Albumin Purification via Exhaustive Diafiltration
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Solution Overview
Problem
Current albumin purification methods using stabilizers like N-acetyltryptophan and sodium caprylate reduce the binding capacity of albumin, making it less effective in detoxification therapies and cell cultures, as these stabilizers compete with toxins for binding sites and hinder the transport function of albumin.
Innovation Solution
A process that involves pasteurization with sodium chloride and N-acetyltryptophan without fatty acids, followed by exhaustive diafiltration to eliminate stabilizers and reduce compounds that reduce albumin's binding capacity, resulting in an albumin solution with a high capacity to bind and transport molecules.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If stabilizers like N-acetyltryptophan and sodium caprylate are added to albumin solution, then the stability and safety of the albumin product is improved, but the binding capacity of albumin for toxins and molecules is reduced
Solution Approach 1:
The invention extracts and removes stabilizers (N-acetyltryptophan and sodium caprylate) from the albumin solution through diafiltration processes. This extraction eliminates the harmful effect of stabilizers on binding capacity while maintaining the stability benefits through alternative stabilization methods
Solution Approach 2:
The invention changes the chemical composition parameters of the albumin solution by eliminating stabilizers and adjusting to a stabilizer-free or minimal stabilizer formulation. This parameter change restores the binding capacity while maintaining product stability through controlled purification processes
2Quantity of substance
If exhaustive diafiltration is used to eliminate stabilizers, then the binding capacity of albumin is improved, but the process complexity and time are increased
Solution Approach 1:
The invention performs preliminary removal of excess stabilizers during the purification process before final formulation. By removing stabilizers early through diafiltration steps, the subsequent processing is simplified and the binding capacity is restored without requiring overly complex final purification steps
3Ease of manufacture
If fatty acids are added during albumin purification, then the purification process is simplified, but the binding capacity of albumin is reduced due to competition for binding sites
Solution Approach 1:
The invention extracts and removes fatty acids from the albumin solution through purification steps. This removal eliminates the competition for binding sites between fatty acids and toxin molecules, thereby restoring the full binding capacity of albumin while maintaining purification effectiveness
Solution Approach 2:
The invention changes the composition parameters by eliminating fatty acids from the final albumin formulation. This parameter change ensures that binding sites remain available for toxin molecules rather than being occupied by fatty acids, thereby maximizing binding capacity
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 process achieves a higher binding capacity for albumin, maintaining safety against pathogen transmission and enhancing detoxification therapy efficiency by reducing the interference of stabilizers, allowing for effective toxin capture and transport in both therapeutic and cultural applications.
Implementation Method 1
the stabilisation of the product of step (a) with NaCl and N-acetyltryptophan without the addition of fatty acids
Implementation Method 2
the pasteurisation of the product of step (b)
Implementation Method 3
a second diafiltration of the product of step (c) until N-acetyltryptophan is extensively eliminated
Data Source
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AI summary
Process for obtaining human albumin of high efficiency for use in detoxification therapy. The process comprises a) a first dialysis (diafiltration); b) the stabilisation of the solution with NaCl and at least one amino acid; c) heating the solution; d) a second dialysis (diafiltration).