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Purification and characterization of an organic solvent-tolerant alkaline cellulase from a halophilic isolate of Thalassobacillus

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Abstract

An extracellular cellulase from Thalassobacillus sp. LY18 was purified 4.5-fold with a recovery of 21 % and a specific activity of 52.4 U mg−1 protein. Its molecular mass was 61 kDa estimated by SDS-PAGE. It was an endoglucanase for soluble cellulose with optimal activity was at 60 °C and pH 8 with 10 % (w/v) NaCl. It was stable from 30 to 80 °C and from pH 7 to 11 with NaCl from 5 to 17.5 % (w/v). EDTA inhibited activity indicating it was a metalloenzyme. Inhibition by diethyl pyrocarbonate and β-mercaptoethanol suggested that histidine residues and disulfide bonds may play important roles in its catalytic function. The cellulase was highly active in non-ionic surfactants and was stable in water-insoluble organic solvents with log P ow ≥ 2.13.

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Acknowledgments

This work was financially supported by Shanxi Provincial Science and Technology Foundation (grants no. 20110021) and Natural Science Fund of Shanxi Province (grants no. 2011021031–4).

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Correspondence to Xin Li.

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Li, X., Wang, HL., Li, T. et al. Purification and characterization of an organic solvent-tolerant alkaline cellulase from a halophilic isolate of Thalassobacillus . Biotechnol Lett 34, 1531–1536 (2012). https://doi.org/10.1007/s10529-012-0938-z

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  • DOI: https://doi.org/10.1007/s10529-012-0938-z

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