Potential application of two thermostable lichenases from a newly isolated Bacillus licheniformis UEB CF: Purification and characterization |
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Authors: | Fatma Chaari Fatma Bhiri Monia Blibech Sameh Maktouf Semia Ellouz-Chaabouni Raoudha Ellouz-Ghorbel |
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Institution: | 1. Unité enzymes et bioconversion, Biology Department, Sfax National School of Engineers, B.P. 1173, 3038 Sfax Cedex, Sfax University, Tunisia;2. Unité de service commun bioréacteur couplé à un ultrafiltre, Sfax National School of Engineers, B.P. 1173, 3038 Sfax Cedex, Tunisia |
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Abstract: | Two thermostable and alkali-stable β-1,3–1,4 glucanases (EC 3.2.1.73) EG1 and EG2 from a newly isolated Bacillus licheniformis UEB CF were purified. The molecular weights of EG1 and EG2 enzymes determined by SDS–PAGE were approximately 30 kDa and 55 kDa, respectively. The N-terminal amino acid sequences of EG1 and EG2 β-glucanases were determined to be GAAPIKKGTTKLN and DINGGGATLPQK, respectively. The optimum temperature, optimum pH, km and Vmax of EG1 were 70 °C, 5.0, 2.1 mg/ml and 21.25 μmol/min/mg, respectively. These values for EG2 were 60 °C, 7.0, 1.82 mg/ml and 18.54 μmol/min/mg, respectively.Both endoglucanases were highly active against barley β-glucan and lichenan. However, they were inactive against CMC and laminarin. The purified β-glucanases were found to be relatively stable toward non-ionic surfactants and oxidizing agents. In addition, both enzymes showed excellent stability and compatibility with a wide range of commercial solid detergents suggesting that they are a potential candidate in detergent industries formulation. |
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