Albumin, which is the most important protein in human serum, plays an essential role in human therapy. It is widely involved in endogenous transport of hydrophobic therapeutic molecules in both vascular and extravascular compartments. This work was performed in order to verify the potential and the best physiological conditions for the strain Kluyveromyces lactis MW98.8C and HP108 harboring the vector pYG107 containing the hsa gene, in conduction extracellular synthesis of human serum albumin (HSA).  Although few transformants of the strains K.lactis MW98.8C and HP108 performing according to Griffithis et al., 1991 were obtained, they have exhibited good stability. Those transformants were culture in YNB glucose with geneticin and storaged at –80oC with 50% glycerol. The MW98.8C and HP108 transformants were cultured continuously in a chemostat in YPD media at two dilution rates.  Once they have reached the steady state, the cultures were transferred to YP media with lactose to induce the lac4 promoter and the synthesis of recombinant HSA. Samples were collected at time intervals and stored at –80oC to be analyzed in SDS-PAGE electrophoresis. These analyses have revealed a higher extracellular concentration of rHSA by HP108. In opposite to literature, it is possible to detect the protein band at 3 hours induction time and the plasmid remains stable up to 50 generation. A productivity of 300mgL-1 of rHSA has been obtained in batch after the biomass has been produced in chemostat at a dilution rate of 0,15h-1. Supported by: CNPq.