This study investigated the effect of Boswellia papyrifera aqueous extract on human salivary peroxidase activity. Salivary peroxidase, a heme-containing enzyme secreted by acinar cells, plays a crucial role in maintaining oral health by generating antimicrobial hypothiocyanite ions (OSCN⁻). Various concentrations of Boswellia papyrifera extract (2–15 g/100 mL) were tested to determine their influence on enzyme activity under different pH and temperature conditions. Results showed that enzyme activity increased significantly in a concentration-dependent manner, with maximal activation observed at 15 g/100 mL. The optimal enzymatic activity was recorded at 37° C and pH 6.5 under control conditions, while the presence of the extract enhanced activity across a broader temperature and pH range. Kinetic analysis revealed a marked increase in catalytic efficiency, as indicated by a higher Vmax (260 U) and a lower Km (0.02 mM) compared to control (Vmax = 204 U; Km = 0.57 mM). These findings suggest that bioactive components of B. papyrifera, such as boswellic acids and terpenoids, may stabilize or activate the enzyme’s catalytic conformation, enhancing substrate affinity and turnover. Overall, the study highlights the potential of B. papyrifera as a natural modulator of salivary peroxidase.
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