Nisin’s stability
Interaction with Food Matrix Nisin’s stability is significantly influenced by food components: Proteins and Fats: In high-protein or high-fat foods (e.g., meat, dairy products), Nisin tends to bind to proteins (e.g., casein) or fat globules through hydrophobic interactions and electrostatic forces, reducing its free concentration and apparent activity. For example, in full-fat milk, the effective free Nisin concentration is 30–40% lower than in skim milk. To mitigate this, higher addition levels (10–20% increase) or compounding with surfactants (e.g., lecithin) are recommended to improve dispersion. Ions and Preservatives: Divalent cations (Ca²⁺, Mg²⁺) can stabilize Nisin’s structure by forming complexes with its carboxyl groups, enhancing heat resistance. Conversely, metal ions such as Fe³⁺ and Cu²⁺ may catalyze oxidative degradation. Compounding with EDTA (a chelating agent) can reduce such adverse effects. Additionally, Nisin exhibits synergistic stability with organic acids (e.g., lactic acid) and plant extracts (e.g., tea polyphenols), while avoiding combination with strong oxidants (e.g., hydrogen peroxide) that may oxidize its amino acid side chains.
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