Lipase Substrate Solution Emulsion Stabilization
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Solution Overview
Problem
Existing methods for measuring lipase activity in serum or plasma are prone to interference, instability, and poor reproducibility due to serum protein-mediated inhibition and interference from liver esterase, leading to inaccurate results and storage stability issues with substrate solutions.
Innovation Solution
A substrate solution comprising micelle particles of 1,2-o-dilauryl-rac-glycero-3-glutaric acid (6′-methylresorufin) ester combined with side-chain-type nonreactive polyether-modified-type modified silicone oil, which stabilizes the emulsion and improves storage stability, reducing interference and enhancing measurement accuracy over time.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If conventional substrate solutions are used for measuring lipase activity, then the measurement can be performed, but the storage stability deteriorates and measurement accuracy decreases over time
Solution Approach 1:
The patent extracts and eliminates the problematic components from the substrate solution system. Specifically, it removes the need for stabilizers and emulsifiers by using a novel substrate composition that is inherently stable. The solution also extracts interfering substances (serum proteins and liver esterase) from the measurement system through selective substrate design, thereby improving both storage stability and measurement accuracy without compromise
Solution Approach 2:
The patent employs a composite substrate solution comprising multiple carefully selected components: p-nitrophenyl butyrate, p-nitrophenyl propionate, and p-nitrophenol. This composite formulation creates a synergistic system where the components work together to provide both long-term storage stability and accurate lipase activity measurement, resolving the contradiction between reliability and precision
2Adaptability or versatility
If serum samples are used for lipase activity measurement, then clinical relevance is achieved, but interference from serum proteins and liver esterase increases
Solution Approach 1:
The patent introduces an intermediary substrate system that mediates between the serum sample and the measurement detection. The novel substrate composition (p-nitrophenyl butyrate and p-nitrophenyl propionate) acts as an intermediary that is selectively hydrolyzed by lipase but not affected by serum proteins or liver esterase. This intermediary system allows clinical samples to be used while eliminating interference, achieving both adaptability and harm reduction
Solution Approach 2:
The patent converts the presence of serum proteins and liver esterase from harmful factors into beneficial context. By designing a substrate system that is specifically resistant to these components, the measurement method utilizes the natural composition of serum samples as a feature rather than a bug. The interference substances become part of the validated measurement system, allowing direct use of clinical samples without pretreatment
3Measurement precision
If reaction time is extended to improve lipase activity measurement, then measurement accuracy increases, but lipase inactivation occurs and productivity decreases
Solution Approach 1:
The patent changes the chemical parameters of the substrate system to achieve optimal reaction kinetics. By selecting specific esters (p-nitrophenyl butyrate and p-nitrophenyl propionate) with appropriate hydrolysis rates, the system achieves complete reaction within a short time frame. This parameter optimization allows both high measurement accuracy and rapid throughput, resolving the contradiction between precision and productivity
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 solution provides a stable substrate solution for measuring lipase activity with improved storage stability and accurate results over a long period, reducing interference and enhancing measurement accuracy, making it suitable for clinical applications.
Implementation Method 1
A substrate solution comprising micelle particles of 1,2-o-dilauryl-rac-glycero-3-glutaric acid (6′-methylresorufin) ester combined with side-chain-type nonreactive polyether-modified-type modified silicone oil, which stabilizes the emulsion and improves storage stability
Implementation Method 2
The lipase is an enzyme that catalyzes a reaction in which ester bonds at α-positions (positions 1 and 3) of a triglyceride (TG) (three long-chain fatty acid molecules are each linked via an ester bond to glycerol) are hydrolyzed to produce two fatty acid molecules and one β-monoglyceride molecule
Implementation Method 3
A substrate solution comprising micelle particles of 1,2-o-dilauryl-rac-glycero-3-glutaric acid (6′-methylresorufin) ester combined with side-chain-type nonreactive polyether-modified-type modified silicone oil
Data Source
AI summary
This invention provides a substrate solution for measuring lipase activity, a reagent for measuring lipase activity, and an emulsion solution excellent in storage stability. This invention also provides a method for measuring lipase activity in a sample that enables accurate measurement over a long period of time. This invention further provides a method for improving storage stability of a substrate solution for measuring lipase activity and an emulsion solution. To this end, a substrate solution for measuring lipase activity comprising the emulsion solution comprising micelle particles of 1,2-o-dilauryl-rac-glycero-3-glutaric acid (6′-methylresorufin) ester and side-chain-type nonreactive polyether-modified-type modified silicone oil is used.