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Physiological aggregation of maltodextrin phosphorylase from Pyrococcus furiosus and its application in a process of batch starch degradation to α-d-glucose-1-phosphate

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Journal of Industrial Microbiology & Biotechnology

Abstract

Maltodextrin phosphorylase from Pyrococcus furiosus (PF1535) was fused with the cellulose-binding domain of Clostridium cellulovorans serving as an aggregation module. After molecular cloning of the corresponding gene fusion construct and controlled expression in Escherichia coli BL21, 83% of total maltodextrin phosphorylase activity (0.24 U/mg of dry cell weight) was displayed in active inclusion bodies. These active inclusion bodies were easily isolated by nonionic detergent treatment and directly used for maltodextrin conversion to α-d-glucose-1-phosphate in a repetitive batch mode. Only 10% of enzyme activity was lost after ten conversion cycles at optimum conditions.

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Acknowledgments

The expert technical assistance of Radoslava Šályová is gratefully acknowledged. This work was supported by the Slovak Research and Development Agency under a contract no. APVV-51-040205 (http://www.biotec.chem.sk/glyctech).

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  1. Institute of Chemistry, Center for Glycomics, Slovak Academy of Sciences, Dúbravská cesta 9, 84538, Bratislava, Slovak Republic

    Jozef Nahálka

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Correspondence to Jozef Nahálka.

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Nahálka, J. Physiological aggregation of maltodextrin phosphorylase from Pyrococcus furiosus and its application in a process of batch starch degradation to α-d-glucose-1-phosphate. J Ind Microbiol Biotechnol 35, 219–223 (2008). https://doi.org/10.1007/s10295-007-0287-4

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  • DOI: https://doi.org/10.1007/s10295-007-0287-4

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