Protease Polypeptide Variants for Higher Activity and pH Stability

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Solution Overview

Problem

Existing proteases lack enhanced catalytic activity and stability, limiting their industrial applications and economic feasibility.

Innovation Solution

A variant polypeptide with specific amino acid modifications at positions 120, 153, 185, 293, 323, 349, and 361, exhibiting increased enzymatic activity, thermal tolerance, and stability, is developed.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Productivity

If wild-type protease is used, then the structure is simple and easy to manufacture, but the catalytic activity and stability are insufficient for industrial applications

Engineering Contradiction:

Improvecatalytic activityVSAvoidpolypeptide structure complexity

Core Design Contradiction:

ProductivityVSDevice complexity

Solution Approach 1:

The patent applies parameter changes by modifying specific amino acid residues at positions 120, 153, 185, 293, 323, 349, and 361 in the protease polypeptide sequence. These targeted substitutions change the physical and chemical parameters of the enzyme, resulting in improved catalytic activity and stability while maintaining the overall structural framework for industrial applicability.

Inventive Principle:

Principle #35Parameter changes

2Reliability

If wild-type protease is used, then the manufacturing process is simple, but the thermal tolerance and pH stability are insufficient

Engineering Contradiction:

Improvethermal tolerance and pH stabilityVSAvoidpolypeptide production complexity

Core Design Contradiction:

ReliabilityVSEase of manufacture

Solution Approach 1:

The patent applies local quality by introducing specific amino acid substitutions at key positions (120, 153, 185, 293, 323, 349, 361) that locally enhance the enzyme's thermal tolerance and pH stability. These localized modifications improve overall reliability without requiring complete redesign of the polypeptide, thus maintaining relative ease of manufacture through targeted mutagenesis.

Inventive Principle:

Principle #3Local quality

3Adaptability or versatility

If protease with enhanced activity is developed, then industrial applicability improves, but the development complexity and time increase

Engineering Contradiction:

Improveindustrial applicabilityVSAvoidvariant development complexity

Core Design Contradiction:

Adaptability or versatilityVSDevice complexity

Solution Approach 1:

The patent applies segmentation by dividing the protease optimization into discrete, manageable components: identifying specific amino acid positions (120, 153, 185, 293, 323, 349, 361) that independently contribute to catalytic activity and stability. This segmented approach allows systematic evaluation of each position's impact, simplifying the overall development process while achieving enhanced industrial applicability.

Inventive Principle:

Principle #1Segmentation

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 polypeptide demonstrates improved catalytic activity, pH stability, acid resistance, and thermal stability, enhancing its suitability for various industrial applications.

Implementation Method 1

Proteases are enzymes that hydrolyze peptide bonds between amino acids that make up proteins

Methodology Applied

Scientific EffectHydrolysis: Hydrolysis

Data Source

PatentEP4660301A1Modified polypeptide having protease activity

Publication Date: 2025.12.10 CJ CHEILJEDANG CORP

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AI summary

The present disclosure relates to a variant polypeptide and use thereof.