Glutamine Synthetase Mutations for L-Glutamine Yield
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Solution Overview
Problem
Current methods for producing L-glutamine are inefficient, and there is a need to enhance the activity of glutamine synthetase to achieve high-yield production.
Innovation Solution
A modified polypeptide of glutamine synthetase is developed by substituting specific amino acids at positions 401, 402, or 404 with different amino acids, leading to increased L-glutamine production without affecting the growth rate.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Productivity
If wild-type glutamine synthetase is used, then the microorganism maintains normal growth rate, but L-glutamine production efficiency is low
Solution Approach 1:
The patent applies parameter changes by substituting specific amino acid residues (positions 401, 402, or 404) in the glutamine synthetase protein sequence. These point mutations modify the enzyme's catalytic properties and substrate binding characteristics, thereby enhancing L-glutamine production efficiency while preserving the microorganism's growth rate through controlled biochemical parameter optimization
2Productivity
If glutamine synthetase activity is enhanced through mutation, then L-glutamine production increases, but enzyme stability may be compromised
Solution Approach 1:
The patent applies local quality by implementing site-directed mutagenesis at specific localized positions (401, 402, or 404) within the glutamine synthetase molecule. These targeted amino acid substitutions modify only the local catalytic or binding regions of the enzyme, enhancing its activity toward L-glutamine synthesis while preserving the overall structural stability and folding of the protein through careful selection of conservative or context-appropriate amino acid replacements
Data Source
AI summary
The present disclosure relates to a modified polypeptide of glutamine synthetase having enhanced activity and a method of producing L-glutamine using the same. Since production of L-glutamine may be increased by using the novel modified polypeptide without a decrease in a growth rate compared to wild-type strains having glutamine synthetase activity, the modified polypeptide may be widely used for mass production of L-glutamine.