Our study focuses on a partial purification, characterization and immobilization of enzyme for phenol removal by polyphenol oxidase (PPO) enzyme from carambola leaves. A PPO partially purified about 4.20-fold with a recovery of 2.93 % yield. The PPO enzyme is a monomeric protein with a molecular weight of ̴ 61 kDa. The Km values for free and immobilized PPO were 20 and 32 mM, respectively. The entrapment of PPO by the SA–PVA–silver nanoparticles (AgNPs) showed the best result for phenol removal. The optimal pH of free and immobilized PPO enzyme activities was 7.5 pH. The optimal temperature of free and immobilized PPO was 40 ℃ and free enzyme activity lost at 60 ℃; The AgNPs immobilized PPO removed 95 % of the phenol on the fifth cycle. The immobilized carambola leaf PPO enzyme could be efficiently used for the removal of phenol from industrial effluents.