The objective of this study was to obtain the tryptic albuminase gene EsTRY from Antarctic krill (Euphausia superba) by screening and cloning, construct the recombinant expression vector EsTRY-pCold-SUMO, realize the high efficiency of heterologous expression in Escherichia coli, and reveal the degradation activity of this enzyme on phthalate esters (PAEs). The gene of trypsin EsTRY of Antarctic krill is 1350 bp in length, encoding 449 amino acids, with a theoretical molecular weight (MW) of 47040.35 Da and a theoretical isoelectric point (pI) of 4.90. Structural analysis revealed the presence of a catalytic triad (Asp/Glu-Ser-His) and a substratespecific binding site, classifying EsTRY as a member of the serine protease family. The esterase activity of EsTRY was determined to be 18973 U/mL, with a specific enzyme activity of 5802.15 U/mg. The optimal reaction temperature was found to be 25 ℃, and the optimal pH was determined to be 7.0. Enzyme-catalyzed degradation experiments demonstrated that EsTRYpossessed the capacity to degrade phthalic acid esters (PAEs), with 13.2%, 34.4%, and 63.5% of the 1 mmol/L of PAEs being degraded within 15 min, respectively. Furthermore, 48.9% of 1 mmol/L DMP, DEP, DPRP, and DBP were degraded within 15 min, and the degradation rates reached 39.4%, 62.7%, 86.8%, and 98.7% within 5 h, respectively. In this paper, we investigated the degradation activity of EsTRY on PAEs, which provides a new potential tool for the biological management of plasticizer pollution, as well as a scientific basis for the efficient utilization and high-value exploitation of Antarctic krill. Key words: Antarctic krill; trypsin; heterologous expression; degradation of plasticisers