Kuvempu University

About: Kuvempu University is a education organization based out in Shimoga, India. It is known for research contribution in the topics: Cyclic voltammetry & Carbon paste electrode. The organization has 1575 authors who have published 2210 publications receiving 39755 citations. The organization is also known as: KU.

Curcumin and capsaicin modulates LPS induced expression of COX-2, IL-6 and TGF-β in human peripheral blood mononuclear cells

Abstract: The mechanism of action of treatment of either curcumin or capsaicin or in combination on LPS (Lipopolysaccharide) induced inflammatory gene expression in peripheral blood mononuclear cells (PBMCs) was investigated using RT-PCR and in silico docking methods. RT-PCR analysis has shown that the curcumin and capsaicin significantly reduced LPS induced over expression of COX-2, IL-6 and TGF-β in PBMCs. Whereas combined molecules demonstrated synergistic response on the reduction of COX-2, IL-6 and TGF-β over expression in LPS induced PBMCs as compared to individual molecules. Further, The docking of curcumin and capsaicin at the active pockets of COX-2, IL-6 and TGF-β has shown − 3.90, − 4.49 and − 5.61 kcal/mol binding energy for curcumin and − 3.80, − 4.78 and − 5.76 kcal/mol binding energy for capsaicin, while multiple ligand simultaneous docking (MLSD) of both molecules has shown higher binding energy of − 4.24, − 5.35 and − 5.83 kcal/mol respectively. This has demonstrated the efficacy of combined curcumin and capsaicin against the LPS induced expression of pro-inflammatory cytokines in PBMCs. These results attributed the coordinated positive modulation on biochemical and molecular cellular process by combined curcumin and capsaicin as compared to individual molecules.

Thermostable lipase from Geobacillus sp. Iso5: Bioseparation, characterization and native structural studies

Abstract: The extracellular thermoalkaline lipase from Geobacillus sp. Iso5 was purified to homogeneity by ultrafiltration, 6% cross-linked agarose and Phenyl spehrose HIC column chromatography. The final purified lipase resulted in 8.7-fold with 6.2% yield. The relative molecular weight of the enzyme was determined to be a monomer of 47 kDa by SDS-PAGE and MALDI-TOF MS/MS spectroscopy. The purified enzyme exhibit optimum activity at 70 °C and pH 8.0. The enzyme retained above 90% activity at temperatures of 70 °C and about 35% activity at 85 °C for 2 h. However, the stability of the enzyme decreased at the temperature over 90 °C. The enzyme activity was promoted in the presence of Ca(2+) and Mg(2+) and strongly inhibited by HgCl2 , PMSF, DTT, K(+) , Co(2+) , and Zn (2+) . EDTA did not affect the enzyme activity. The secondary structure of purified lipase contains 36% α-helix and 64% β-sheet which was determined by Circular dichromism, FTIR, and Raman Spectroscopy.