Lipase Variants for Calcium-Independent Detergent Activity
Find Innovative SolutionsGenerate Solutions
Solution Overview
Problem
Current lipases used in detergent compositions face challenges with reduced activity due to interference from other active ingredients and low calcium levels, leading to decreased effectiveness in lipid stain removal.
Innovation Solution
Development of lipase variants with specific modifications at defined positions, such as substitutions and deletions, to enhance lipase activity and independence from calcium levels, allowing them to function effectively in detergent environments.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Productivity
If lipases are used in detergent compositions, then lipid stain removal performance is improved, but lipase activity is reduced due to interference from other active ingredients and low calcium levels
Solution Approach 1:
The patent applies parameter changes by modifying the amino acid sequence of lipase at specific positions (1, 2, 3, 5, 8, 43, 45, 105, 167, 178, 224-236, 239, 244) to create variants with altered properties. These sequence modifications result in lipase variants that maintain or enhance activity in detergent compositions with low calcium levels and presence of interfering ingredients, thereby resolving the contradiction between productivity and reliability.
2Object-affected harmful factors
If calcium concentration is reduced in detergent compositions, then fabric graying is prevented, but lipase activity is reduced
Solution Approach 1:
The patent modifies the lipase protein structure through amino acid substitutions at specific positions to create variants that are less dependent on calcium for activity. This allows the detergent to maintain low calcium levels to prevent fabric graying while the modified lipase retains sufficient activity for lipid stain removal, thus resolving the contradiction between preventing harmful effects and maintaining enzyme activity.
3Adaptability or versatility
If lid domain is modified to be in open conformation or removed, then interfacial activation is eliminated, but lipase activity and stability are reduced
Solution Approach 1:
The patent applies parameter changes by modifying specific amino acid positions that influence lid domain conformation and calcium binding. The modifications at positions such as 43, 45, 167, and 224-236 alter the structural dynamics of the lid domain and calcium interaction, creating variants that achieve calcium independence and interfacial activation independence while maintaining or enhancing lipase activity, thus resolving the contradiction between adaptability and reliability.
Data Source
AI summary
The present invention relates to lipase 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.


