Bacillus subtilis EG1 and Leuconostoc mesenteroides BW2 were isolated for use as protease- and lipaseproducing bacteria, respectively. Bacillus subtilis EG1 strain was confirmed to have strong proteolytic activity after 45 h of culturing on a skim milk plate. The culture medium inoculated with B. subtilis EG1 had relatively higher protein resolution and showed many more emulsion forms than that inoculated with L. mesenteroides BW2. The pH of the culture medium with B. subtilis EG1 gradually increased to 6.83, whereas that of the culture medium with L. mesenteroides BW2 decreased to 3.6 due to organic acid production. On the initial day, the soluble peptide contents of the culture media with B. subtilis EG1 and L. mesenteroides BW2 were 0.65 μmol/mL and 0.56 μmol/mL, respectively. However, just 3 d after culture, the soluble peptide content of the media with B. subtilis EG1 increased to 2.0 μmol/mL. The lipase activity of B. subtilis EG1 reached a maximum value of 24.6 units/mg protein on the first day of incubation in a mealworm medium. The proteases of P1, P2, and P9 isozymes of B. subtilis EG1 were the major active enzymes.