Xylanase Polypeptide Thermal Stability via Amino Acid Substitutions
Find Innovative SolutionsGenerate Solutions
Solution Overview
Problem
Existing xylanases have low thermal stability, making it difficult to apply them in various industrial fields that require activity under harsh conditions such as high temperature and basic conditions.
Innovation Solution
A modified polypeptide with xylanase activity is developed, which includes specific amino acid substitutions at positions 2, 3, 28, 38, 56, 62, 65, 80, 93, 114, 144, 146, 149, 151, 161, and 165, enhancing its thermal tolerance and stability.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If native xylanase is used, then xylanase activity is maintained, but thermal stability is low
Solution Approach 1:
The patent applies parameter changes by modifying specific amino acid residues at positions 2, 3, 28, 38, 56, 62, 65, 80, 93, 114, 144, 146, 149, 151, 161, and 165 of the xylanase protein sequence. These amino acid substitutions alter the protein's structural and functional parameters to achieve enhanced thermal stability while preserving catalytic activity under harsh conditions including high temperature and basic pH environments.
2Adaptability or versatility
If xylanase is applied in harsh conditions (high temperature, basic conditions), then industrial application is enabled, but enzyme activity is lost
Solution Approach 1:
The patent applies local quality by making targeted modifications at specific amino acid positions within the xylanase protein structure. Each position (2, 3, 28, 38, 56, 62, 65, 80, 93, 114, 144, 146, 149, 151, 161, and 165) was selectively modified to confer specific functional properties, allowing the enzyme to adapt to harsh industrial conditions while maintaining localized catalytic functionality.
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 exhibits improved thermal tolerance and stability, allowing it to maintain activity under conditions that would inactivate native xylanases, thus expanding its applications in industrial fields.
Implementation Method 1
Xylanase (EC 3.2.1.8) is a hydrolase that randomly degrades the β-1,4 backbone of xylan
Data Source
AI summary
The present disclosure relates to a modified polypeptide having xylanase activity and use thereof.