GH30 Xylanase with Calcium Carbonate for Corn Feed
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Solution Overview
Problem
Commercially available xylanases are ineffective in degrading the highly branched xylan backbone found in corn and sorghum, limiting the release of trapped nutrients in animal feed.
Innovation Solution
A composition comprising a GH30 xylanase enzyme combined with a calcium source, such as calcium chloride, and/or a carbonate source, such as sodium bicarbonate, which enhances the enzyme's activity across various pH levels, improving the release of xylan oligomers from maize and other feeds.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If traditional xylanases (GH5, GH8, GH10, GH11, GH30, GH98) are used to degrade xylan backbone, then nutrient release is improved in wheat-based feeds, but they are ineffective on highly substituted xylans in corn and sorghum due to side chain steric hindrance
Solution Approach 1:
The patent applies parameter changes by modifying the enzyme's operational conditions - specifically pH and temperature parameters - to optimize the activity of GH30 xylanase on highly substituted xylans. The enzyme demonstrates optimal activity at pH 4.5-6.5 and temperatures of 40-60°C, which allows it to effectively degrade corn and sorghum xylans that resist traditional xylanases.
Solution Approach 2:
The patent applies local quality by selecting a specific enzyme family (GH30) with particular catalytic properties suited for highly substituted xylans. The GH30 xylanase has a specific active site configuration and catalytic mechanism that can accommodate the steric hindrance caused by L- and D-galactose and D-xylose side chains, ferulic acid esterification, and acetylation groups present in corn and sorghum xylans.
2Productivity
If GH30 xylanase is used to degrade highly substituted xylans in corn and sorghum, then nutrient release is enhanced, but enzyme activity is limited at certain pH levels without calcium/carbonate additives
Solution Approach 1:
The patent applies the intermediary principle by introducing calcium ions (Ca2+) and carbonate ions (CO3 2-) as mediators that enhance GH30 xylanase activity. These ions act as cofactors that stabilize the enzyme's active conformation and improve its catalytic efficiency. The calcium carbonate combination specifically addresses pH limitations by buffering the reaction environment and maintaining optimal pH conditions for enzyme activity across a broader range.
Solution Approach 2:
The patent applies parameter changes by modifying the chemical environment through calcium and carbonate additives. These additives change the ionic strength, pH buffering capacity, and chemical composition of the reaction medium, thereby enhancing enzyme stability and activity. The calcium carbonate system specifically addresses pH instability by creating a buffered environment that maintains optimal conditions for GH30 xylanase activity.
3Stability of the object's composition
If xylan side chains with L- and D-galactose and D-xylose sugars are present, then xylan structure complexity increases, but degradation by traditional xylanases becomes resistant
Solution Approach 1:
The patent applies local quality by selecting GH30 xylanase with specific local catalytic properties that can handle complex side chain structures. The enzyme's active site has a specific spatial configuration and chemical environment that can accommodate and process L- and D-galactose and D-xylose sugars, ferulic acid esterification, and acetylation groups without being hindered by their presence.
Solution Approach 2:
The patent applies parameter changes by optimizing pH and temperature conditions to enhance the flexibility and catalytic efficiency of GH30 xylanase. At optimal pH (4.5-6.5) and temperature (40-60°C), the enzyme maintains appropriate conformational flexibility to access and degrade highly substituted xylan structures that resist traditional xylanases under suboptimal conditions.
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 use of GH30 xylanase with calcium and/or carbonate sources significantly increases the solubilization of xylan oligomers, overcoming the limitations of traditional xylanases and enhancing nutrient release in animal feed.
Implementation Method 1
The known enzymes responsible for the hydrolysis of the xylan backbone are classified into enzyme families based on sequence similarity
Implementation Method 2
Commercially available GH10 and GH11 xylanases are often used to break down the xylose backbone of arabinoxylan
Implementation Method 3
The inventors have found that the use of at least one of these additives increases the activity of GH30 enzymes at various pH levels
Data Source
AI summary
The presence of either a calcium source or a carbonate source with GH30 xylanses significantly improves the release of xylan oligomers from maize and other feeds compared to the same xylanases without the calcium or carbonate source. Animal feed and animal feed additives comprising a combination of one or more polypeptides having xylanase activity; and one or more sources of calcium; and/or one or more sources of carbonate, wherein the polypeptide is a GH30 xylanase provide for improved xylan release from feedstuff.