Protease Stability in Liquid Detergents via Amino Acid Substitutions
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Solution Overview
Problem
Proteases used in detergents and cleaning agents often exhibit insufficient catalytic performance and stability, especially in liquid surfactant-containing preparations, leading to suboptimal cleaning results due to instability and unfavorable interactions with phosphonates.
Innovation Solution
A protease from Bacillus pumilus with specific amino acid substitutions at positions P9, Q62, D101, N130, G166, N187, S216, N238, or Q271, which enhances storage stability and maintains enzymatic activity in detergents and cleaning agents, even after extended storage periods.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If conventional proteases are used in liquid surfactant-containing detergents, then the detergent can be formulated with surfactants and phosphonates, but the protease shows insufficient stability and catalytic performance after storage
Solution Approach 1:
The patent applies parameter changes by modifying the amino acid sequence of the protease at specific positions (P9, Q62, D101, N130, G166, N187, S216, N238, or Q271) to alter its physical and chemical properties. These sequence changes result in improved stability and catalytic performance of the protease in liquid detergent formulations during storage, directly resolving the contradiction between reliability and productivity.
2Duration of action of stationary object
If proteases are stored in detergents for extended periods, then the detergent remains available for use, but the protease loses catalytic activity due to instability
Solution Approach 1:
The patent modifies the protease's amino acid sequence parameters to enhance its stability during storage. The specific substitutions at positions P9, Q62, D101, N130, G166, N187, S216, N238, or Q271 enable the protease to maintain its enzymatic activity and structural integrity over extended storage periods in detergent formulations, thus resolving the contradiction between storage duration and reliability.
3Adaptability or versatility
If phosphonates are added to liquid surfactant preparations, then the detergent formulation is enhanced, but unfavorable interactions occur between phosphonates and the protease
Solution Approach 1:
The patent applies local quality by making specific localized changes to the protease molecule at particular amino acid positions (P9, Q62, D101, N130, G166, N187, S216, N238, or Q271). These localized modifications reduce unfavorable interactions with phosphonates while preserving the protease's catalytic function, allowing the detergent to contain both phosphonates and active protease simultaneously, thus resolving the contradiction between formulation flexibility and harmful interactions.
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 stability and catalytic activity over time, ensuring effective cleaning performance on protease-sensitive soils across a wide temperature range, maintaining at least 90% of the reference washing performance.
Implementation Method 1
They break down protein-containing dirt on the items being cleaned. Particularly important here are proteases of the subtilisin type... which are serine proteases due to the catalytically active amino acids. They act as nonspecific endopeptidases and hydrolyze any acid amide bonds that lie inside peptides or proteins.
Data Source
AI summary
The invention relates to proteases having an amino acid sequence with at least 70% sequence identity to the amino acid sequence given in SEQ ID No. 2, across its whole length, and comprising an amino acid substitution on at least one of the positions P9, Q62, D101, N130, G166, N187, S216, N238 or Q271, relating in each case to the numbering according to SEQ ID No. 2. The invention also relates to the production and use thereof. Such proteases exhibit very good stability, in particular storage stability, while at the same time having a good cleaning performance.