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Turkish Journal of Biology

DOI

10.3906/biy-1207-37

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. Ni^2^+ 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 \beta-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 K_m, V_{max}, K_{cat}, and K_{cat}/K_m for barley \beta-glucan and carboxymethyl cellulose were 5.9 mg/mL, 9804 U/mg, 6.14 × 105 min^{-1}, and 1.04 × 10^5 and 34.8 mg/mL, 1825 U/mg, 1.14 × 10^5 min^{-1}, and 0.33 × 10^4, respectively. Hydrolysis of CMC liberated cellobiose, cellotriose, cellotetraose, and a detectable amount of glucose. These results suggest that the endoglucanase might potentially be used in enzymatic reactions and to investigate the efficacy of feed enzymes.

Keywords

Characterization, endoglucanase, enzyme kinetics, detergent- and organic solvent-resistant, purification, Peniophora sp. NDVN01

First Page

377

Last Page

384

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