Updated project metadata. Trypanosoma evansi is a parasite of African origin that has evolutionary proximity to Trypanosoma brucei. This parasite, which causes the surra, has the broadest range of hosts, including wild and domestic mammals, and its geographic distribution is the widest among all trypanosomes. This disease causes numerous economic losses in livestock in countries in the Americas, Africa, and Asia. This work aims to obtain in vitro secreted proteins from T. evansi and identify potential treatment and diagnostic biomarkers of surra. For this, in an experimental group, the parasite was purified in an ion-exchange column (DEAE-Cellulose) and maintained in a secretion medium. In a second group, there was no purification of the parasites. Also, each group was maintained at 37 ºC and 27 ºC. Finally, we identified the proteins through mass spectrometry. We found a total of 246 proteins and noticed that the temperature appears to modulate protein secretion. We observed negligible differences in proteins from purified and non-purified sets. We observed that most secreted proteins are related to molecular function (F) of binding, catalytic activity, structural molecule activity, and biological process (P) of metabolic process, cellular process, localization, and biological regulation. We also verified that most secretome proteins have homologous proteins with trypanosomatids T. brucei, T. b. gambiense, T. vivax, and T. equiperdum. However, despite this, it was possible to identify the presence of exclusive T. evansi epitopes with potential biomarkers for differential surra diagnosis. We identified epitopes of proteins that are part of the glycolytic process of the parasite, which can be used in immunotherapy by the production of anti-proteins from the glycolytic process. Finally, this is the first work that provide a big picture of the T. evansi secretome and could be the starting point to elucidate biological issues related to surra.