Purification and properties of the catalytic domain of the thermostable pullulanase type II from Thermococcus hydrothermalis

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Abstract

A pullulanase type II was produced in Escherichia coli using the relevant gene from Thermococcus hydrothermalis. This protein was purified and its pullulanolytic and amylolytic activities were characterised. The optimum temperature and Ca2+ concentration for each activity were identical (105 °C and 0.09 mM), whereas the optimum pH (pHpullulan 5.75, pHamylose 5) and the influence of Ca2+ ions on the kinetic parameters were different. Further analyses revealed that this enzyme exhibits an endo-processive-like action and specifically cleaves α-1,6 bonds in pullulan.

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