The economic viability of cellulose biotransformation remains constrained by high enzyme costs, with processive endoglucanases emerging as promising candidates due to their dual-function hydrolysis mechanism. However, comprehensive kinetic and synergistic analyses of these enzymes are notably limited. This study investigates the kinetic properties of GH5 processive endoglucanase (M3-1) through various kinetic models. Inverse Michaelis-Menten analysis revealed M3-1's superior substrate recognition capacity, demonstrating 95.5 % productive binding site coverage compared to 48.8 % in non-processive endoglucanases. This enhanced efficiency is attributed to M3-1's distinctive structural features, particularly its open and deep cleft configuration. Pre-steady-state kinetics identified substrate association as the rate-limiting step, providing crucial direction for enzyme engineering efforts. Synergistic studies with cellobiohydrolase (CBH) demonstrated remarkable degradation synergy (DS value up to 8.2 on filter paper) and improved substrate resistance compared to traditional EG/CBH combinations. We propose a novel bidirectional degradation mechanism for the M3-1/CBH system, operating both inside-out and outside-in. The effectiveness of M3-1/CBH combination was further enhanced by up to 320 % through the addition of nonionic surfactants and expansin. These findings advance our understanding of processive endoglucanases and their potential applications in biomass conversion.