In this study, characterization of the immobilized yeast cells for ethanol production by varying the initial sugar and yeast cell concentration was performed. The results have indicated that the effective fermentation can be achieved using 1% of the immobilized yeast cells with 10-12% of initial total reducing sugar concentration. The role of plant and fungal based chemicals as activators were studied and the studies indicated that Chitin and Rhizopus Oryza biomass has shown signifi cant effects of increase in fermentation rate (47% and 23.94%) in free and immobilized cell-activator systems respectively. Continuous ethanol production studies with immobilized yeast cells suggested that the productivity can be improved up to 100% by reducing retention time. Also, these studies confi rmed the reusability of beads for up to 16 days without losing activity.
Requirement for a sophisticated analytical method using HPLC and HPTLC is in high demand to meet the needs of a small scale industry for analysis of drugs that are relatively expensive. Hence a simple method was proposed in the routine determination of Mafenide acetate in pharmaceutical formulations and bulk dosage forms that can be less expensive. An analytical method was developed for the estimation of Mafenide acetate drug substance by liquid chromatography. The chromatographic separation was achieved on phenyl column (Eclipse XDB-Phenyl 250*4.6, 5um) at ambient temperature. The separation was achieved employing a mobile phase consisting of 0.1 %v/v Trifluoroacetic acid in water: Methanol (10:90). The flow rate was 1.0 ml/ minute and ultraviolet detector at 245nm. The average retention time for Mafenide acetate was 3.3 minutes. The proposed method was validated for selectivity, precision, linearity and accuracy. All validation parameters were checked and are found within the acceptable range. The assay methods were found to be linear ranging from 50-150 µg/ml for Mafenide acetate. The parameters considered for the procedure are related limit, selectivity, linearity, range, accuracy and precision are defined. Thesample solution leads to unequivocal, absolute identification of the analyte peak of interest apart from all other matrix components. The objective of our work is to form a basis for production procedure and control, which are designed to assure that the drug products have the identity, Quality, and purity. The results obtained could be treated as simple, sensitive and reproducible for determination of Mafenide acetate in pharmaceutical formulations.
The capability of an algal species to remove NO2 and NO in the simulated fl ue gas was established using Dunaliella salina in Photobioreactors under two variants of NOx sources. The concentrations studies were in the range between 25ppm to 150ppm. The diffusion of NOx and subsequent reaction with water resulted in NO3-and NO2-in the growth medium. Algal growth by absorption of NO3-and NO2-created a nitrate gradient in the bulk medium resulting in NOx uptake rates from the gas phase of up to 96%, leaving the unconsumed nitrogen of up to 7 mg-N/L in the growth medium. Algal species having an initial cell density of 2.8x105 cells/mL grew to the cell density of 1.73x107 cells/mL
Endo- β-N-acetylgucosaminidases (ENGases) are the enzymes that catalyze both hydrolysis and
transglycosylation reactions. It is of interest to study ENGases because of their ability to synthesize glycopeptides.
Homology models of Human, Arabidopsis thaliana and Sorghum ENGases were developed and their active sites
marked based on information available from Arthrobacter protophormiae (PDB ID: 3FHQ) ENGase. Further, these
models were docked with the natural substrate GlcNAc-Asn and the inhibitor Man3GlcNAc-thiazoline. The catalytic
triad of Asn, Glu and Tyr (N171, E173 and Y205 of bacteria) were found to be conserved across the phyla. The crucial
Y299F mutation showing 3 times higher transglycosylation activity than in wild type Endo-A is known. The hydrolytic
activity remained unchanged in bacteria, while the transglycosylation activity increased. This Y to F change is found
to be naturally evolved and should be attributing higher transglycosylation rates in human and Arabidopsis thaliana
ENGases. Ligand interactions Ligplots revealed the interaction of amino acids with hydrophobic side chains and polar
uncharged side chain amino acids. Thus, structure based molecular model-ligand interactions provide insights into
the catalytic mechanism of ENGases and assist in the rational engineering of ENGases.
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