This work reports the use of size exclusion chromatography (SEC) applied to recovery, purification and characterization of hyaluronic acid (HA) obtained from Streptococcus zooepidemicus by submerged and solid state fermentation. The presence of proteic contaminants was identified by electrophoresis in polyacrylamide gel under denaturant conditions (SDS-PAGE) and quantified by the Bradford method. The recovery and pre-purification of HA from the proteic contaminants were performed by subsequent operations of precipitation with ethanol and dissolution with saline solution (performed up to four times). After four purification steps, for both submerged and solid state fermentation, the total protein concentration was reduced about 90 % and the HA concentration decreased about 16%. The characterization of molar mass distribution of the HA samples was performed by size exclusion chromatography (SEC) in analytical scale using Shodex OHPak SB806M HQ column, refractive index detector, 0.1 M sodium nitrate solution as mobile phase, flow rate of 0.8 mL.min-1. Experiments were also performed in semi-preparative scale for protein separation and molar mass fractionation using Superose 6 column, refractive index and UV/Vis (in wavelength of 280 nm) detector, 0.1 M sodium nitrate solution as mobile phase and flow rate of 0.8 mL.min-1. The injection volumes were 20 µL in analytical scale and 400 µL in semi-preparative scale. All runs were performed at room temperature for both scales. Molar mass (MM) distribution of HA samples was assessed by SEC using pullulan markers (polymer of similar hydrodynamic volume as compared to HA) as molar mass standards over the range of 5.8 x 103 Da to 8.53 x 105 Da. The MM of samples of HA obtained from submerged fermentation were found to be in the range of 103 to 107 Da, after being submitted to four pre-purification steps. The purification steps not only decreased proteic contamination but also increased the average molar mass of the samples. For solid state fermentation, the MM distribution was found to be in the range of 103 to 105 Da. In the runs with the semi-preparative Superose 6 column, it was possible to separate HA fractions, free of proteic contaminants, with molar mass above 105 Da.