Thermostable Phytase Variants for High-Temperature Feed Processing
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Solution Overview
Problem
Commercially available phytases lack thermostability, which limits their effectiveness in industrial processes and feed processing applications where high temperatures are involved, resulting in reduced enzyme activity and stability.
Innovation Solution
Development of phytase variants with specific amino acid substitutions, such as at positions 33, 45, 54, 89, 101, 139, 166, 175, 176, 179, 184, 185, 202, 262, 280, 340, 393, 397, and 398, that enhance thermostability, allowing the enzymes to maintain activity and stability at high temperatures, and providing improved stability against proteases.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If commercially available phytases are used in industrial processes, then phytate degradation activity is provided, but thermostability is insufficient leading to reduced enzyme activity and stability at high temperatures
Solution Approach 1:
The patent applies parameter changes by modifying amino acid sequences at specific positions (1, 33, 45, 54, 89, 101, 139, 166, 175, 176, 179, 184, 185, 202, 262, 280, 340, 393, 397, 398, 412) to alter the thermal stability parameters of the phytase enzyme. These sequence modifications enable the enzyme to maintain its structural integrity and catalytic activity at elevated temperatures without compromising its phytate degradation function.
Solution Approach 2:
The patent implements local quality by introducing specific amino acid substitutions at targeted positions within the enzyme structure rather than uniform modifications throughout. This localized approach allows specific regions of the phytase molecule to gain enhanced thermostability while preserving the catalytic active sites and overall enzymatic function required for phytate degradation.
2Stability of the object's composition
If amino acid substitutions are introduced to enhance thermostability, then stability at high temperatures is improved, but enzyme structure complexity increases
Solution Approach 1:
The patent utilizes parameter changes by systematically modifying specific amino acid positions to achieve thermostability enhancement. By focusing changes on predetermined positions (1, 33, 45, 54, 89, 101, 139, 166, 175, 176, 179, 184, 185, 202, 262, 280, 340, 393, 397, 398, 412), the enzyme structure complexity is minimized while still achieving the desired stability improvement.
3Productivity
If phytase is exposed to high temperatures during feed processing, then feed processing efficiency is maintained, but enzyme recovery is reduced due to loss of phytase activity
Solution Approach 1:
The patent applies parameter changes by modifying the thermal stability parameters of the phytase enzyme through amino acid substitutions. This enables the enzyme to withstand the high temperatures required for efficient feed processing while maintaining sufficient activity and allowing for better enzyme recovery, thus resolving the contradiction between processing efficiency and enzyme recovery.
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 thermostable phytase variants exhibit improved recovery and stability during demanding processing conditions, such as high-temperature feed processing, maintaining enzyme activity and increasing the availability of phosphate and other nutrients for monogastric animals.
Implementation Method 1
Phytases are a group of phosphatase enzymes that catalyse the hydrolysis of phytic acid
Data Source
AI summary
A phytase variant, a method for its manufacturing, an animal feed, a feed supplement, a dry and a liquid formulation, a method of degrading phytic acid, a method of manufacturing a phytase variant, a method of manufacturing a feed pellet, and a recombinant host cell configured to produce at least one polypeptide are disclosed, wherein the phytase variant comprises amino acid substitutions and has at least 95% amino acid sequence identity with amino acids of SEQ ID NO: 1.