Serine Protease Variant Mutations for Thermal Stability and Activity

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Solution Overview

Problem

Existing serine proteases lack sufficient thermal stability and activity for enhanced industrial applications.

Innovation Solution

A serine protease variant is developed by substituting specific amino acids at positions 180 and/or 331 or 361 with tyrosine, glutamic acid, histidine, leucine, methionine, asparagine, glutamine, or tryptophan, maintaining at least 75% sequence homology to SEQ ID NO: 10 or 7, and is produced using a Bacillus sp. microorganism.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Reliability

If amino acid substitution is performed to improve thermal stability and activity, then enzyme performance is enhanced, but protein structure complexity increases

Engineering Contradiction:

Improvethermal stabilityVSAvoidprotein structure complexity

Core Design Contradiction:

ReliabilityVSDevice complexity

Solution Approach 1:

The patent applies local quality by performing site-directed mutagenesis at specific positions (180, 331, 361) of the serine protease sequence. Instead of random mutations throughout the protein, the invention focuses on substituting amino acids only at these critical positions to improve thermal stability and activity, thereby enhancing performance while minimizing unnecessary structural complexity

Inventive Principle:

Principle #3Local quality

Solution Approach 2:

The patent employs parameter changes by substituting specific amino acid residues at defined positions in the serine protease sequence. This involves changing the chemical parameters (amino acid type) at specific locations to optimize enzyme performance, achieving improved thermal stability and catalytic activity through controlled sequence modification

Inventive Principle:

Principle #35Parameter changes

2Productivity

If amino acid substitution is performed to enhance activity, then enzymatic performance improves, but manufacturing complexity increases

Engineering Contradiction:

Improveenzymatic activityVSAvoidmanufacturing complexity

Core Design Contradiction:

ProductivityVSEase of manufacture

Solution Approach 1:

The invention applies local quality by targeting specific positions (180, 331, 361) for amino acid substitution to enhance enzymatic activity. This localized approach allows for improved productivity through focused mutations at critical residues, while simplifying the manufacturing process compared to random mutagenesis or whole-protein redesign

Inventive Principle:

Principle #3Local quality

Solution Approach 2:

The patent applies preliminary action by pre-identifying the critical positions (180, 331, 361) in the serine protease sequence that are most likely to influence activity and stability. This preliminary analysis of sequence structure and functional importance allows for targeted mutagenesis, reducing manufacturing complexity by avoiding trial-and-error approaches

Inventive Principle:

Principle #10Preliminary action

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 variant exhibits superior activity and stability, enabling diverse industrial applications including feed and food production, leather processing, and contact lens cleaning.

Implementation Method 1

a serine protease variant, in which an amino acid corresponding to position 180 of SEQ ID NO: 10 is substituted with a different amino acid

Methodology Applied

Scientific EffectProteolysis: Hydrolysis

Data Source

PatentEP4692340A1Novel serine protease variant

Publication Date: 2026.02.11 CJ CHEILJEDANG CORP

AI summary

The present disclosure relates to a novel serine protease variant.