Sertraline is an important selective serotonin reuptake inhibitor (SSRI)-type of antidepressant that has strongly supported the effort against depression worldwide. (4S)-tetralone is the key intermediate in sertraline synthesis whose supply has been limited by the lack of available chiral resolution routes that are operationally simple and environmentally friendly. The Pseudovibrio-ω-Transaminase (P-ω-TA) is a pyridoxal-5’-phosphate (PLP)-dependent transaminase identified in marine sponge Pseudovibrio sp. WM33 that has shown good chiral resolution of (4S)-tetralone, which can convert (1S,4S) -demethylsertraline to (4S) -tetrahydronaphthalone, but direct application of this enzyme suffers from the high cost caused by the complicated preparation, single-use property and poor stability. In this study, we explored immobilization of P-ω-TA using bacteriophage T4 capsid as the carrier through self-assembly for recoverable biocatalysis. By fusing P-ω-TA to the non-essential small outer capsid protein (Soc) of T4, affinity immobilization of the enzyme on the T4 capsid has been achieved with a high copy number. The immobilized P-ω-TA retains the full activity and can be easily recovered by centrifugation for repeated use. In a five-round recover and reuse process, the average recovery of enzyme activity was >93% for each round. It has been demonstrated that immobilized P-ω-TA maintains the (S) -type selective resolution at the chiral center of the substrate and the catalytic ability for (1S,4S)-4-(3,4-dichlorophenyl)-1,2,3,4-tetrahydronaphthalen-1-amine; hydrochloride. Immobilization of P-ω-TA reduces the biocatalysis cost on chiral resolution of (4S)-tetralone, and helps establishing a greener synthetic route for sertraline.