01 / The question
How do you turn a colour change into an enzyme model?
The horseradish peroxidase project used optical measurements to characterise enzyme activity. The challenge was to move from an instrument signal to an interpretable rate model.
02 / The intuition
A mechanism worth testing.
Calibration and controls connect absorbance to chemistry. The time evolution matters before any kinetic parameters are fitted.
03 / The work
Inside the method.
Explore each part of the approach.
01Acquire kinetic traces
Multi-wavelength spectrophotometry and a microplate reader tracked the assay over time.
02Estimate rates
Dilution series, blanks and replicates supported rate estimation and calibration.
03Fit and question the model
The analysis considered Michaelis–Menten parameters, assay sensitivity and comparison with literature values.
04 / The observations
What emerged.
The notes document kinetic fitting and analytical-limit calculations. Original curves and fit uncertainties are not yet included.
This account is based on recorded project notes. Original reports, figures and datasets are not embedded here.
05 / The limits
Where the evidence stops.
Parameters depend on the assay conditions and fitting assumptions. Neither precision nor a detection limit is asserted without the corresponding measurements.
The academic foundations