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Mannanase Transfer into Hexane and Xylene by Liquid–Liquid Extraction

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Abstract

The formation of noncovalent complexes between glycosidase, endo-1,4-β-d-mannanase, and ionic surfactant di(2-ethylhexyl) sodium sulfosuccinate (AOT) was shown to promote protein transfer into organic solvents such as xylene and hexane. It was found that mannanase can be solubilized in hexane and in xylene with concentration at least 2.5 and 2.0 mg/ml, respectively. The catalytic activity of the enzyme in hexane spontaneously increases with the concentration of AOT and is about 10% of the activity in aqueous system. In xylene, a catalytic activity higher than that in bulk aqueous conditions was found for the samples containing 0.1–0.3 mg/ml of mannanase, while for the samples with a higher concentration of enzyme, the activity was hardly detected.

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Acknowledgments

This work was funded by the Danish National Advanced Technology Foundation through the ProSURF platform (Protein-Based Functionalization of Surfaces). SS thanks Elin Ellebaek Petersen and Masoud Zargahi (Genencor, Danisco A/S) for support and fruitful discussions.

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Authors and Affiliations

  1. Interdisciplinary Nanoscience Center (iNANO), Aarhus University, Aarhus C, 8000, Denmark

    Stepan Shipovskov, Flemming Besenbacher & Duncan S. Sutherland

  2. Genencor, Danisco A/S, Brabrand, 8220, Denmark

    Karsten M. Kragh, Brian S. Laursen & Charlotte H. Poulsen

  3. Department of Physics and Astronomy, Aarhus University, Aarhus C, 8000, Denmark

    Flemming Besenbacher

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  1. Stepan Shipovskov
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  2. Karsten M. Kragh
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  6. Duncan S. Sutherland
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Correspondence to Stepan Shipovskov.

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Shipovskov, S., Kragh, K.M., Laursen, B.S. et al. Mannanase Transfer into Hexane and Xylene by Liquid–Liquid Extraction. Appl Biochem Biotechnol 160, 1124–1129 (2010). https://doi.org/10.1007/s12010-009-8661-5

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