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A novel extracellular endoglucanase from a basidiomycete strain Peniophora sp. NDVN01 was purified 2.8-fold to homogeneity through ammonium sulfate precipitation and gel filtration with Bio-Gel P-100 and Sephadex G-75. The endoglucanase had a specific activity of 163.8 U/mg protein and a molecular mass of 32 kDa. | Turkish Journal of Biology Turk J Biol (2013) 37: 377-384 © TÜBİTAK doi:10.3906/biy-1207-37 http://journals.tubitak.gov.tr/biology/ Research Article Purification and characterization of a novel detergent- and organic solvent-resistant endo-beta-1,4-glucanase from a newly isolated basidiomycete Peniophora sp. NDVN01 1,2 1 2,3, 2 2 Dinh Kha TRINH , Dinh Thi QUYEN *, Thi Tuyen DO , Ngoc Minh NGHIEM Department of Life Science, College of Sciences, Thai Nguyen University, Quyet Thang Commune, Thai Nguyen City, Vietnam 2 Institute of Biotechnology, Vietnam Academy of Science and Technology, 10600 Hanoi, Vietnam 3 Department of Biotechnology and Pharmacology, University of Science and Technology of Hanoi, 10600 Hanoi, Vietnam Received: 19.07.2012 Accepted: 09.11.2012 Published Online: 30.07.2013 Printed: 26.08.2013 Abstract: A novel extracellular endoglucanase from a basidiomycete strain Peniophora sp. NDVN01 was purified 2.8-fold to homogeneity through ammonium sulfate precipitation and gel filtration with Bio-Gel P-100 and Sephadex G-75. The endoglucanase had a specific activity of 163.8 U/mg protein and a molecular mass of 32 kDa. Optimum temperature and pH were at 60 °C and 4.5, respectively. The enzyme was stable at up to 42 °C and in the pH range of 3.5–5.5 with a residual activity of over 80% for 24 h of treatment. Ni2+ activated but other metal ions showed no or slight inhibitory effect on the enzyme activity. The endoglucanase showed a high resistance to most tested detergents and organic solvents. The endoglucanase catalyzed the hydrolysis of barley β-glucan and carboxymethyl cellulose (CMC), but not toward xylan, locust bean gum, and Avicel, typical substrates for xylanase, mannanase and exoglucanase, respectively. The kinetic parameters Km, Vmax, Kcat, and Kcat/Km for barley β-glucan and carboxymethyl cellulose were 5.9 mg/mL, 9804 U/mg, 6.14 × 105 min–1, and 1.04 × 105 and 34.8 mg/mL, 1825 U/mg, 1.14 × 105 min–1, and 0.33 × 104, respectively. .
