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.

A Laccase of Fomes durissimus MTCC-1173 and Its Role in the Conversion of Methylbenzene to Benzaldehyde

Abstract: A laccase has been purified from the liquid culture growth medium containing bagasse particles of Fomes durissimus. The method involved concentration of the culture filtrate by ultrafiltration and anion exchange chromatography on diethyl aminoethyl cellulose. The sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS-PAGE) and native polyacrylamide gel electrophoresis both gave single protein band indicating that the enzyme preparation was pure. The molecular mass of the purified laccase determined from SDS-PAGE analysis was 75 kDa. Using 2,6-dimethoxyphenol as the substrate, the determined Km and kcat values of the laccase are 182 μM and 0.35 s−1, respectively, giving a kcat/Km value of 1.92 × 103 M−1 s−1. The pH and temperature optimum were 4.0 and 35 °C, respectively. The purified laccase has yellow colour and does not show absorption band around 610 nm found in blue laccases. Moreover, it transformed methylbenzene to benzaldehyde in the absence of mediator molecules, property exhibited by yellow laccases.

Oxidation of polyaromatic hydrocarbons in systems containing water miscible organic solvents by the lignin peroxidase of Gleophyllum striatum MTCC-1117.

Abstract: Lignin peroxidase has been purified to homogeneity using a process of concentration by ultrafiltration and anion exchange chromatography on diethylaminoethyl (DEAE) cellulose from the liquid culture filtrate of the brown rot fungi Gleophyllum striatum MTCC‐1117. The molecular mass of the purified enzyme is 43 kDa as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS‐PAGE) analysis. The K m values for the enzyme using veratryl alcohol, hydrogen peroxide and n‐propanol were 66 µM, 82 µM and 476 µM, respectively. The pH and temperature optima of the enzyme were 2.8 and 25°C, respectively. The enzyme is completely inhibited by 20% of the water miscible organic solvents acetone dioxane, diethylether, acetonitrile and dimethylformamide. The lignin peroxidase oxidizes polycyclic aromatic hydrocarbons pyrene, acenaphthene, anthracene, dibenothiophene and 9‐methyl anthracene.