Biochemical characterization of a recombinant pullulanase from Thermococcus kodakarensis KOD1 (pages 336–343)
T. Han, F. Zeng, Z. Li, L. Liu, M. Wei, Q. Guan, X. Liang, Z. Peng, M. Liu, J. Qin, S. Zhang and B. Jia
Article first published online: 8 JUL 2013 | DOI: 10.1111/lam.12118
Significance and Impact of the Study: Pullulanases have a great potential in industrial applications including the starch industry, the production of maltose syrups and high-purity glucose and fructose. In this study, a pullulanase from hyperthermophilic archaeon Thermococcus kodakarensis KOD1 was successfully expressed in Escherichia coli and the recombinant enzyme can be purified and characterized. The high activity, broad pH range and stability implicate it as a potential enzyme for industrial applications.