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Vile Parle west, India

Mehta R.S.,University of Mumbai | Jholapara R.J.,University of Mumbai | Sawant C.S.,Shri Cb Patel Research Center
International Journal of Pharma and Bio Sciences | Year: 2013

Poultry industry waste contains a major proportion of feathers, which comprise mainly of keratin.Keratin is an insoluble, fibrous protein, which makes the feathers resistant to proteolytic enzymes. Several microorganisms can carry out the degradation of such complex substrates. The present study exploits the ability of soil bacteria to degrade feather wastes. Bacteria can degrade feather keratin with their enzyme: keratinase. By screening poultry farm soil samples, two feather degrading isolates were obtained which showed degradation of 1% feathers within 7 days. On the biochemical identification and 16S rRNA sequencing, the isolates showed 99% homology with Bacillus licheniformis and Bacillus subtilis. Medium optimization for maximum enzyme production was performed. The optimized conditions showed significant increase in enzyme production, as determined by the activity i.e. 14.344U/ml/min for B. licheniformis and 12.934U/ml/min for B. subtilis. The study shows the potential of the isolates to carry out eco-friendly disposal of feathers.

Jholapara R.J.,Institute of Management Sciences | Mehta R.S.,Institute of Management Sciences | Sawant C.S.,Shri Cb Patel Research Center
International Journal of Pharma and Bio Sciences | Year: 2013

Chitinases are group of enzymes which play a significant role in degrading chitin. The present study explores the natural ability of the bacteria to utilize chitin as a source of energy. Soil samples were screened for chitinolytic organisms and strain which produced highest chitinolytic activity was selected. Biochemical analysis revealed that the isolate belongs to the genus Bacillus. It was identified upto the species level as Bacillus licheniformis, using 16S rRNA based identification system. The cultural conditions for production of chitinase was optimized which resulted in a significant increase in the enzyme activity. The study demonstrates the potential of the isolate for industrial application such as production of bioactive chitin-oligosachharides.

Shinde Sachin R.,Shri Cb Patel Research Center | Suvarna I.B.,Shri Cb Patel Research Center | Namdev S.P.,Shri Cb Patel Research Center | Suman B.Y.,Shri Cb Patel Research Center | Ashok M.B.,Shri Cb Patel Research Center
E-Journal of Chemistry | Year: 2010

A Simple, fast and precise reversed phase high performance liquid chromatographic method is developed for the simultaneous determination of satranidazole and ofloxacin. Chromatographic separation of these drugs were performed on Kromasil C18 column (250 x 4.6 mm, 5 μ) as stationary phase with a mobile phase comprising of 20 mM potassium dihydrogen phosphate: acetonitrile in the ratio of 60:40 (v/v) containing 0.1% glacial acetic acid at a flow rate of 1 mL/min and UV detection at 318 nm. The linearity of satranidazole and ofloxacin were in the range of 1.5 to 3.6 μg/mL and 1.0 to 2.4 μg/mL respectively. The recovery was calculated by standard addition method. The average recovery was found to be 100.63% and 100.02% for satranidazole and ofloxacin respectively. The proposed method was found to be accurate, precise and rapid for simultaneous determination of satranidazole and ofloxacin.

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