Leptospirosis is a spirochetal zoonotic disease that cause 350,000–500,000 severe human infections annually with an incidence of 10 cases per 100,000 in humid, subtropical regions of the world and a mortality rate of 10%. Subunit recombinant vaccines consist of purified antigens and represent a possible intervention against leptospirosis. Leptospiral immunoglobulin-like (Lig) proteins are of great interest as mediators of pathogenetic mechanisms, serodiagnostic antigens, and as effective recombinant vaccinogens. The non-identical carboxy-terminus portion of LigA protein (LigANI) is a vaccine candidate whose immu¬noprotective potential has been demonstrated in several studies. The aim of this work was to establish the downstream process for recombinant LigANI protein and the methodologies for process control. The wet cell pellet was lysed by homogeneizer and centrifuged to obtain the soluble fraction. Protein purification proceeded in three main steps: Immobilized Metal Affinity Chromatography (IMAC), gel filtration (GF) and Ion Exchange chromatography (IEX). LigANI was obtained with high purity (~99%) in a final yield of 20% (~95mg/g of wet cell paste) and demonstrated immunogenicity (recognition by leptospirosis patient sera) and antigenicity (recognition by hiperimmune sera produced in rabbit). The DNA and LPS residual in the final sample were beyond the limit permitted for vaccines.