Purification and characterization of an extracellular cellulase from Anoxybacillus gonensis O9 isolated from geothermal area in Turkey
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Attribution-NonCommercial-NoDerivs 3.0 United Statesinfo:eu-repo/semantics/closedAccesshttp://creativecommons.org/licenses/by-nc-nd/3.0/us/Date
2015Access
Attribution-NonCommercial-NoDerivs 3.0 United Statesinfo:eu-repo/semantics/closedAccesshttp://creativecommons.org/licenses/by-nc-nd/3.0/us/Metadata
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Genc, B., Nadaroglu, H., Adiguzel, A., & Baltaci, O. (2015). Purification and characterization of an extracellular cellulase from Anoxybacillus gonensis O9 isolated from geothermal area in Turkey. Journal of environmental biology, 36(6), 1319.Abstract
In the present study, cellulase was purified and characterized from Anoxybacillus gonensis (Gen bank Number: KM596794) which was isolated and characterized from Agri Diyadin Hot spring. It was found to synthesize cellulase which had a wide range of industrial applications. Twenty four-hour-cultured bacteria induced cellulase production and specific activities during the purification steps were 1.47, 81.06 and 109.4 EU mg(-1) protein at crude extract, ammonium sulphate precipitated and DEAE-Sephadex purification steps. The highest enzyme activity was observed at 50 degrees C and the optimum range of pH was 3-10. Molecular weight of enzyme was determined approximately 40kDa. The kinetic parameters of cellulase against carboxymethylcellulose (CMC) were 153.4 mu mol min(-1) mg for V-max and 0.46mM for K-m. Among effectors of the enzyme, Zn2+, Ca2+, Co2+ and EDTA decreased enzyme activity.
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