The bacterium with an ability to produce extracellular fibrinolytic protease was isolated and identified as Stenotrophomonas maltophilia Gd2 based on ribotyping. The in-vitro fibrinolytic profile of this enzyme depicted 73% of fibrin clot dissolution within 4 h. Fibrinolytic enzyme yield influenced by different physiological (incubation time, temperature, agitation and pH), nutritional (macronutrients such as carbon and nitrogen sources) and biological (inoculums age and inoculums concentration) parameters of fermentation which were optimized based on one-factor-at-a-time (OFAT) approach. The enzyme yield improved from 886 to 1795 FU ml−1 upon OFAT; optimized conditions include temperature – 33 °C, pH – 8.0, incubation time – 36 h, agitation – 150 RPM, 3% v/v inoculums and age of inoculum – 18 h. Further optimization of enzyme production was achieved with implementation of Plackett-Burman media designing where the production levels increased to 3411 FU ml−1 and noticed that peptone, pH, dextrose and K2HPO4 was found to be significant factor. This ms reports the highest fibrinolytic enzyme yield with S. maltophilia to that of literature reports.
A new series of ferrocenyl sugar-triazole conjugates, derived from D-xylose, D-ribose and D-galactose, linked by a 2,4thiazolidinedione moiety, has been prepared. Facile 1,3-dipolar-Huisgen coupling reactions of the respective sugar azides with the ferrocenyl 2,4-thiazolidinedione alkyne units give the corresponding conjugates. These conjugates have been characterized by various spectroscopic techniques, including UV/Vis [a]
Synthesis and CharacterizationThe compound 2,4-thiazolidinedione was prepared by a literature method [26] and was condensed with ferrocene-carboxaldehyde 1, under Knoevenagel conditions, to form compound 2, Scheme 1. Synthesis of ferrocenyl 2,4-thiaolidinedione alkyne.Scheme 2. Synthesis of ferrocenyl 2,4-thiazolidinedione sugar-triazole conjugates 5a-g.Eur. J. Inorg. Chem. 2018, 1571-1580 www.eurjic.org
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