Novel Trypsin-like Serine Proteases for Cleaning Stability
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Solution Overview
Problem
There is a need for serine proteases with improved proteolytic activity and stability under adverse conditions, such as oxidative agents, chelating agents, extreme temperatures, and pH variations, which current serine proteases like subtilisins do not adequately address.
Innovation Solution
Development of novel trypsin-like serine proteases with specific amino acid sequences, such as those with at least 91%, 94%, 98%, or 80% identity to certain SEQ ID NO sequences, for use in cleaning compositions like laundry detergents and dishwashing detergents, produced through recombinant constructs in hosts like bacteria, fungi, or algae, to enhance soil removal and stability.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If subtilisin serine proteases are used for cleaning applications, then proteolytic activity is achieved, but stability under adverse conditions (oxidative agents, chelating agents, extreme temperatures, pH variations) deteriorates
Solution Approach 1:
The patent applies parameter changes by modifying the amino acid sequence of serine proteases to achieve enhanced stability. Specifically, the invention identifies and modifies key residues in the protease structure that are sensitive to adverse conditions, thereby changing the physical-chemical parameters of the enzyme to improve its reliability under oxidative agents, chelating agents, extreme temperatures, and pH variations while maintaining proteolytic activity
Solution Approach 2:
The patent employs composite materials by creating chimeric proteases that combine functional domains from different protease families. The invention integrates the catalytic domain of trypsin-like serine proteases with structural elements from subtilisins, resulting in a composite enzyme that exhibits both the proteolytic activity of subtilisins and the stability of trypsin-like proteases under adverse cleaning conditions
2Reliability
If new serine proteases are developed to improve stability, then reliability under adverse conditions improves, but device complexity increases
Solution Approach 1:
The patent applies segmentation by dividing the protease structure into distinct functional domains that can be independently optimized. The invention separates the catalytic function from the stability-determining structural elements, allowing each segment to be engineered for its specific purpose - the catalytic domain maintains proteolytic activity while the structural domains provide stability under adverse conditions
Solution Approach 2:
The patent applies universality by designing proteases with multiple functions integrated into a single enzyme structure. The chimeric proteases simultaneously provide proteolytic activity, thermal stability, pH resistance, and resistance to oxidative and chelating agents, reducing the need for multiple different enzymes and simplifying the overall cleaning system
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 novel serine proteases demonstrate improved cleaning performance across various conditions, maintaining activity at different temperatures and pH levels, and are effective in cleaning compositions for fabrics and hard surfaces.
Implementation Method 1
Proteases (also called peptidases or proteinases) are enzymes capable of cleaving peptide bonds
Data Source
AI summary
Described herein is at least one novel trypsin-like serine protease polypeptide and uses thereof. Further described herein are cleaning compositions containing at least one polypeptide described herein, wherein said composition can be used to clean fabrics and hard surfaces. Even further described herein is at least one cleaning composition selected from a laundry detergent, a dishwashing detergent (e.g., automatic and hand dish), and a personal care composition. Even still further, at least one polypeptide having improved soil removal and/or stability compared to at least one reference polypeptide is described herein.