Variant Phytase Enzyme Stability in Feed Pelleting
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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 under processing conditions like pelleting, which further complicates their effectiveness.
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 in the gastrointestinal tract of animals, thereby improving nutrient availability and reducing phosphorus excretion.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If wild-type phytase is used in feed processing, then phosphorus release function is provided, but the enzyme is inactivated by temperature during pelleting process
Solution Approach 1:
The patent applies parameter changes by modifying amino acid residues in the phytase protein structure to alter its thermal stability parameters. Specific substitutions at positions 60, 65, 69, 73, 74, and 79 change the enzyme's conformational properties, allowing it to maintain catalytic activity at higher temperatures during feed pelleting while preserving its phosphorus-releasing function.
2Reliability
If phytase is added to improve nutrient availability, then phosphorus excretion is reduced, but the enzyme is inactivated by low pH and pepsin in the gastrointestinal tract
Solution Approach 1:
The patent modifies the phytase enzyme's structural parameters through amino acid substitutions that enhance its resistance to acidic conditions and proteolytic degradation. These changes stabilize the enzyme's three-dimensional structure under gastrointestinal conditions, allowing it to remain active in the low pH environment and resist pepsin digestion, thereby maintaining its function throughout the digestive tract.
3Quantity of substance
If inorganic phosphorus is supplemented to feeds, then nutritional deficiencies are corrected, but feeding costs increase significantly
Solution Approach 1:
The patent employs the self-service principle by enabling the phytase enzyme to autonomously release bound phosphorus from phytate and other phosphorus-containing compounds in the feed. This self-catalyzed phosphorus liberation makes endogenous phosphorus sources bioavailable to animals, eliminating or reducing the need for expensive inorganic phosphorus supplements while maintaining adequate nutrition.
4Quantity of substance
If phytase is exposed to high pressure during processing, then cell wall rupture improves nutrient availability, but enzyme activity is reduced
Solution Approach 1:
The patent applies parameter changes by modifying the phytase enzyme's structural parameters through amino acid substitutions that enhance its mechanical stability. These modifications strengthen the protein's three-dimensional structure, allowing it to withstand the high pressure and mechanical stress of feed processing while maintaining catalytic function and continuing to release phosphorus effectively.
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 environmental phosphorus pollution, while also being more cost-effective by maintaining activity under conditions that typically inactivate wild-type phytases.
Implementation Method 1
Phytase is a phosphatase that catalyzes the hydrolysis of O—P bonds in phytate and releases inorganic usable phosphorous
Data Source
AI summary
The present invention relates to variant phytase enzymes and their use thereof.