Polypeptide Enzyme Degrades Deoxynivalenol Toxin
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Solution Overview
Problem
Current methods for detoxifying deoxynivalenol (DON) are limited by the need for specific cultivation requirements of microorganisms and the inefficacy of binding agents due to DON's hydrophilic nature, making it difficult to remove from food and feed, and there is a need for a microorganism-free enzyme formulation for safe and fast detoxification.
Innovation Solution
A polypeptide with a specific amino acid sequence (SEQ ID NO: 1) capable of degrading DON to 7-one-8-hydroxy-8-ene-DON, which is less toxic, is used to modify the C7-atom of DON, altering its toxicity and structure, thereby detoxifying it.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If microorganisms are used for DON detoxification, then DON degradation capability is improved, but specific cultivation requirements increase complexity and reduce ease of manufacture
Solution Approach 1:
The patent extracts the essential detoxification function from the entire microorganism system and isolates it into a specific enzyme (polypeptide with at least 70% identity to SEQ ID NO: 1). This enzyme can be produced through recombinant expression in simple host systems like E. coli, eliminating the need for complex microorganism cultivation while retaining the DON degradation capability. The enzyme is then formulated for direct application.
Solution Approach 2:
The patent introduces a recombinant expression system as an intermediary between the natural microorganism and the final application. The gene encoding the detoxification enzyme is cloned into expression vectors and expressed in simplified host organisms, creating a practical production system that avoids the cultivation complexities of the original toxin-degrading microorganisms while maintaining their beneficial function.
2Reliability
If binding agents are used to remove DON, then removal capability is improved, but effectiveness deteriorates due to DON's hydrophilic nature
Solution Approach 1:
The patent fundamentally changes the mechanism from physical binding (which fails due to DON's hydrophilic properties) to enzymatic degradation. The polypeptide enzyme chemically modifies DON by hydroxylating it at the C7 position, converting it to 7-one-8-hydroxy-8-ene-DON, which has altered properties including reduced toxicity and changed solubility characteristics, thereby overcoming the limitation of hydrophilic interaction.
3Reliability
If chemical or physical treatment is applied to DON, then detoxification is attempted, but effectiveness is insufficient
Solution Approach 1:
The patent replaces ineffective chemical or physical treatment methods with a biological enzymatic system. The polypeptide enzyme performs specific chemical transformation of DON through hydroxylation, a precise biochemical reaction that chemically alters the toxin structure and reduces its toxicity, achieving where conventional physical or chemical methods failed.
Solution Approach 2:
The patent transforms the harmful DON toxin into a beneficial or harmless product through enzymatic conversion. The enzyme catalyzes the transformation of DON into 7-one-8-hydroxy-8-ene-DON, which has reduced toxicological properties, thereby converting a harmful substance into something safe or even potentially useful.
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 polypeptide effectively converts DON to 7-one-8-hydroxy-8-ene-DON, reducing its toxicity and providing a novel means for detoxification that is economically viable and applicable in food and feed systems without the need for microorganism cultivation.
Implementation Method 1
A polypeptide with a specific amino acid sequence (SEQ ID NO: 1) capable of degrading DON to 7-one-8-hydroxy-8-ene-DON, which is less toxic, is used to modify the C7-atom of DON, altering its toxicity and structure
Data Source
AI summary
The present invention relates to means and methods for degrading DON and/or DON derivative/s comprising a polypeptide comprising an amino acid sequence having at least 70% identity to the amino acid sequence set forth in SEQ ID NO: 1.