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BACKGROUND Streptomyces transglutaminase (TGase) is naturally synthesized as zymogen (pro-TGase), which is then processed to produce active enzyme by the removal of its N-terminal pro-peptide. This pro-peptide is found to be essential for overexpression of soluble TGase in E. coli. However, expression of pro-TGase by E. coli requires protease-mediated(More)
Streptomyces transglutaminase (TGase) is an important industrial enzyme that catalyzes cross-linking of proteins. It is secreted as a zymogene and then is activated by proteases under physiological conditions. Although the activation process of TGase has been well investigated, the physiological function of TGase in Streptomyces has not been revealed. In(More)
Streptomyces transglutaminase (TGase) has been widely used in food, pharmaceutical and textile industries. Streptomyces TGase is naturally synthesized as zymogen (pro-TGase), which is then processed to produce active enzyme by removing its N-terminal pro-peptide. Although the pro-peptide is essential for TGase folding and secretion, few studies have been(More)
We demonstrate the generation of a 1.1-1.7µ m supercontinuum in a 1.3m long air-suspended-core tellurite holey-fiber with a nominal zero-dispersion wavelength of ~1.38µm. The fiber is pumped at 1.06µm with a 20ps pulsed fiber laser. The high Raman gain-coefficient of tellurite glass is attributed a key role in the supercontinuum generation.
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