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Updated: Jun 29, 2026
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Measuring Lactase Enzymatic Activity in the Teaching Lab
Published on: August 6, 2018
[A new oxidase method for analyzing L-lactate]
H M Pavlishko1, M M Maĭdan, A A Sybirnyĭ
1Institute of Cell Biology, NAS of Ukraine, Lviv.
Ukrains'Kyi Biokhimichnyi Zhurnal (1999 )
|August 3, 2002
Summary
A novel colorimetric method accurately measures L-lactate in biological samples without peroxidase. This sensitive technique is applicable to analyzing L-lactic acid in dairy products like kefir and yogurt.
Area of Science:
- Biochemistry
- Analytical Chemistry
Context:
- L-lactate analysis is crucial in biological and food science.
- Existing methods often rely on peroxidase, which can interfere with certain assays.
- A need exists for a sensitive, reliable, and peroxidase-free L-lactate detection method.
Purpose:
- To develop and validate a new oxidase-coupled colorimetric method for L-lactate quantification.
- To establish the sensitivity and linearity range of the developed assay.
- To adapt the method for analyzing L-lactic acid in fermented dairy products.
Summary:
- A peroxidase-free, oxidase-coupled colorimetric assay was developed for L-lactate.
- The method utilizes lactate oxidase to convert lactate to pyruvate, followed by a dye-producing reaction with 3-methyl-2-benzothiazolinone hydrazone (MBTH) and ferric ions.
- The assay demonstrates high sensitivity (0.1 micromole) and linearity (0.1-1.0 micromole), with excellent correlation (r = 0.99943).
Impact:
- Provides a sensitive and accurate alternative for L-lactate determination in biological fluids.
- Enables reliable quantification of L-lactic acid in food products like kefir and yogurt.
- Reduces potential interference by eliminating the need for peroxidase.
