The emergence of antibiotic-resistant bacteria, such as methicillin-resistant Staphylococcus aureus, highlights the urgent need for alternative antimicrobial strategies like bacteriophages (phages). This study developed calcium crosslinked pectin films for bacterial enzyme-triggered phage release. A newly isolated lytic phage, SAC, rapidly inhibited S. aureus within 1 h at a multiplicity of infection of 1, with bactericidal activity lasting for up to 24 h. SAC remained stable across temperatures (−18 to 60 °C) and pH levels (5–10), and its genome lacked antibiotic resistance and virulence genes. SAC was incorporated into 1.5 % (w/v) pectin films crosslinked with 5 % (w/v) calcium chloride, which improved the film's moisture barrier properties by forming a dense polymer matrix and thereby enhanced the protection of phages against external humidity and desiccation. Pectinase exposure accelerated film degradation and phage release. In soy milk, the phage-loaded film reduced bacterial counts by 8.90-log CFU/mL without added pectinase, and by 10.47-log CFU/mL when pectinase was added, compared to those in control group. These results highlight the potential of SAC-loaded pectin films as a novel enzyme-responsive system for targeted antibacterial activity in food packaging applications.