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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

1Department of Chemistry, Biotechnology Research Laboratory, University of Balochistan, Quetta 87300 
2School of Biological Sciences, University of the Punjab, Quaid-e-Azam Campus, Lahore 54590

*      Corresponding author: masoodbioeng@hotmail.com

 

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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Pakistan Journal of Zoology

December

Vol. 50, Iss. 6, Pages 1999-2398

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