Cholesterol Esterase Selectivity for Remnant Lipoprotein Detection
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Solution Overview
Problem
Existing methods for measuring cholesterol in remnant-like lipoprotein are not sufficiently selective, easy to use, or time-efficient, despite their use of enzymes like cholesterol esterase and cholesterol oxidase.
Innovation Solution
A method utilizing a cholesterol esterase with a higher lipoprotein lipase activity ratio compared to cholesterol esterase activity, combined with cholesterol oxidase or dehydrogenase, to selectively measure cholesterol in remnant-like lipoprotein from various lipoproteins, allowing for high selectivity and rapid measurement.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Measurement precision
If conventional cholesterol esterase is used for measuring cholesterol in remnant-like lipoprotein, then the measurement can be performed, but the selectivity to remnant-like lipoprotein is insufficient
Solution Approach 1:
The patent applies parameter changes by selecting a cholesterol esterase with specific activity ratio characteristics (lipoprotein lipase activity/cholesterol esterase activity within 12-7000). This parameter selection enables the enzyme to preferentially hydrolyze cholesterol esters in remnant-like lipoprotein over other lipoproteins, achieving high selectivity while maintaining measurement reliability through the standardized enzymatic reaction process
2Measurement precision
If antibody immobilization on gel is used to improve selectivity, then measurement selectivity increases, but the operation becomes more complex and time-consuming
Solution Approach 1:
The patent extracts the selectivity function from the complex antibody-immobilized gel system and transfers it to the cholesterol esterase enzyme itself. By selecting an enzyme with appropriate activity ratios, the selectivity is inherent to the enzymatic reaction, eliminating the need for antibody immobilization and gel-based separation systems, thus simplifying the device and operation while maintaining high measurement selectivity
Solution Approach 2:
The cholesterol esterase enzyme performs self-service by inherently discriminating between remnant-like lipoprotein and other lipoproteins based on its activity characteristics. The enzyme automatically achieves selectivity through its biochemical properties without requiring external separation systems or complex pretreatment steps, making the measurement process simpler and more direct
3Measurement precision
If conventional measurement methods are used, then cholesterol can be measured, but the measurement time period is extended
Solution Approach 1:
The patent changes the kinetic parameters of the measurement system by selecting a cholesterol esterase with optimal activity ratio that rapidly hydrolyzes cholesterol esters in remnant-like lipoprotein. This parameter optimization accelerates the enzymatic reaction rate, enabling quick achievement of measurement endpoint while maintaining accuracy through the specific enzyme characteristics and controlled reaction 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
Enables precise and sensitive measurement of cholesterol in remnant-like lipoprotein with improved selectivity and reduced measurement time, avoiding the need for antibody immobilization on gels and simplifying the procedure.
Implementation Method 1
a cholesterol esterase and a cholesterol oxidase or a cholesterol dehydrogenase are allowed to act so that cholesterol ester is converted into cholesterol
Implementation Method 2
measuring the produced hydrogen peroxide or reduced coenzyme
Data Source
AI summary
There are provided a method and reagent for measuring cholesterol in remnant-like lipoprotein in a sample with high sensitivity by more simple operation. The method for measuring cholesterol in remnant-like lipoprotein uses a cholesterol esterase, in which the activity ratio of a lipoprotein lipase to a cholesterol esterase (lipoprotein lipase activity/cholesterol esterase activity) is from 12 to 7000 in a method for measuring cholesterol in the lipoprotein by measuring hydrogen peroxide or a reduced coenzyme obtained by allowing the cholesterol esterase and a cholesterol oxidase or a cholesterol dehydrogenase to act on a test sample containing a lipoprotein.