Lipase Variants for Harsh Cleaning Environments
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Solution Overview
Problem
Current cleaning and fabric care compositions often interfere with the stability and activity of lipases, making it difficult for them to effectively remove lipid stains in harsh environments.
Innovation Solution
Development of lipase variants with increased thermostability, specifically through substitutions such as S152A+D255G, Q49K+T176N+D255G, and others, which maintain at least 75% sequence identity to a parent lipase, enhancing their stability and activity in challenging compositions.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Productivity
If lipase is used in harsh cleaning compositions, then lipid stain removal capability is improved, but enzyme stability and activity deteriorate due to interfering ingredients
Solution Approach 1:
The patent applies parameter changes by modifying the amino acid sequence of the lipase enzyme through site-directed mutagenesis. Specific substitutions (e.g., S152A, D255G, Q49K, T176N) alter the enzyme's physical and chemical properties, particularly its thermostability and resistance to denaturation by surfactants and other cleaning composition ingredients, thereby maintaining stability while preserving lipid stain removal capability
Solution Approach 2:
The patent creates a composite enzyme system by combining multiple amino acid substitutions within the lipase molecule. These substitutions work synergistically to confer enhanced stability properties, creating a composite structure that resists degradation by various interfering ingredients in cleaning compositions while maintaining catalytic activity
2Productivity
If lipase is used in harsh cleaning compositions, then lipid stain removal capability is improved, but enzyme activity deteriorates due to interfering ingredients
Solution Approach 1:
The patent modifies enzyme activity parameters through amino acid substitutions that alter the enzyme's conformational stability and active site accessibility. The substitutions (e.g., N97D, R131A, V247F) fine-tune the enzyme's catalytic properties, ensuring high activity in harsh cleaning environments where wild-type lipase would be inhibited or inactivated
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; 13; 14; 15; 17; 18; 29; 30; 33; 34; 36; 37; 38; 40; 41; 43; 44; 45; 46; 47; 49; 50; 5 51; 52; 54; 55; 57; 58; 59; 60; 69; 70; 71; 72; 81; 82; 85; 86; 87; 89; 90; 91; 92; 94; 95; 96; 97; 99; 100; 101; 102; 103; 105; 108; 111; 115; 116; 118; 119; 120; 122; 123; 124; 126; 127; 128; 129; 130; 131; 132; 133; 134; 136; 144; 152; 155; 157; 158; 159; 161; 162; 163; 177; 178; 181; 182; 184; 185; 187; 189; 191; 196; 197; 199; 203; 205; 206; 207; 208; 209; 211; 215; 220; 221; 222; 223; 224; 226; 229; 230; 232; 235; 236; 240; 242; 243; 244; 247; 248; 252; 254; 255; 257; 10 260; 261; 262 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.