Xylanase Polypeptide Variants With Disulfide Bridges for Thermal Stability

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Solution Overview

Problem

Most xylanases exhibit low pH and thermal stability, limiting their application in various industrial fields.

Innovation Solution

A modified polypeptide with xylanase activity, featuring specific amino acid substitutions and disulfide bridges, enhancing thermal tolerance and stability.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Temperature

If amino acid substitutions and disulfide bridges are introduced to improve thermal stability, then thermal tolerance and stability are enhanced, but protein structure complexity increases

Engineering Contradiction:
Improvethermal stabilityVSAvoidprotein structure complexity
Core Design Contradiction:
TemperatureVSDevice complexity

Solution Approach 1:

The patent applies parameter changes by systematically modifying specific amino acid positions (28 and 52) in the xylanase polypeptide sequence. Through site-directed mutagenesis, the inventors changed amino acid residues at these positions to create variants with improved thermal stability. The disulfide bridge formation between cysteine residues at positions 3-36, 5-34, 20-41, 34-41, or 36-41 represents a structural parameter change that reinforces the protein framework, enabling the enzyme to maintain activity at higher temperatures while preserving catalytic function.

Inventive Principle:
Principle #35Parameter changes

2Adaptability or versatility

If multiple amino acid substitutions are made to enhance industrial applicability, then versatility in harsh conditions improves, but manufacturing complexity increases

Engineering Contradiction:
Improveindustrial applicabilityVSAvoidmanufacturing complexity
Core Design Contradiction:
Adaptability or versatilityVSEase of manufacture

Solution Approach 1:

The patent implements local quality by making targeted amino acid substitutions at specific positions (28 and 52) rather than throughout the entire polypeptide chain. This localized modification approach allows the protein to gain improved thermal and pH stability while minimizing the complexity of manufacturing. The disulfide bridges are formed at specific strategic locations within the protein structure, providing localized structural reinforcement that enhances overall stability without requiring complex global restructuring of the protein or manufacturing process.

Inventive Principle:
Principle #3Local quality

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 polypeptide demonstrates improved thermal stability and resistance, enabling its effective use in diverse industrial applications.

Implementation Method 1

Xylanase (EC 3.2.1.8) is a hydrolase that randomly degrades the β-1,4 backbone of xylan

Methodology Applied
Scientific EffectHydrolysis: Hydrolysis

Data Source

PatentUS12577549B2Modified polypeptide having xylanase activity
Publication Date: 2026.03.17 KEMIN INDUSTRIES INC
  • US12577549B2 patent drawing
  • US12577549B2 patent drawing
  • US12577549B2 patent drawing

AI summary

The present disclosure relates to a modified polypeptide having xylanase activity and the use thereof.