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Serpins: Purification and characterization of potent protease inhibitors fromClostridium thermocellum
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AbstractClostridium thermocellumproduces an extracellular cellulosome (a multiprotein complex produced by firmicutes bacteria), which, owing to its extracellular location, is open to protease attack. Serine protease inhibitors (serpins) protect bacteria against protease attack. However, their structure and function are poorly characterized. This study identified and amplified the serpin 1270 gene from the C. thermocellum genome. Purified serpins were cloned into the pTXB1 vector using the one-step sequence and ligation-independent cloning reaction and transformed into Escherichia coli BL21 DE3 cells. Enzyme overexpression and purification and enzyme inhibitory assays were performed. The results showed that serpin 1270 has 89% inhibition against Bacillus subtilisin and 64% inhibition against trypsin, chymotrypsin, and papain.
Cold Spring Harbor Laboratory
Title: Serpins: Purification and characterization of potent protease inhibitors fromClostridium thermocellum
Description:
AbstractClostridium thermocellumproduces an extracellular cellulosome (a multiprotein complex produced by firmicutes bacteria), which, owing to its extracellular location, is open to protease attack.
Serine protease inhibitors (serpins) protect bacteria against protease attack.
However, their structure and function are poorly characterized.
This study identified and amplified the serpin 1270 gene from the C.
thermocellum genome.
Purified serpins were cloned into the pTXB1 vector using the one-step sequence and ligation-independent cloning reaction and transformed into Escherichia coli BL21 DE3 cells.
Enzyme overexpression and purification and enzyme inhibitory assays were performed.
The results showed that serpin 1270 has 89% inhibition against Bacillus subtilisin and 64% inhibition against trypsin, chymotrypsin, and papain.
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