A new Bacillus licheniformis mutant strain producing serine protease efficient for hydrolysis of soy meal proteins

Resumo

Induced mutagenesis with γ-irradiation of the industrial strain Bacillus licheniformis-60 VKM B-2366 D was used to obtain a new highly active producer of an extracellular serine protease, Bacillus licheniformis-145. Samples of dry concentrated preparations of serine protease produced by the original and mutant strains were obtained, and identity of their protein composition was established. Alkaline serine protease subtilisin DY was the main component of the preparations. The biochemical and physicochemical properties of the Protolicheterm-145 enzyme preparation obtained from the mutant strain were studied. It exhibited proteolytic activity (1.5 times higher than the preparation from the initial strain) within broad ranges of pH (5–11) and temperature (30–70°C). Efficient hydrolysis of extruded soybean meal protein at high concentrations (20 to 50%) in the reaction mixture was the main advantage of the Protolicheterm-145 preparation. Compared to the preparation obtained using the initial strain, the new preparation with increased proteolytic activity provided for more complete hydrolysis of the main non-nutritious anti-nutritional soy proteins (glycinin and β-conglycinin) with the yield of soluble protein increased by 19–28%, which decreased the cost of bioconversion of the proteinaceous material and indicated promise of the new preparation in resource-saving technologies for processing soybean meals and cakes.