Deen Dayal Upadhyay Gorakhpur University

About: Deen Dayal Upadhyay Gorakhpur University is a education organization based out in Gorakhpur, Uttar Pradesh, India. It is known for research contribution in the topics: Thermal decomposition & Lymnaea acuminata. The organization has 1032 authors who have published 1591 publications receiving 21734 citations. The organization is also known as: Gorakhpur University.

Synthesis, structural characterization and biological studies of neodymium(III) and samarium(III) complexes with mercaptotriazole Schiff bases

Abstract: A series of neodymium(III) and samarium(III) complexes of type [Ln(L)Cl(H2O)3] have been synthesized with Schiff bases (LH2) derived from 3-(phenyl/substituted phenyl)-4-amino-5-mercapto-1,2,4-triazoles and isatin. The structures of the complexes were established using elemental analysis, molar conductivities, magnetic moments, infrared, NMR (1H, 13C) and UV–visible spectra, X-ray diffraction and mass spectrometry. The thermal behaviour of these compounds under non-isothermal conditions was investigated using thermogravimetry and differential thermogravimetry. The intermediates obtained at the end of various thermal decomposition steps were identified from elemental analysis and infrared spectral studies. All the ligands and their complexes were also screened for their antibacterial activity against Staphylococcus aureus and Bacillus subtilis and antifungal activity against Aspergillus niger, Aspergillus flavus and Colletotrichum capsici. The screening results were correlated with the structural features of the compounds. Copyright © 2015 John Wiley & Sons, Ltd.

Characterization of a neutral pectin lyase produced by Oidiodendron echinulatum MTCC 1356 in solid state fermentation.

Abstract: A neutral pectin lyase produced by a new fungal strain Oidiodendron echinulatum MTCC 1356 under solid state fermentation using wheat bran as agro waste has been studied. The enzyme was purified by ammonium sulphate precipitation (30-60%), DEAE anion exchange and Sephadex G-100 column chromatographies. The SDS-PAGE and native PAGE revealed two bands of sizes 42 and 47 kDa. The enzyme was purified 37 fold with specific activity of 4.5 U/mg and 2.25% yield. The K(m) and V(max) values determined using citrus pectin were 1.2 mg/ml and 0.36 IU/min respectively. The pH and temperature optima were pH 7.0 and 50 °C, respectively. The pH stability was around 5.0 for 24 h at 20 °C. The purified enzyme retained maximum activity for 30 min upto 50 °C. The activation energy for thermal denaturation of the purified enzyme was found to be 60.0 kJ/Mol. The effects of various metal ions and protein inhibitors on enzyme activity have revealed total inhibition of the enzyme activity in the presence of Ag(+) and Cu(+) and KMnO(4) at 1 mM. The neutral pectin lyase showed retting of Crotalaria juncea fibre in the presence of EDTA.

Purification and characterisation of lignin peroxidase from Pycnoporus sanguineus MTCC-137

Abstract: Extracellular secretion of lignin peroxidase from Pycnoporus sanguineus MTCC-137 in the liquid culture growth medium amended with lignin containing natural sources has been shown. The maximum secretion of lignin peroxidase has been found in the presence of saw dust. The enzyme has been purified to homogeneity from the culture filtrate of the fungus using ultrafiltration and anion exchange chromatography on DEAE-cellulose. The purified lignin peroxidase gave a single protein band in sodium dodecylsulphate polyacrylamide gel electrophoresis corresponding to the molecular mass 40 kDa. The K m, k cat and k cat/K m values of the enzyme using veratryl alcohol and H2O2 as the substrate were 61 M, 2.13 s−1, 3.5 × 104 M−1s−1 and 71 M, 2.13 s−1, 3.0 × 104 M−1 s−1 respectively at the optimum pH of 2.5. The temperature optimum of the enzyme was 25°C.

Pectinases: from microbes to industries

Abstract: Pectinases are a group of enzymes that degrade pectic substances present in plant cell walls. Depending upon their nature, whether acidic or alkaline, they play an important role in fruit juice and textile industries. Recent studies on these enzymes deciphered their other industrial applications such as oil extraction, coffee and tea fermentation, treatment of industrial wastewater, and biobleaching of pulp. Use of pectinases over chemicals in these industries makes the whole process environment-friendly. This chapter focuses on the applications of microbial pectinases in the food, agriculture, and environment sectors.