage stability, making it suitable for use in washing agents.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If conventional proteases are used in washing and cleaning agents, then they can provide basic proteolytic activity, but they do not exhibit sufficient catalytic activity and storage stability under standard washing conditions
Solution Approach 1:
The patent applies parameter changes by modifying the amino acid sequence of the protease through specific substitutions at defined positions. These sequence changes alter the enzyme's physical and chemical properties, resulting in improved storage stability and catalytic activity under washing conditions while maintaining the fundamental proteolytic function.
Solution Approach 2:
The invention applies local quality by introducing specific amino acid substitutions at particular positions within the protease sequence. These localized changes at specific sites modify the enzyme's properties without altering its overall structure, enabling improved stability and activity while preserving the core catalytic function.
2Productivity
If conventional proteases are used in washing and cleaning agents, then they can provide basic cleaning function, but they do not exhibit sufficient cleaning performance on protein-sensitive soilings
Solution Approach 1:
The patent applies parameter changes by modifying the amino acid sequence of the protease through specific substitutions at defined positions. These sequence changes alter the enzyme's physical and chemical properties, resulting in improved storage stability and catalytic activity under washing conditions while maintaining the fundamental proteolytic function.
Solution Approach 2:
The invention applies local quality by introducing specific amino acid substitutions at particular positions within the protease sequence. These localized changes at specific sites modify the enzyme's properties without altering its overall structure, enabling improved stability and activity while preserving the core catalytic function.
3Productivity
If proteases are optimized for catalytic activity, then cleaning performance improves, but storage stability deteriorates
Solution Approach 1:
The patent applies parameter changes by modifying the amino acid sequence of the protease through specific substitutions at defined positions. These sequence changes alter the enzyme's physical and chemical properties, resulting in improved storage stability and catalytic activity under washing conditions while maintaining the fundamental proteolytic function.
Solution Approach 2:
The invention applies local quality by introducing specific amino acid substitutions at particular positions within the protease sequence. These localized changes at specific sites modify the enzyme's properties without altering its overall structure, enabling improved stability and activity while preserving the core catalytic function.
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 modified protease demonstrates improved proteolytic activity and increased stability, achieving enhanced cleaning results on protein-sensitive soilings across various temperature ranges and extended storage periods.
Implementation Method 1
They act as non-specific endopeptidases and hydrolyze any acid amide bonds that are inside peptides or proteins
Data Source
AI summary
Proteases may include an amino acid sequence having at least 70% sequence identity with the amino acid sequence given in SEQ ID NO:1 over its entire length and, in each case based on the numbering according to SEQ ID NO:1. The protease may have (i) amino acid substitutions, such as 9T, 133A, 144K, 252T and 271E, at the positions corresponding to positions 9, 133, 144, 252 and 271; and (ii) at least one further amino acid substitution at at least one of the positions corresponding to positions 3, 4, 82, 156, 162 or 218. The production and use of said proteases help to improve cleaning performance.