Gene Expression in Escherichia coli and Purification of Recombinant Type II Pullulanase from a Hyperthermophilic Archaeon, Pyrobaculum calidifontis
Gene Expression in Escherichia coli and Purification of Recombinant Type II Pullulanase from a Hyperthermophilic Archaeon, Pyrobaculum calidifontis
Habib-ur-Rehman1, Masood Ahmed Siddiqui1,*, Abdul Qayyum1, Arifa Bano1 and Naeem Rashid2
ABSTRACT
Type II pullulanase also known as amylopullulanase hydrolyzes α-1,6 glycosidic bonds in pullulan and α-1,6 as well as α-1,4 glycosidic bonds in starch. Most of the previously reported type II pullulanases are metal ion dependent and hard to purify, to homogeneity, due to low level of expression or the proteolytic machinery of the host. Herein we report expression in Escherichia coli and purification of metal ion independent type II pullulanase from Pyrobaculum calidifontis. Thermophilic origin and metal ion independency of the enzyme reported in this study make it a potential candidate for starch hydrolyzing industry.
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August 2018
Vol. 50, Iss. 4, Pages 1199-1600
