Abstract—Cellulose is major source of plant biomass and β-1,4-glucosidic bonds in its structure are hydrolyzed by cellulases. These enzymes can be produced by microorganisms including fungi, bacteria and actinomycetes and are used today for the industrial applications in the pulp and paper, food and textile industries and in the conversion of plant biomass materials into industrially useful products such as sugars and bio-ethanol. The cost of production and low yields of these enzymes are the major problems for industrial applications. For this reason, there is a requirement that new microbial enzyme sources are investigated with the aim of improving cellulase production. In this study, the endo-β-1, 4 glucanase from local isolate Trichoderma ouroviride was produced in submerged fermentation using carboxymethylcellulose as a carbon source. The enzyme was purified by ammonium sulphate precipitation and gel chromatography with 7, 2-fold in a yield of 4, 1%. The optimal pH and temperature of purified enzyme was determined. In conclusion, the optimal pH and temperature for hydrolytic activity toward CMC was 50°C and pH 5, 0, respectively. It was understood that the purified enzyme has adequate activity and properties for industrial applications.

Index Terms—Cellulase, characterization, purification, trichoderma ouroviride.

S. Şahin and İ. Ozmen are with the Suleyman Demirel University, Faculty of Arts and Science, Chemistry Department, Turkey (e-mail: selmihansahin@ sdu.edu.tr, ismailozmen@sdu.edu.tr ).
Hacı H. Bıyık is with the Adnan Menderes University, Faculty of Arts and Science, Biology Department, Turkey (e-mail: hbiyik@adu.edu.tr ).

 

Cite:Selmihan Şahin, İsmail Ozmen, and Hacı H. Bıyık, "Purification and Characterization of Endo-β-1, 4-Glucanase from Local Isolate Trichoderma Ouroviride," International Journal of Bioscience, Biochemistry and Bioinformatics vol. 3, no. 2, pp. 129-132, 2013.