Heat stability and reactivation of mare milk lysozyme.

The research paper explores the stability and reactivation of lysozyme in mare’s milk under varying temperature and pH conditions, showing lysozyme activity as stable at acidic and neutral pH but unstable at alkaline pH, with evidence of a reactivation process occurring under certain conditions.

Textarea of the Research

The study focused on mare milk’s lysozyme, an enzyme known for its antibacterial properties. The researchers wanted to understand how changes in temperature and pH affect lysozyme’s stability and potential for reactivation.

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Findings of the Study

The study revealed insights related to the stability of lysozyme activity under different pH and temperature conditions and indicated a reactivation process.

• At acidic and neutral pH levels, lysozyme activity remains stable even when subjected to heat treatment. This indicates that lysozyme in mare’s milk maintains its antibacterial properties under these conditions, which is crucial for the milk’s health benefits.
• In contrast, lysozyme activity becomes unstable at alkaline pH levels (pH 9), showing a decrease in the enzyme’s antibacterial properties under this condition.
• Interestingly, in some instances, the research found evidence of a reactivation process. In these cases, even after being subjected to changes in temperature and pH, the lysozyme appeared to regain its antibacterial functionality. The reactivation of lysozyme was observed to reach between 30% to 40% post incubation of the water-based solution at 4 C for 20 days at a pH level of 3 or 6.

The findings indicate that understanding the conditions affecting the stability and reactivation of lysozyme can be instrumental in maximising the antibacterial properties of mare’s milk.