Extracellular Alkaline Lipase from a Novel Fungus
 Curvularia sp. DHE 5: Optimisation of Physicochemical Parameters, Partial Purification and Characterisation

• Published in: Food technology and biotechnology Vol. 55; no. 2; pp. 206 - 217
• Main Authors: El-Ghonemy, Dina Helmy, El-Gamal, Mamdouh S, Tantawy, Amir Elsayed, Ali, Thanaa Hamed
• Format: Journal Article
• Language: English
• Published: Croatia Sveuciliste U Zagrebu 01.04.2017; Sveuciliste u Zagrebu, Prehramheno-Biotehnoloski Fakultet; University of Zagreb Faculty of Food Technology and Biotechnology
• Subjects: agro-industrial residues; Ammonium; Ammonium sulfate; Curvularia sp. DHE 5; Dialysis; Enzymes; Fermentation; Fractionation; Fungi; Glycerol; Growth; Inoculum; Lipase; lipase characterisation; Moisture content; Morphology; Oils & fats; Olive oil; optimisation of culture conditions; Original Scientific Papers; pH effects; Phenols; Physicochemical properties; Plates; Potassium chloride; Production processes; Purification; Seeds; Solid state fermentation; Substrates; Temperature effects; Thermal stability; Vegetable oils; Wheat; Wheat bran; Egypt; Alexandria Egypt; optimisation of culture conditions; Curvularia sp. DHE 5; agro-industrial residues; lipase characterisation; lipase
• ISSN: 1330-9862; 1334-2606
• DOI: 10.17113/ftb.55.02.17.4958

Thirty isolated fungal strains were screened for lipase production using Phenol Red plates, containing tributyrin as lipidic substrate, and a novel fungus identified genetically as sp. DHE 5 was found as the most prominent strain. Various agro-industrial substrates were evaluated as inert supports for lipase production in solid-state fermentation. The highest yield of lipase ((83.4±2.2) U/g on dry mass basis) was reported with wheat bran medium after seven days of fermentation at pH=7.0, temperature of 30 °C, 70% moisture content, inoculum size of 1.27·10 spore/mL and 2% olive oil as an inducer. Supplementation of the medium with 0.05% KCl as an ion source further increased lipase production to (88.9±1.2) U/g on dry mass basis. The enzyme was partially purified through ammonium sulphate fractionation (40%) followed by dialysis, and its optimum pH and temperature were reported at 8.0 and 50 °C, respectively, with remarkable pH and thermal stability.