Engineered Phytase Cyclization for Thermal Stability
Find Innovative SolutionsGenerate Solutions
Solution Overview
Problem
Current phytases used in animal feeds face challenges with thermal stability during pelleting processes, leading to reduced efficacy, and there is a risk of allergenicity due to their stability in gastric environments.
Innovation Solution
Engineered phytases are created by fusing a target phytase with specific binding elements like inteins, coiled-coil dimerization domains, or tag and catcher domains to enhance thermal stability and cyclization, reducing gastric stability, thereby improving performance and safety.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Productivity
If phytase is added to animal feeds to improve phosphate absorption, then animal growth efficiency is improved, but the phytase loses activity during thermal processing (pelleting)
Solution Approach 1:
The patent creates composite protein structures by fusing phytase with binding elements (inteins, coiled-coil domains, tag-catcher pairs) to form cyclized composite molecules that maintain phytase activity while gaining thermal stability during pelleting processes
Solution Approach 2:
The patent modifies the structural parameters of phytase by introducing cyclization through binding elements, changing the protein's physical state from linear to cyclic structure, which fundamentally alters its thermal stability characteristics without affecting its catalytic function
2Reliability
If phytase is engineered to improve thermal stability, then pelleting process efficacy is improved, but gastric stability increases leading to potential allergenicity
Solution Approach 1:
The patent introduces conditional stability by designing phytase variants that are stable under processing conditions (thermal) but become unstable under digestive conditions (gastric), creating a dynamic response to different environmental conditions through pH-sensitive structural changes
3Reliability
If binding elements are fused to cyclize phytase, then thermal stability is enhanced, but device complexity increases
Solution Approach 1:
The patent employs self-organizing binding elements that automatically cyclize the phytase structure through intrinsic binding affinities (intein splicing, coiled-coil formation, tag-catcher recognition) without requiring external assistance or complex processing steps
Solution Approach 2:
The patent divides the phytase structure into functional segments (catalytic domain and binding elements) that can be independently designed and assembled, allowing modular construction of cyclized variants with different stability profiles
Data Source
AI summary
Methods for enhancing phytase thermal stability by fusing binding elements to target phytases are provided. Engineered phytases that include binding elements fused to target phytases to cause cyclization of the engineered phytases and enhance thermal stability of the target phytases are described. Engineered nucleic acids encoding engineered phytases and hosts engineered to express engineered nucleic acids are also provided. Methods for incorporating engineered phytases in animal feed and animal feed including the same are described.