Variant Phytases Thermostability pH Stability Feed Processing
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Solution Overview
Problem
Phytate in plant-based feeds is indigestible and acts as an anti-nutritional factor, leading to inefficient protein digestion and mineral deficiencies in animals, requiring costly supplementation with inorganic phosphorus, and existing phytases are not stable enough to withstand processing conditions like heat and pH variations.
Innovation Solution
Development of variant phytases with specific amino acid substitutions that enhance thermostability and pH stability, allowing them to maintain activity during feed processing and improve nutrient availability in animal feeds.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If conventional phytase is used in animal feed, then phosphorus availability is improved, but the enzyme is inactivated by heat during feed processing
Solution Approach 1:
The patent applies parameter changes by modifying the amino acid sequence of phytase through site-directed mutagenesis. Specific amino acid residues were mutated to create thermostable variants that maintain enzymatic activity at elevated temperatures (up to 80°C) during feed processing, thereby resolving the contradiction between enzyme reliability and heat stability.
2Reliability
If conventional phytase is used in animal feed, then phosphorus availability is improved, but the enzyme is inactivated by low pH in the gastrointestinal tract
Solution Approach 1:
The patent modifies the pH stability parameters of phytase through amino acid sequence changes. Specific residues were mutated to enhance the enzyme's resistance to acid inactivation, allowing it to function effectively in the low pH environment of the animal gastrointestinal tract while maintaining phosphorus availability.
3Quantity of substance
If inorganic phosphorus is supplemented in feeds, then phosphorus deficiency is corrected, but production costs increase
Solution Approach 1:
The patent enables the feed enzyme to perform the function of inorganic phosphorus supplementation by making phytate accessible to monogastric animals. The thermostable and acid-stable phytase variants allow animals to digest phytate and release bound phosphorus, making the feed system self-sufficient regarding phosphorus without requiring expensive inorganic supplements.
4Productivity
If phytase is added to improve nutrient availability, then protein digestion is enhanced, but the enzyme is degraded by proteases in the gastrointestinal tract
Solution Approach 1:
The patent modifies the protease resistance parameters of phytase through amino acid sequence mutations. The engineered variants have altered surface residues that protect the enzyme from degradation by gastric and intestinal proteases, thereby maintaining enzyme stability and ensuring sustained nutrient digestion efficiency throughout the gastrointestinal tract.
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 variant phytases provide improved thermal and pH stability, leading to enhanced nutrient accessibility and reduced phosphorus excretion, thus addressing the nutritional deficiencies and cost issues associated with traditional phytase instability.
Implementation Method 1
Phytase is a phosphatase that catalyzes the hydrolysis of O—P bonds in phytate and releases inorganic usable phosphorous
Implementation Method 2
Phytase is a phosphatase that catalyzes the hydrolysis of O—P bonds in phytate
Data Source
AI summary
The present invention relates to variant phytase enzymes and their use thereof.