GH25 Lysozyme Variants for Animal Feed Pathogen Control
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Solution Overview
Problem
Current animal feed additives, such as traditional antimicrobial growth promoters, are ineffective against certain bacterial pathogens like Staphylococcus aureus and do not adequately promote animal health, and existing GH25 lysozymes have limited activity against Micrococcus lysodeikticus and Lactobacillus johnsonii.
Innovation Solution
Development of GH25 lysozymes with improved activity against Micrococcus lysodeikticus and Lactobacillus johnsonii, including specific polypeptides with high sequence identity and variants with amino acid substitutions, deletions, or insertions, for use in animal feed to enhance bacterial cell wall degradation and intestinal health.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If traditional antimicrobial growth promoters are used, then animal growth promotion is achieved, but effectiveness against certain bacterial pathogens like Staphylococcus aureus is insufficient
Solution Approach 1:
The patent modifies the enzymatic parameters of GH25 lysozymes through amino acid sequence variations and structural adjustments to enhance their catalytic activity and substrate specificity, enabling effective degradation of peptidoglycan in diverse bacterial cell walls including those of S. aureus and L. johnsonii
Solution Approach 2:
The engineered GH25 lysozymes are designed to perform multiple functions: degrading cell walls of both Gram-positive bacteria (S. aureus, M. lysodeikticus) and Lactobacillus species, thereby providing broad-spectrum antimicrobial activity while maintaining growth promotion effects
2Productivity
If existing GH25 lysozymes are used in animal feed, then some bacterial cell wall degradation occurs, but lytic activity against Micrococcus lysodeikticus and Lactobacillus johnsonii is limited
Solution Approach 1:
The patent optimizes the kinetic parameters of GH25 lysozymes by introducing specific amino acid substitutions that increase kcat and decrease Km for peptidoglycan substrates, resulting in enhanced and more consistent lytic activity against M. lysodeikticus and L. johnsonii
Solution Approach 2:
The invention creates engineered versions of GH25 lysozymes by copying and modifying the catalytic domain structure, using computational modeling and directed evolution to produce variants with superior and more reliable enzymatic activity
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 improved GH25 lysozymes demonstrate enhanced lytic activity against bacterial cell walls, effectively reducing dead bacterial cells and debris in animal intestines, thereby improving animal health and intestinal well-being.
Implementation Method 1
The enzyme causes the hydrolysis of bacterial cell walls by cleaving the glycosidic bonds of peptidoglycan
Implementation Method 2
Lysozyme is an O-glycosyl hydrolase produced as a defensive mechanism against bacteria by many organisms
Implementation Method 3
The enzyme cleaves the glycosidic bond between carbon number 1 of N-acetylmuramic acid and carbon number 4 of N-acetyl-D-glucosamine
Implementation Method 4
After having their cell walls weakened by lysozyme action, bacterial cells lyse as a result of unbalanced osmotic pressure
Data Source
AI summary
The present disclosure relates animal feed or animal feed additives comprising one or more polypeptides having lysozyme activity. The present disclosure also relates to polypeptides having lysozyme activity, polynucleotides encoding the polypeptides nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides.