Published: CABEQ 30 (2) (2016) 265-278
Paper type: Original Scientific Paper
S. Sahin, I. Ozmen and H. Bıyık
Abstract
An endo-β-1,4-glucanase (EG), produced under submerged fermentation by local
isolate Trichoderma atroviride, was purified using ammonium sulfate precipitation, column and ion exchange chromatography with 55.16 fold and a specific activity of 30.9
EU mg–1. The studies of PAGE, SDS-PAGE and zymogram test have been carried out.
The EG had optimum activity at pH 5.0 and 50 °C respectively. Using CMC as substrate,
the enzyme showed maximum activity (Vmax) of 6.7 (µmol glucose min–1) mL–1 with its
corresponding Km (Michaelis-Menten constant) value of 1.12 mg mL–1. While the EG
activity was activated by NaCl, inhibited by MgCl2 and MgSO4. Otherwise, Tween 80,
Triton X-100 and the total saponins known as biosurfactants enhanced the EG activity.
The obtained EG had low Km and high thermal stability. Additionally, usability of the EG
in biotechnological application was investigated. The results showed that the EG had
potentially sufficient effects on denim fabric and pretreated lignocellulosic wastes.
This work is licensed under a Creative Commons Attribution 4.0 International License
Keywords
endo-β-1,4-glucanase, purification, characterization, biosurfactant, saponin, Trichoderma atroviride