The fermentation kinetics of protease inhibitor production by streptomyces fradiae

Streptomyces fradiae에서 분리한 단백질 분해효소 저해물질 생성의 동력학적 특성

The objectives of the current studies were to establish the optimal conditions for the production of extracellular protease inhibitor in a strain of Streptomyces fradiae. As results, it was found that cell specific growth rate was very critical for the production of protease inhibitor and the optimum specific growth rate was found to be 0.05 h$^{-1}$ . Dissolved oxygen tension and pH were also important to regulate the inhibitor production. The inhibitory mode of the purified inhibitor to .alpha.-chymotrypsin was found to be competitive (K$_{i}$=5.5*10$^{-7}$ M). One mole of inhibitor could bind two moles of .alpha.-chymotrypsin and the complex has very low dissociation constant.t.