GH26 Mannanase Polypeptides for Efficient Mannan Hydrolysis
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Solution Overview
Problem
Existing technologies are inefficient in degrading mannan-containing substances, limiting their application in areas such as detergent stain removal, bioethanol production from softwood, animal feed improvement, and coffee extract hydrolysis.
Innovation Solution
Development of polypeptides from glycoside hydrolyase family 26 with mannanase activity, including variants and fragments, for use in detergent compositions and other applications, along with nucleic acid constructs and host cells for production.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Productivity
If existing mannanase technologies are used, then mannan degradation can be achieved, but the degradation efficiency is insufficient
Solution Approach 1:
The patent applies parameter changes by modifying the amino acid sequence of mannanase polypeptides through specific substitutions, deletions, and/or insertions to create variants with improved catalytic activity. The polypeptides are defined by sequence identity thresholds (≥80%, ≥85%, ≥90%, ≥95%, or ≥98% to reference sequences), representing systematic parameter optimization to enhance mannan degradation efficiency while maintaining functional reliability
2Productivity
If polypeptide variants with high sequence identity are developed, then mannanase activity is improved, but the complexity of polypeptide characterization increases
Solution Approach 1:
The patent establishes a hierarchical parameter system where polypeptides are classified by sequence identity thresholds (80%, 85%, 90%, 95%, 98%) to reference sequences, creating a structured framework that balances activity improvement with manageable characterization complexity. This parameter-based classification allows systematic optimization without requiring complete re-characterization of each variant
Solution Approach 2:
The patent uses reference polypeptide sequences (SEQ ID NOs: 1-20) as templates or copies that define the core structure. Variants are generated by making limited modifications to these established sequences, allowing researchers to leverage the known properties of reference sequences while exploring improved variants, thereby reducing the overall characterization burden
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 polypeptides effectively degrade mannan-containing substances, enhancing applications in detergents, bioethanol production, animal feed, and coffee extract processing.
Implementation Method 1
endo-1,4-β-mannanases (EC 3.2.1.78), which hydrolyze the internal glycoside bonds in the mannan backbone
Implementation Method 2
The main enzyme type participating in the degradation of mannans are endo-1,4-β-mannanases
Data Source
AI summary
The present invention relates to polypeptides having mannanase activity, catalytic domains, and carbohydrate binding modules, and polynucleotides encoding the polypeptides, catalytic domains, and carbohydrate binding modules. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides, catalytic domains, and carbohydrate binding modules.