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Title: Purification and characterisation of an extra cellular protease inhibitor and extracellular proteases of Stroptomyces lividans '66'
Author: Oetari, A.
Awarding Body: University College of Swansea
Current Institution: Swansea University
Date of Award: 1996
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A proteinaceous protease inhibitor was identified and characterised from Streptomyces livdans '66' culture supernatants. The protein has a molecular weight of ˜11-kD. Comparison of the amino acid residues in a conserved region (two β-strands near the N-terminus involved in dimerization) indicated that this protein is related to other previously characterized Streptomyces proteinaceous protease inhibitors. The inhibitor obtained in this study has specificity for chymotrypsin-like serine proteases. A biological function of the inhibitor could be to control the activity of a native serine protease. Observations on the pH stability of the extracellular serine proteases of Streptomycs lividans '66' indicates that there are at least two types, one of which is stable in acidic pH and the other in neutral/alkaline pH. Their activities, however, are negligible in a liquid medium. Studies on the effect of carbon and nitrogen sources in complex and minimal solid media underline the importance of these sources for the production of proteases and protease inhibitor, and for morphological differentiation. Enhanced production of the serine protease and protease inhibitor occurred in the presence of glucose. The present study implies that the protease inhibitor of Streptomycs livdans '66' may regulate proteases during mycelial growth, aerial mycelium formation and sporulation. The neutral/alkaline serine protease may play a role in the proteolysis of substrate mycelia for aerial mycelium formation, while the acidic protease may play a role in the proteolysis of mycelia during sporulation.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available