This study investigates the effects of Premna microphylla Turcz. pectin (PMP) on chicken myofibrillar protein (CMP) gels. PMP was extracted from the leaves of Premna microphylla using the ammonium oxalate method. Four concentrations of PMP (0, 0.5, 1.0, and 1.5%) were incorporated into CMP. Several analytical techniques were employed, including rheological analysis, intermolecular force measurements, Fourier transform infrared spectroscopy (FTIR), SDS-PAGE, scanning electron microscopy (SEM), and Differential scanning calorimetry (DSC). The results showed that PMP incorporation significantly reduced cooking loss and enhanced the water-holding capacity of CMP gels. Solubility, turbidity, zeta potential, and surface hydrophobicity exhibited concentration-dependent behavior. These properties initially increased from 0% to 1.0% PMP but decreased to 1.5% PMP. Rheological analysis revealed that PMP increased gel viscosity, structural stability, and water retention, particularly at 1.0% addition. DSC analysis indicated that PMP exerted a concentration-dependent dual effect on the thermal stability of CMP gels: the thermal denaturation temperature (Tm) decreased at low PMP concentrations but increased at higher concentrations. FTIR results revealed that PMP promoted a conformational transition of CMP from α-helix to β-sheet structures. SEM observations confirmed that PMP enhanced the gel network, producing a denser and more stable microstructure. These findings suggest that PMP is a promising natural agent for improving the gelation properties and structural integrity of protein-based gels. In addition, PMP showed potential applications in enhancing the texture and functionality of meat-based products.