The use of antimicrobial peptides (AMPs) synthesized by bacteria (bacteriocins) is an alternative for combating multidrug resistant bacterial strains and their production by recombinant route is a viable option for their mass production. The bacteriocin E-760 isolated from the genus?Enterococcus?sp. has been shown to possess inhibitory activity against Gram-negative and Gram-positive bacteria. In this study, the expression of a chimeric protein coding for E-760 in the nucleus of?C. reinhardtii?was evaluated, as well as, its antibacterial activity. The synthetic gene E-760S was inserted into the genome of?C. reinhardtii?using?Agrobacterium tumefaciens. A transgenic line was identified in TAP medium with hygromycin and also by PCR. The increment in the culture medium temperature of the transgenic strain at 35 °C for 10 min, increased the production level of the recombinant protein from 0.14 (Non-induced culture, NIC) to 0.36% (Induced culture, IC) of total soluble proteins (TSP); this was quantified by an ELISA assay. Recombinant E-760 possesses activity against?Staphylococcus aureus?in 0.34 U log,?Staphylococcus agalactiae?in 0.48 U log,?Enterococcus faecium?in 0.36 U log,?Pseudomonas aeruginosa?in 2 U log and for?Klebsiella pneumoniae, the activity was 0.07 U log. These results demonstrate that the nucleus transformation of?C. reinhardtii?can function as a stable expression platform for the production of the synthetic gene E-760 and it can potentially be used as an antibacterial agent.