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.

Exact solution of one-dimensional relativistic jet with relativistic equation of state

Abstract: We study the evolution of one-dimensional relativistic jets, using the exact solution of the Riemann problem for relativistic flows For this purpose, we solve equations for the ideal special relativistic fluid composed of dissimilar particles in flat space-time and the thermodynamics of fluid is governed by a relativistic equation of state We obtain the exact solution of jets impinging on denser ambient media The time variation of the cross-section of the jet-head is modeled and incorporated We present the initial condition that gives rise to a reverse shock If the jet-head cross-section increases in time, the jet propagation speed slows down significantly and the reverse-shock may recede opposite to the propagation direction of the jet We show that the composition of jet and ambient medium can affect the jet solution significantly For instance, the propagation speed depends on the composition and is maximum for a pair-dominated jet, rather than a pure electron-positron or electron-proton jet The propagation direction of the reverse-shock may also strongly depend on the composition of the jet

Purification and characterization of pectin lyase secreted by Aspergillus flavus MTCC 10938

Abstract: An indigenously isolated fungal strain Aspergillus flavus MTCC 10938 was subjected to pectin lyase (PNL) production under submerged fermentation conditions. The enzyme was purified to homogeneity from the culture filtrate of the fungus involving concentration by ultrafiltration, anion exchange chromatography on DEAE cellulose and gel filtration chromatography on Sephadex G-100. The purified PNL gave a single protein band in SDS-PAGE analysis with a relative molecular mass corresponding to 50 kDa. Using citrus pectin as the substrate the Km and kcat values of the enzyme were obtained as 1.7 mg/ml and 66 s−1, respectively. The optimum pH of the purified PNL from A. flavus MTCC 10938 was 8.0 and up to 90% of its activity retained in the pH range from 3.0 to 11.0 after 24 h incubation. The optimum temperature of the purified enzyme was revealed at 55°C and it was completely stable up to 40°C when exposed for 30 min. The purified A. flavus MTCC 10938 PNL showed efficient retting of Crotalaria juncea fibres.