Serine Protease Variant with Targeted Residue Changes for Thermal Stability
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Solution Overview
Problem
There is a need to develop a serine protease with improved thermal stability and increased activity for enhanced industrial cost-effectiveness and efficiency.
Innovation Solution
A serine protease variant is provided, which includes specific amino acid substitutions at positions 12 and/or 116 from the N-terminus, enhancing its enzymatic activity by up to 200% compared to the wild-type enzyme.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If wild-type serine protease is used, then the enzyme structure is simple and easy to manufacture, but the thermal stability and enzymatic activity are insufficient for industrial applications
Solution Approach 1:
The patent applies parameter changes by modifying specific amino acid residues at positions 12 and 116 in the serine protease sequence. These targeted substitutions change the local chemical and physical parameters of the enzyme structure, resulting in improved thermal stability and enzymatic activity while maintaining overall structural simplicity suitable for industrial manufacturing.
Solution Approach 2:
The invention implements local quality by introducing specific amino acid substitutions at predetermined positions (12 and 116) rather than modifying the entire enzyme structure. This localized modification approach improves thermal stability and activity at critical regions while keeping the rest of the enzyme structure simple and easy to manufacture.
2Productivity
If wild-type serine protease is used, then the manufacturing process is simple, but the enzymatic activity is low reducing industrial efficiency
Solution Approach 1:
The patent improves productivity by changing specific amino acid parameters at positions 12 and 116. These parameter changes result in up to 200% increase in enzymatic activity compared to wild-type, significantly enhancing industrial efficiency while the manufacturing process remains straightforward through standard protein expression techniques.
3Reliability
If serine protease with improved thermal stability is developed, then industrial cost-effectiveness increases, but the enzyme requires complex amino acid substitutions
Solution Approach 1:
The patent resolves this contradiction by applying local quality - introducing only two specific amino acid substitutions at positions 12 and 116 rather than complex modifications throughout the sequence. This minimal localized change achieves improved thermal stability and industrial cost-effectiveness without requiring elaborate enzyme engineering.
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 serine protease variant exhibits superior activity, making it useful for various industrial applications.
Implementation Method 1
serine proteases (or serine endopeptidases) are enzymes characterized by having in common an active serine residue in their active sites, which cleave peptide bonds in proteins
Implementation Method 2
in which serine serves as a nucleophilic amino acid at a protease's active site
Data Source
AI summary
The present disclosure relates to a novel serine protease variant.