TAILIEUCHUNG - Purification and characterization of a novel detergent- and organic solvent-resistant endo-beta-1,4-glucanase from a newly isolated basidiomycete Peniophora sp. NDVN01
A novel extracellular endoglucanase from a basidiomycete strain Peniophora sp. NDVN01 was purified 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 U/mg protein and a molecular mass of 32 kDa. | Turkish Journal of Biology Turk J Biol (2013) 37: 377-384 © TÜBİTAK doi: 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: Accepted: Published Online: Printed: Abstract: A novel extracellular endoglucanase from a basidiomycete strain Peniophora sp. NDVN01 was purified 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 U/mg protein and a molecular mass of 32 kDa. Optimum temperature and pH were at 60 °C and , respectively. The enzyme was stable at up to 42 °C and in the pH range of – 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 mg/mL, 9804 U/mg, × 105 min–1, and × 105 and mg/mL, 1825 U/mg, × 105 min–1, and × 104, respectively. .
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