AI-Driven Thermophile Discovery
Using AI-guided metagenomic analysis to discover naturally thermostable Phytase starting points from environmental thermophilic organisms.
Phytases are crucial feed enzymes used in the animal nutrition industry to hydrolyze phytate (inositol hexaphosphate), the primary storage form of phosphorus in plants. This hydrolysis releases digestible phosphorus, calcium, and other essential minerals, significantly reducing the need for costly mineral supplementation and decreasing phosphorus excretion, thereby lowering environmental impact. However, commercial Phytases face challenges including inactivation during feed pelleting (high temperature/moisture), low activity across the varying pH conditions of the animal gastrointestinal (GI) tract, and insufficient phytate degradation efficiency. This often necessitates high enzyme dosages or supplementary chemical pre-treatment.
Our specialized enzyme optimization services are focused on creating Phytase variants with superior robustness and efficacy. Our core objectives include: engineering superior thermal stability for pelleting tolerance; enhancing activity across the broad physiological pH range of the GI tract; and maximizing the degradation efficiency of phytate for optimal mineral release. Consult with our experts to design a customized strategy that ensures comprehensive phytate degradation and cost-effective feed formulation.
Get a QuoteThe maximum efficacy of Phytases in modern feed processing and animal nutrition is limited by the following technical barriers:
Our engineering platforms are dedicated to resolving these complex stability and activity challenges for the feed industry.
We apply integrated protein engineering strategies to enhance your target Phytase:
Superior Pelleting Tolerance
Using Directed Evolution to introduce stabilizing mutations, ensuring high residual activity after exposure to the heat and shear stress of the pelleting process.
Broadened pH Activity Range
Engineering the enzyme's active site to optimize its catalytic performance across the wide physiological pH range (e.g., pH 2.5 to 6.0) found throughout the animal GI tract.
Increased Degradation Efficiency
Maximizing the enzyme's catalytic speed and ensuring complete hydrolysis of phytate and its intermediate forms for maximal phosphorus and mineral release.
Resistance to Digestive Proteases
Using Rational Design to modify exposed loops and cleavage sites, increasing the enzyme's half-life against stomach and intestinal proteases.
Our experts are ready to apply these integrated capabilities to achieve next-generation Phytases with unparalleled feed stability and mineral release efficacy.
We leverage a suite of cutting-edge platforms to deliver highly functional enzyme variants:
AI-Driven Thermophile Discovery
Using AI-guided metagenomic analysis to discover naturally thermostable Phytase starting points from environmental thermophilic organisms.
Directed Evolution for Pellet Stability
We utilize HTS platforms optimized to screen for variants that maintain high activity after simulated pelleting heat and moisture stress.
Rational Design for pH Adaptation
Using structural modeling to rationally design mutations that shift the enzyme's pKa values, optimizing activity across the acidic stomach and neutral intestine environments.
Thermal and pH Activity Profiling
We offer full stability profiling, including half-life measurement after high-temperature exposure and comprehensive activity testing across pH 2.5 to pH 6.0.
Integrated Enzyme Production and Formulation
Specialized custom production services optimized for high-yield expression, suitable for direct incorporation into industrial feed processing.
Partner with us to harness these platforms for next-generation feed enzyme performance and cost reduction.
Our enzyme optimization projects follow a flexible, milestone-driven workflow:
Technical communication is maintained throughout the project. We encourage potential clients to initiate a consultation to discuss their specific feed enzyme challenges and explore how our technologies can achieve superior performance and bioavailability.
We provide comprehensive support, including:
How do you improve thermal stability for pelleting?
We use Directed Evolution coupled with high-throughput screening under simulated pelleting conditions (80℃-95℃) to select for variants with enhanced structural rigidity, such as those with optimized hydrophobic cores and reinforced surface interactions.
What is the main strategy for broadening the pH activity profile?
The primary strategy is Rational Design guided by structural modeling. We engineer charged or polar residues near the active site to maintain an optimal protonation state for catalysis across both the acidic (stomach) and neutral (intestine) pH environments.
How is protease resistance achieved?
We use Rational Design to identify and mutate exposed proteolytic cleavage sites on the enzyme's surface. This modification prevents premature degradation by endogenous proteases in the animal GI tract, increasing the functional half-life.
What methods are used to test phytate degradation efficacy?
We use standard protocols involving the measurement of released inorganic phosphate (Pi) from phytate-containing substrates under simulated digestive conditions. Efficacy is quantified via colorimetric assays or high-performance ion chromatography to confirm maximum mineral release.
If your question is not addressed through these resources, you can fill out the online form below and we will answer your question as soon as possible.
CD Biosynsis
Copyright © 2025 CD Biosynsis. All rights reserved.