Physiological roles of leupeptin and extracellular proteases in mycelium development of Streptomyces exfoliatus SMF13

Article Abstract:

The physiological roles of the extracellular proteases made by Streptomyces exfoliatus SMF13 were examined in terms of mycelial growth, autolysis of mycelia after the stationary phase in submerged culture, and morphological differentiation of surface culture. The extracellular proteases made are chymotrypsin-like protease, metalloprotease and trypsin-like protease. The addition of leupeptin inhibited the autolysis of mycelia after the stationary phase in submerged culture; on surface cultures, aerial mycelium formation is very much retarded by the addition of leupeptin.

Proteases, Molecular microbiology

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Trypsin-like protease of Streptomyces exfoliatus SMF13, a potential agent in mycelial differentiation

Article Abstract:

Trypsin-like protease (TLP) and leupeptin have morphological differentiation roles in Streptomyces exfoliatus, as formation of aerial mycelium coincides with the production of TLP. This can be concluded, because in bld mutants obtained from UV-mutagenesis, morphological differentiation is repressed under conditions preventing leupeptin inactivating enzyme and TLP synthesis. In whi mutant, mycelium autolysis and TLP and LIE production are retarded compared to the parent strain. TLP hydrolyzes mycelium protein extract but leupeptin inhibits this.

Physiological aspects, Fungi, Microbial enzymes

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Cloning and heterologous expression of the gene for BLIP-II, a beta-lactamase-inhibitory protein from Streptomyces expoliatus SMF19

Article Abstract:

Experiments were performed to clone and analyze a gene encoding beta-lactamase-inhibitory proteins (BLIP-I and BLIP-II) and its heterologous expression in Escherichia coli and Streptomyces lividans. Results showed that BLIP-II was a different protein as suggested by the different molecular mass and amino acid sequence observed from those of BLIP from S. clavuligerus. It was also observed that while BLIP may function as a protector of autogenous beta-lactam antibiotics from beta-lactamase, BLIP-II does not have this protective ability.

Escherichia coli, Cloning, Beta lactamases, Enzyme inhibitors, Beta lactam antibiotics

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