Mutant β-glucosidase Reducing Lignin Adsorption
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Solution Overview
Problem
Current biomass saccharification enzymes, particularly β-glucosidase from Trichoderma genus, exhibit low activity due to nonspecific adsorption on lignin residues, reducing efficiency in biomass conversion to glucose.
Innovation Solution
A mutant β-glucosidase is developed by substituting amino acid residues at specific positions with asparagine, reducing nonspecific adsorption and maintaining high activity in the presence of saccharification residues, thereby enhancing biomass saccharification efficiency.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Productivity
If β-glucosidase from Trichoderma genus is used for biomass saccharification, then the enzyme can degrade cellulose into glucose, but the enzyme activity is reduced due to nonspecific adsorption on lignin
Solution Approach 1:
The patent applies parameter changes by modifying the amino acid sequence of β-glucosidase at specific positions (787, 790, and/or 797) to alter the enzyme's interaction properties with lignin. This chemical parameter modification reduces nonspecific adsorption while preserving catalytic activity, directly resolving the contradiction between maintaining enzyme activity and avoiding harmful adsorption.
Solution Approach 2:
The patent applies local quality by making targeted modifications at specific amino acid positions (787, 790, 797) rather than altering the entire enzyme structure. This localized modification approach changes the interaction properties at specific regions of the enzyme that contact lignin, while leaving the catalytic core intact, thus resolving the contradiction between activity and adsorption.
2Reliability
If biomass saccharification enzyme adsorbs on lignin, then the enzyme may be stabilized on the substrate, but the enzyme activity is reduced due to nonspecific adsorption
Solution Approach 1:
The patent modifies specific amino acid parameters at positions 787, 790, and/or 797 to change the enzyme's surface properties. This parameter change allows the enzyme to maintain stable interaction with biomass substrate while reducing nonspecific adsorption on lignin, thereby preserving enzyme activity and resolving the contradiction between stability and productivity.
3Productivity
If amino acid residues are substituted to reduce nonspecific adsorption, then enzyme activity in the presence of lignin is improved, but the enzyme structure is modified
Solution Approach 1:
The patent applies local quality by substituting amino acid residues at specific positions (787, 790, 797) rather than making widespread structural changes. This localized modification approach improves saccharification efficiency by reducing lignin adsorption while minimizing disruption to the overall enzyme structure and its catalytic function.
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 mutant β-glucosidase demonstrates improved activity and reduced adsorption on lignin, leading to increased saccharification efficiency and stability during biomass conversion.
Implementation Method 1
a β-glucosidase (BGL) which produces glucose by hydrolyzing the cellobiose produced by these enzymes
Implementation Method 2
the mutant β-glucosidase demonstrates improved activity and reduced adsorption on lignin, leading to increased saccharification efficiency
Implementation Method 3
a biomass saccharification enzyme also adsorbs on components which are not degraded by the enzyme, such as lignin, ash, and other components, and this called the nonspecific adsorption
Data Source
AI summary
Provided is a mutant β-glucosidase capable of more efficiently saccharifying biomass. A mutant β-glucosidase comprising an amino acid sequence having at least 80% sequence identity to SEQ ID NO: 1, wherein the amino acid sequence has asparagine at one or more positions selected from the group consisting of positions corresponding to positions 787, 790, and 797 of SEQ ID NO: 1, and has β-glucosidase activity.