Lactoperoxidase (LPO) is a natural antimicrobial enzyme found in goat milk that helps inhibit bacterial growth and prolong freshness through its role in the milk’s innate defense system.
Beyond its biological function, goat milk LPO has gained attention in food science for its use in milk authentication, quality assessment, and detection of heat treatment or adulteration.
Lactoperoxidase (LPO) is a naturally occurring enzyme found in the milk of many mammals, including goats. It plays an important role in the milk's defense system by helping prevent the growth of harmful bacteria.
This enzyme is also becoming increasingly valuable in food science for detecting milk adulteration and assessing dairy quality.
Lactoperoxidase is part of the milk's innate antimicrobial system.
It catalyzes a specific biochemical reaction: it uses hydrogen peroxide (H₂O₂) to oxidize thiocyanate ions (SCN⁻), producing a compound called hypothiocyanite (OSCN⁻). This product has antimicrobial effects, meaning it can slow or stop the growth of certain bacteria in raw milk.
This reaction is one of the reasons fresh milk can resist spoilage for a limited time under proper conditions. It’s a built-in preservation mechanism, especially important in species like goats, where milk may be used in raw or minimally processed forms.
While lactoperoxidase is found in many types of milk—including cow, goat, and human—the enzyme's structure and activity levels vary by species.
Goat milk LPO has distinct biochemical properties that make it useful in identifying goat milk specifically. These differences allow scientists to use goat milk LPO as a marker for food authentication.
This testing is primarily performed in food science laboratories. It may be considered in the following scenarios:
One of the most important applications of LPO testing is verifying goat milk products' authenticity. Because goat milk can be more expensive and is often preferred by individuals with cow milk sensitivity, there is potential for economic fraud.
Testing for goat-specific lactoperoxidase can help detect whether cow’s milk has been mixed into a product labeled as 100% goat milk.
LPO testing is often used alongside other protein markers such as kappa-casein to strengthen the accuracy of milk identification.
Lactoperoxidase testing is also used in quality control to evaluate the freshness and microbial resistance of goat milk.
LPO is heat-sensitive. Common processing methods like pasteurization inactivate this enzyme.
Therefore, the presence of active LPO may suggest that milk is raw or minimally processed.
Loss of LPO activity after heating can be used to confirm proper pasteurization or thermal treatment.
Detecting LPO in a dairy sample can confirm that goat milk is present. Because this enzyme has species-specific features, it can help distinguish goat milk from cow or other milks.
The presence of LPO may signify that the sample is authentic goat milk (especially if combined with other markers).
The level of LPO activity suggests a possible estimate of quantity or processing status.
A lack of detectable goat milk LPO can mean a few things:
It’s essential to interpret these results in the context of how the milk was handled or processed. Even genuine goat milk may show low LPO activity if it has been heat-treated.
Buys, E. M., & Seifu, E. (2021). Enzymes Indigenous to Milk: Lactoperoxidase. Elsevier EBooks, 670–676. https://doi.org/10.1016/b978-0-12-818766-1.00252-x
Zapico, P., Gaya, P., De Paz, M., Nuñez, M., & Medina, M. (2010). Influence of Breed, Animal, and Days of Lactation on Lactoperoxidase System Components in Goat Milk. Journal of Dairy Science, 74(3), 783–787. https://doi.org/10.3168/jds.S0022-0302(91)78225-8
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