Mannanase Variant Stability via Non-Glycosylated Position 283
Find Innovative SolutionsGenerate Solutions
Solution Overview
Problem
Mannans in industrial applications, such as laundry and animal feed, pose challenges due to their poor solubility and high water binding capacity, leading to viscosity issues and reduced digestibility, and existing mannanases lack stability in varying storage and use conditions.
Innovation Solution
Development of mannanase variants with a non-glycosylated amino acid at position 283, which exhibit improved stability and activity, and enzyme compositions including these variants, preservatives, stabilizers, and additional enzymes for enhanced performance in industrial processes.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If wild type mannanase is used, then mannan degradation activity is achieved, but stability in varying storage and use conditions is poor
Solution Approach 1:
The patent applies parameter changes by modifying specific amino acid residues (positions 283, 285, 300, 340, 400, 419, 433, or 446) in the mannanase enzyme sequence. These mutations alter the enzyme's structural and functional parameters to achieve both high stability in storage and use conditions and maintained mannan degradation activity, resolving the contradiction between stability and productivity.
2Productivity
If mannanase is used in laundry applications, then mannan degradation occurs, but enzyme stability in detergent conditions is reduced
Solution Approach 1:
The patent modifies specific amino acid parameters at positions 283, 285, 300, 340, 400, 419, 433, or 446 to enhance the enzyme's resistance to detergent conditions while maintaining its mannan degradation capability in laundry applications.
Solution Approach 2:
The patent creates an enzyme composition combining the modified mannanase with detergent formulations and stabilizers, creating a composite system that maintains enzyme activity and stability in the challenging detergent environment during laundry processing.
3Productivity
If wild type mannanase is produced in host cell, then enzyme production is achieved, but specific activity and yield are limited
Solution Approach 1:
The patent changes amino acid parameters at glycosylation-related positions (283, 285, 300, 340, 400, 419, 433, or 446) to optimize the enzyme's production characteristics in host cells, resulting in improved specific activity and yield while controlling post-translational modification.
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 variants demonstrate improved stability and specific activity, effectively degrading mannan in laundry detergents and animal feed, enhancing digestibility and nutritional value, while maintaining performance across different temperatures and conditions.
Implementation Method 1
Mannanase increases average daily gain, feed efficiency, weight uniformity and livability in all monogastric animals. Enzymatic degradation of mannans reduces digesta viscosity of high water soluble mannans and leads to production of manno-oligosaccharides
Implementation Method 2
N-linked glycosylation of proteins is a type of post-translational modification where a sugar molecule oligosaccharide known as glycan is attached to an amide nitrogen group of an asparagine (Asn, N) residue of a protein.
Data Source
AI summary
Variants of mannanase, compositions including the variants, to methods for their production to methods of using the variants to degrade and modify mannan containing material.