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Related Experiment Video

Updated: Feb 6, 2026

Measuring Lactase Enzymatic Activity in the Teaching Lab

Measuring Lactase Enzymatic Activity in the Teaching Lab

Published on: August 6, 2018

Measuring Lactase Enzymatic Activity in the Teaching Lab.

Cattleya S Leksmono¹, Claudia Manzoni², James E Tomkins¹

¹School of Pharmacy, University of Reading.

Journal of Visualized Experiments : Jove

|August 21, 2018

Summary

This study introduces a simple enzyme assay for first-year pharmacy students using lactase (an enzyme found in dietary supplements). The protocol measures lactase activity by monitoring the hydrolysis of ortho-nitrophenol-beta-D-galactopyranoside (ONPG) at different temperatures.

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Measuring Lactase Enzymatic Activity in the Teaching Lab

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Published on: August 23, 2016

Area of Science:

Biochemistry
Enzymology
Biomedical Sciences

Background:

Enzyme function is crucial for biological and biomedical sciences.
Undergraduate education requires accessible enzyme analysis protocols.
Lactase, relevant to human health, serves as a practical enzyme model.

Purpose of the Study:

To provide an entry-level protocol for enzyme reactions and analysis.
To introduce first-year pharmacy students to enzyme kinetics.
To demonstrate enzyme activity using a commercially available enzyme.

Main Methods:

Lactase extraction from dietary supplement tablets.
Colorimetric assay using ortho-nitrophenol-beta-D-galactopyranoside (ONPG) as a substrate.
Measurement of enzyme activity at varying temperatures (ice, room temperature, 37 °C) via absorbance at 420 nm.

Main Results:

The protocol successfully quantifies lactase activity.
Temperature significantly affects the rate of enzymatic hydrolysis of ONPG.
The assay provides a foundation for more advanced enzyme activity studies.

Conclusions:

This protocol offers a practical and accessible method for undergraduate enzyme analysis.
The study highlights the importance of temperature in enzyme kinetics.
The assay is adaptable for exploring various enzyme activities and conditions.