Xylanase Mutants With Targeted Residue Changes for Higher Specific Activity
Find Innovative SolutionsGenerate Solutions
Solution Overview
Problem
Current xylanases have limitations in specific activity, which affects their application in industries such as feed, papermaking, and biomass energy, leading to increased production costs and reduced efficiency in nutrient digestibility in livestock and poultry feed.
Innovation Solution
Development of xylanase mutants with specific amino acid substitutions, including positions 78, 143, 148, 163, 177, and 206, resulting in improved specific activity, with enhancements ranging from 12.3% to 106.4% compared to wild-type xylanase.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If wild-type xylanase is used, then production cost is reduced, but specific activity is insufficient
Solution Approach 1:
The patent applies parameter changes by modifying specific amino acid positions (78, 143, 148, 163, 177, 206) in the xylanase protein sequence to improve specific activity. The mutant xylanase achieves 12.3%-106.4% higher specific activity than wild-type while maintaining production feasibility through targeted mutagenesis of the gene sequence.
2Productivity
If xylanase with higher specific activity is developed, then production cost decreases, but enzyme structure complexity increases
Solution Approach 1:
The patent applies local quality by introducing mutations at specific localized positions (78, 143, 148, 163, 177, 206) rather than throughout the entire protein structure. This targeted approach improves specific activity while minimizing structural complexity changes, as only 6 specific residues are modified out of the total protein sequence.
3Reliability
If conventional xylanase is used in feed, then feed cost is reduced, but nutrient digestibility is insufficient
Solution Approach 1:
The patent applies parameter changes by modifying the xylanase enzyme's specific activity through amino acid substitutions, which directly enhances its ability to degrade xylan in feed. This improved enzymatic activity increases nutrient digestibility in livestock and poultry, addressing the technical contradiction between digestibility and feed cost.
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 xylanase mutants demonstrate significantly increased specific activity, reducing production costs and enhancing their applicability in the feed industry by improving nutrient digestibility and reducing viscous feces excretion in livestock and poultry.
Implementation Method 1
Xylanase refers to the general term for enzymes that can degrade xylan into xylo-oligosaccharides and xylose
Data Source
AI summary
Provided is a xylanase mutant having improved specific activity, comprising any one or more mutation sites of M78F, V143I, R148K, F163W, I177V, and V206L. The specific activity of the mutant is improved, the production cost of xylanase is reduced, and the mutant can be used in feed.