Publications by authors named "Florette Szukala"
Article Synopsis
- Eukaryotic serpins are known protease inhibitors involved in various physiological processes, particularly in inflammatory bowel diseases, but bacterial serpins, especially those from gut microbiota, are less studied.
- Research focused on two putative serpin genes from the gut bacterium Eubacterium sireaum, leading to the discovery and purification of their proteins, named Siropins, which effectively inhibit specific human serine proteases related to inflammation.
- Biochemical analysis showed Siropins have distinct properties; Siropin 1 is stable at low pH while Siropin 2 is thermoactive, both exhibiting strong inhibitory capabilities that may help regulate intestinal protease activity.
The phyL gene encoding phytase from the industrial strain Bacillus licheniformis ATCC 14580 (PhyL) was cloned, sequenced, and overexpressed in Escherichia coli. Biochemical characterization demonstrated that the recombinant enzyme has an apparent molecular weight of nearly 42 kDa. Interestingly, this enzyme was optimally active at 70-75 °C and pH 6.
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