http://nopr.niscpr.res.in/handle/123456789/60221 2026-10-12T13:19:56Z http://nopr.niscpr.res.in/handle/123456789/60230 Title: Decolorization of anthraquinone based dye (Vat Brown R) by Pseudomonas aeruginosa NCH - Optimization and kinetic study Authors: Mohanty, Swati Sambita; Kumar, Arvind Abstract: The objective of this research work is related to the fact that the source of isolation and acclimatization process influences the microorganism’s potential for the decolorization of various substances. Some of the widely used anthraquinone vat dyes decolorization by the pure bacterial strain is a significant aspect that will assist in the in-situ bioremediation of the ecosystem.The present study is to evaluate the enhanced decolorization of Vat Brown R by an isolated bacterium, Pseudomonas aeruginosa NCH, from textile dye wastewater under aerobic conditions. The effect of pH, temperature, and inoculum size was optimized using response surface methodology with the box-behnken experimental design. The strain NCH showed maximum decolorization efficacy under optimum conditions at pH 9.76, temperature 34.69C, and an inoculum size of 9.51% (v/v), respectively. A decolorization of 90.34% was observed with 100 mg L−1of Vat Brown R within 18h under these conditions. Confirmatory experiments have verified the optimum combination of the three variables predicted by RSM. Kinetics study was carried out using various approaches: Michaelis-Menten (Vmax = 29.1 mg L−1 h−1 and Km = 25.2 mg L−1), Lineweaver-Burk (Vmax = 30.12 mg L−1 h−1 and Km = 26.91 mg L−1), and Eadie-hofstee model (Vmax = 30.23 mg L−1h−1and Km = 27.29 mg L−1), and the results showed that the degradation followed a first-order reaction kinetics. The subsequent degradation of the dye and the formation of metabolites were studied using analytical techniques such as UV-vis spectroscopy and FT-IR analysis. UV-vis spectroscopy validated the detoxification of the dye and confirmed that Pseudomonas sp. NCH overcomes this decolorizing activity through biodegradation. This study investigated the highest decolorization efficiency of strain NCH used in the biodegradation of wastewaters containing anthraquinone dyes. Page(s): 709-717 2022-07-01T00:00:00Z http://nopr.niscpr.res.in/handle/123456789/60229 Title: Biochemical characterization with kinetic studies of melanogenic enzyme tyrosinase from white button mushroom, Agaricus bisporus Authors: Kaur, Ravneet; Sharma, Shivani; Kaur, Satvir; Sodhi, HS Abstract: In Agaricus bisporus, color is a key determinant for marketability and consumer acceptability. However, postharvest browning has become a major concern, affecting the overall economics of the mushroom industry. In button mushrooms, the tyrosinase enzyme (E.C.1.14.18.1) is responsible for the browning reactions by catalyzing the conversion of monophenols and diphenols into quinones which polymerize to form melanin. Thus, the present study focused on the purification and characterization of tyrosinase from A. bisporus. This enzyme was purified with a final yield of 19.71% and 32.05 purification fold. The study of enzymatic activity over a temperature (5-45°C) and pH range (3-10) showed that the optimum temperature was 35°C with pH 7. The kinetic studies revealed that Km values were different for catechol (0.71 mM) and L-dopa (0.87 mM), which indicated a higher affinity of the enzyme for catechol. Inhibition studies showed that cinnamic acid is a non-competitive inhibitor while salicylic acid is a competitive inhibitor of tyrosinase. The molecular weight of the enzyme was found to be 43 kDa and different amide regions were reflected by the FTIR spectra of the enzyme. This study may provide valuable insights into the structure, biochemical properties, and inhibition of tyrosinase enzyme for controlling mushroom browning. Page(s): 718-725 2022-07-01T00:00:00Z http://nopr.niscpr.res.in/handle/123456789/60228 Title: Effects of heavy metals on the viability of A549 cells Authors: Qian-wen, Wang; Jae-sik, Jeon; Kyung, Kim Jae Abstract: Heavy metals, such as Cd and Pb, are present in the particulate matter (PM) suspended in ambient air. Once internalized, they often accumulate in the human body and cannot be metabolized for long periods. Most previous studies on Cd and Pb metabolism used high concentrations of these heavy metals. In this study, we analysed the effects of low concentrations of Cd or Pb (similar to their concentrations in the PM) on the viability of lung epithelial cells and the secretion of pro-inflammatory factors, IL-6 and IL-8. A549 cells were cultured in the presence of Cd and Pb at 1 μg/L and 1 mg/L for 0, 4, 12, and 24 h and analysed using WST-8 and lactate dehydrogenase (LDH) assays and ELISA. Our results revealed that Cd and Pb induced comparable cytotoxicity and secretion of pro-inflammatory cytokines, IL-6 and IL-8, in a time-dependent manner, even at low concentrations. Altogether, our results suggest that heavy metals present in PM can cause chronic long-term effects on human lungs. Page(s): 726-731 2022-07-01T00:00:00Z http://nopr.niscpr.res.in/handle/123456789/60227 Title: Designing of promising Tromethamine-Diflunisal-Pyrrole combinations based on COX binding, drug-properties and safety Authors: Nambiar, Megha P; AR, Biju Abstract: Gastric issues that accompany the use of NSAIDs (Non-steroid anti-inflammatory drugs) are always a serious global concern. The inhibition of the Cycloxygenase enzyme (COX) limits the prostaglandin synthesis and thereby facilitates the control of pains, inflammation etc. But this creates gastric issues due to the reduction of mucin formation in the stomach. The present work was performed to create a modification in the structure of NSAID drug Diflunisal, to reduce the gastric effect of acidic moiety in the structure and elevate the overall biological properties. The drug Tromethamine, a base used in acidosis treatment was substituted to reduce the acidic issues. The heterocyclic compound pyrrole was substituted to elevate the properties. Neutral, salt, amide and ester combinations of Tromethamine-Diflunisal were designed, optimized and docked to the crystal structures of COX-1 (PDB ID: 6Y3C) and COX-2 (PDB ID: 5IKR) enzymes, using PyRx software. The combinations with lower COX-1 and COX-2 binding energies relative to Diflunisal were noted. It was analysed if the combinations of Diflunisal, Tromethamine and pyrrole lowers drug-properties or induce toxicities. Pyrrole substitution at position R4 was not found favourable for COX binding. Among the favourable combinations, DF19 is the Diflunisal- Pyrrole-Tromethamine combination, equally favourable for binding to COX targets. Page(s): 732-740 2022-07-01T00:00:00Z