Structural and Functional Stability of Natural Actomyosin From Freshwater Snail ( Bellamya bengalensis ): Unraveling Thermal and pH Effects

The structural and functional stability of natural actomyosin (NAM) extracted from freshwater snail ( Bellamya bengalensis ) was systematically evaluated across a wide pH (2–12) and temperature (20°C–90°C) range. NAM exhibited remarkable thermal stability up to 40°C at pH 6, beyond which a sharp increase in turbidity indicated protein aggregation. The highest solubility (69.90%) was observed at 40°C around pH 6, whereas the lowest solubility (9.41%) occurred at pH 4, corresponding to its isoelectric point. Surface hydrophobicity increased progressively with temperature up to 50°C and at pH 6, followed by a gradual decline, whereas sulfhydryl content decreased with rising temperature but increased with pH, reflecting protein conformational changes associated with unfolding and rearrangement of native structures. These observations were corroborated by differential scanning calorimetry and SDS–PAGE, which revealed distinct protein conformational changes. Enzymatic functionality, assessed by Ca 2+ ‐ATPase activity, was maximal at 40°C and pH 6, whereas foaming and emulsifying capacities were also significantly enhanced at approximately 40°C and under slightly alkaline pH conditions. Collectively, these findings highlight that NAM from B. bengalensis maintains structural integrity and desirable functional attributes up to 40°C and near‐neutral pH, providing a scientific foundation for its future exploration in food‐related systems.