Modified Xylanase C-Terminal Deletion for Thermal Stability
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Solution Overview
Problem
Existing xylanases have limitations in activity and stability, particularly when the cellulose-binding domain is removed, which can lead to reduced enzyme activity.
Innovation Solution
A modified xylanase is developed by deleting the cellulose-binding module 1 (CBM1) of the xylanase produced by Talaromyces cellulolyticus CF-2612 strain, resulting in a polypeptide with enhanced enzyme activity and stability at higher temperatures and various pH levels.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Productivity
If the cellulose-binding domain (CBM1) is removed from xylanase, then the enzyme activity is significantly increased, but the enzyme may lose stability and binding capability
Solution Approach 1:
The patent removes the cellulose-binding domain (CBM1) from the xylanase enzyme structure. This extraction of a specific functional module results in increased enzymatic activity while maintaining stability through the remaining structural components, resolving the contradiction between activity enhancement and stability preservation
Solution Approach 2:
The patent modifies the enzyme's structural parameters by deleting specific amino acid residues (12-73 amino acid residues) corresponding to the CBM1 domain. This parameter change in the protein sequence leads to altered enzymatic properties, achieving higher activity while maintaining thermal and pH stability
2Productivity
If the cellulose-binding domain is removed from xylanase, then the enzyme activity is increased, but the enzyme may become less effective in biomass processing
Solution Approach 1:
The cellulose-binding domain is extracted from the enzyme, and the patent demonstrates that the remaining enzyme structure retains sufficient functionality for biomass processing applications, achieving both activity enhancement and process effectiveness
Solution Approach 2:
Instead of adding binding domains to enhance effectiveness, the patent inverts the approach by removing the binding domain to achieve higher activity, relying on the catalytic domain's inherent capabilities to process biomass effectively
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 xylanase exhibits 1.3 to 1.9 times higher enzyme activity compared to wild-type xylanase at 45°C and maintains stability at 70°C, with improved thermal and pH stability, making it more effective in biomass processing.
Implementation Method 1
Xylanase is a generic term for a group of enzymes that hydrolyze xylan
Implementation Method 2
xylanase is used in the enzymatic degradation of agricultural waste for alcohol fuels, enzymatic treatment for liberating saccharides in animal feed
Data Source
AI summary
Provided is a modified xylanase. The polypeptide has xylanase activity and has an amino acid sequence with deletion of at least 12 consecutive amino acid residues at the C-terminus of the amino acid sequence of SEQ ID NO: 1 or an amino acid sequence having at least 90% identity with the amino acid sequence of SEQ ID NO: 1.