Artificial Beta-Glucan-Binding Protein Stability
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Solution Overview
Problem
Existing β-glucan-binding proteins face challenges in stability, particularly pH and heat stability, which limits their practicality for various applications, including early diagnosis of deep mycosis and detection in functional foodstuffs.
Innovation Solution
A novel artificial β-glucan-binding protein with a specific amino acid sequence (SEQ ID NO: 1) is developed, which exhibits enhanced binding stability and is expressed in E. coli for higher yield, forming the basis of a β-glucan detection kit and bacterium transformation.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If native β-glucan-binding proteins derived from insects are used, then β-glucan binding activity is achieved, but binding stability decreases under varying pH and NaCl conditions
Solution Approach 1:
The patent applies parameter changes by modifying the amino acid sequence of native β-glucan-binding proteins to create artificial variants with optimized properties. Specifically, the invention changes pH and ionic strength parameters of the protein structure through amino acid substitutions, deletions, or additions, resulting in proteins that maintain stable binding activity across a broader range of pH conditions (pH 4-10) and salt concentrations, thereby resolving the contradiction between binding stability and adaptability
2Reliability
If artificial β-glucan-binding proteins are developed, then binding stability is improved, but amino acid sequence and production characteristics remain unclear
Solution Approach 1:
The patent applies copying by creating artificial β-glucan-binding proteins based on copied and modified amino acid sequences from native proteins. The invention uses sequences similar to those found in nature (such as those from silkworm or other insect proteins) as templates, then introduces specific mutations to improve stability while maintaining the core binding function. This approach allows systematic optimization of the amino acid sequence to achieve both high binding stability and clear production characteristics
3Measurement precision
If native β-glucan-binding proteins are used for detection, then β-glucan detection is possible, but detection stability under varying temperature and pH conditions is insufficient
Solution Approach 1:
The patent applies parameter changes by engineering artificial β-glucan-binding proteins with modified amino acid sequences that exhibit enhanced stability across varying temperature and pH conditions. The invention specifically optimizes the protein's isoelectric point and thermal stability parameters, allowing the detection system to maintain measurement precision under diverse environmental conditions, thereby resolving the contradiction between detection accuracy and detection stability
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 artificial β-glucan-binding protein demonstrates superior β-glucan binding activity and stability across varying pH and temperature conditions, enabling stable and quantitative detection of β-glucan, outperforming natural forms in yield and stability.
Implementation Method 1
a β-glucan-binding protein according to the present invention contains an amino acid sequence represented by SEQ ID NO: 1
Data Source
AI summary
The β-glucan-binding protein contains an amino acid sequence represented by SEQ ID NO: 1.