Characterization of production of an extracellular proteinase inhibitor from streptomyces chromofuscus 34–1 with alkaline phosphatase activity and antiviral effect

Abstract

An extracellular proteinase inhibitor with alkaline phosphatase activity was produced by Streptomyces chromofuscus 34–1. Production of the proteinase inhibitor was closely associated with mycelial growth. The origin of carbon source did not significant effect the production of the inhibitor. The specific growth rate μ (h−1) and specific uptake of starch and glucose qcarb (gl−1h−1) are similar in the both cases of carbon sources. The specific proteinase inhibitory production rate q (TIU l−1 h−1) was high in the presence of glucose (about 33%). The production of alkaline phosphatase showed two phase kinetics. During the early exponential phase the alkaline phosphatase activity has a maximum at 24 h of cultivation. The next maximum was found to be at the end of cultivation. The highest specific alkaline phosphatase activity was determined at the second maximum during the cultivation of the strain (3800 mU/mg). Specific alkaline phosphatase production rate q (U l−1h−1) is higher in the presence of glucose. The proteinase inhibitor produced by Streptomyces chromofuscus 34–1 showed significant protective effect in the murine model of experimental influenza A/Aichi/2/67 (H3N2) virus infection. © 2005 Taylor and Francis Group, LLC.