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Purification
and characterization of an extracellular cellulase from Anoxybacillus
gonensis O9 isolated from geothermal area in Turkey
Berna Genc1,
Hayrunnisa Nadaroglu2*, Ahmet Adiguzel3 and Ozkan
Baltaci3
1Department of
Genetic and Bioengineering, Faculty of Engineering and Life Sciences,
Gumushane University, 29100, Gumushane, Turkey
2Department of
Food Technology, Erzurum Vocational Training School, Ataturk University,
25240 Erzurum, Turkey
3Department of
Molecular Biology and Genetics, Faculty of Science, Ataturk University, 25240
Erzurum, Turkey
*Corresponding
Author E-mail: hnisa25@atauni.edu.tr
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Publication
Data
Paper received:
19 July 2014
Revised received:
30 December 2014
Accepted:
20 March 2015
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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 50oC 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 ?mol min-1 mg for Vmax and 0.46mM for Km.
Among effectors of the enzyme, Zn2+, Ca2+, Co2+
and EDTA decreased enzyme activity. ????
Key
words
Anoxybacillus
gonensis, 16S rRNA sequencing, Cellulase, Characterization
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