Optimization of protease production by Bacillus licheniformis in Sugarcane bagasse using statistical experimental design

Sugarcane bagasse, the residue obtained after extracting the sugar juice from sugarcane was tested for the production of protease under solid-state fermentation (SSF) using Bacillus licheniformis. The fermentation variables were selected in accordance with Plackett-Burman design and were further optimized via response surface methodological approach. Four significant variables (K2HPO4, Beef extract, NaNO3 and Glycine) were selected for the optimization studies. The optimum values for the selected variables were; K2HPO4 -0.3464g/gds, Beef extract- 0.1039g/gds, NaNO3- 0.0334g/gds and Glycine- 0.1027g/gds. A second-order model equation was suggested and then validated experimentally.The model adequacy was very satisfactory as the coefficient of determination was 0.95. The maximum protease production was 146.28U/gd

Optimization of production, biochemical characterization and In Vitro evaluation of the therapeutic potential of fibrinolytic enzymes from a new Bacillus Amyloliquefaciens

The capacity of fibrinolytic enzymes to degrade blood clots makes them of high relevance in medicine and in the pharmaceutical industry. In this work, forty-three microorganisms of the genus Bacillus were evaluated for their potential to produce fibrinolytic proteases. Thirty bacteria were confirmed as producers of fibrinolytic enzymes, the best results obtained for the strain Bacillus amyloliquefaciens UFPEDA 485. The optimization of the enzyme production conditions was done by a central composite design (CCD) star 23 that allowed to define the optimal conditions for soybean flour and glucose concentrations and agitation rate. The highest fibrinolytic activity (FA) of 813 U mL-1 and a degradation of blood clot in vitro of 62% were obtained in a medium with 2% (w/v) of soybean flour and 1% (w/v) glucose at 200 rpm after 48 h of cultivation, at pH 7.2 and 37 °C. The obtained fibrinolytic enzyme was characterized biochemically. Fibrinolytic activity was inhibited by PMSF (fluoride methylphenylsulfonyl - C7H7FO2S) 91.52% and EDTA (ethylenediaminetetraacetic acid - C10H16N2O8) 89.4%, confirming to be a serine- metallo protease. The optimum pH and temperature were 7.0 and 37 oC, respectively, and the enzyme was stable for 12 h. The fibrinolytic activity at physiological conditions of this enzyme produced by Bacillus amyloliquefaciens UFPEDA 485, as well as its long term stability, demonstrate that it has suitable characteristics for human and veterinary applications, and promises to be a powerful drug for the treatment of vascular diseases.We express our thanks to Coordination for the Improvement of Higher Level Education Personnel (CAPES) - Doctoral Sandwich Program (PDSE) Nº 0259/ 12-8 and National Council for Scientific and Technological Development (CNPq) - Nº 202026/2011-6 for the financial support

The use of vasopressors in Takotsubo cardiomyopathy: Impact on neurological practice

10.1016/j.ijcard.2009.06.052International Journal of Cardiology1451131-IJCD