Lipase Variants for Detergent Stability and Hydrolytic Activity
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Solution Overview
Problem
Current cleaning and fabric care compositions often interfere with the effectiveness of lipases in removing lipid stains, necessitating the development of lipase variants with improved properties such as increased thermostability and hydrolytic activity for better performance in harsh detergent environments.
Innovation Solution
The development of lipase variants with specific substitutions at various positions, resulting in enhanced thermostability, hydrolytic activity, and stability in detergent environments, achieved through modifications that maintain or improve the enzyme's functionality in cleaning applications.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Productivity
If lipase is used in cleaning compositions, then lipid stain removal ability is improved, but the enzyme activity is reduced due to interference from other active ingredients in the composition
Solution Approach 1:
The patent applies parameter changes by modifying the amino acid sequence of the lipase enzyme through site-directed mutagenesis. Specific residues are substituted to alter the enzyme's properties, making it more resistant to interference from detergent ingredients while maintaining catalytic activity. This changes the molecular parameters of the enzyme to improve its performance in harsh cleaning environments.
2Productivity
If lipase is used in detergent environments, then cleaning performance is improved, but the enzyme stability is reduced due to harsh conditions
Solution Approach 1:
The patent modifies physical-chemical parameters of the lipase by introducing specific amino acid substitutions that enhance the enzyme's structural stability. These changes make the enzyme more resistant to denaturation by detergents, surfactants, and other harsh ingredients, thereby maintaining stability while preserving cleaning performance.
3Productivity
If lipase is used in cleaning compositions, then hydrolytic activity is improved, but the thermostability is reduced due to exposure to high temperatures during washing
Solution Approach 1:
The patent applies parameter changes by substituting specific amino acid residues that are involved in maintaining the enzyme's thermal stability. These substitutions strengthen the protein structure through enhanced intramolecular interactions, allowing the lipase to retain hydrolytic activity at elevated washing temperatures without denaturation.
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 lipase variants exhibit improved performance in cleaning, with increased thermostability and hydrolytic activity in detergents, effectively addressing the limitations of existing lipases in harsh cleaning compositions.
Implementation Method 1
Lipases are important biocatalysts which have shown to be useful for various applications
Implementation Method 2
lipase activity, at least 75% but less than 100% sequence identity to SEQ ID NO: 3
Data Source
AI summary
The present invention relates to a lipase variant of a parent lipase, which variant has lipase activity, at least 75% but less than 100% sequence identity to SEQ ID NO: 3 and comprises a substitution at one or more positions corresponding to positions 1; 2; 3; 4; 5; 6; 7; 9; 10; 11; 12; 16; 19; 30; 31; 34; 36; 37; 39; 40; 42; 44; 51; 52; 53; 54; 56; 58; 59; 70; 71; 72; 73; 83; 84; 86; 88; 90; 92; 93; 95; 96; 100; 101; 102; 104; 106; 109; 110; 112; 117; 119; 124; 125; 127; 128; 131; 132; 133; 134; 135; 137; 158; 159; 160; 161; 162; 163; 165; 166; 167; 168; 170; 181; 182; 183; 189; 190; 192; 194; 196; 202; 210; 211; 212; 220; 225; 227; 228; 229; 230; 231; 233; 237; 238; 239; 240; 242; 246; 247; 248; 252; 259; 262; 264; 269 of SEQ ID NO: 3. 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.