Please use this identifier to cite or link to this item: http://localhost:8080/xmlui/handle/123456789/408
Title: Recombinant expression and characterization of L-Asparaginase II from a moderately thermotolerant bacterial isolate
Authors: Vidya, J
Pandey, A
Keywords: Moderately thermotolerant
L-asparaginase II
PelB leader
Nickel affinity
Thermostability
Issue Date: Jul-2012
Publisher: Springer
Citation: Applied Biochemistry and Biotechnology
Abstract: A moderately thermotolerant bacterium belonging to Enterobacteriaceae, which can grow at 44.5 °C, was isolated from cow dung; L-asparaginase II gene was isolated by PCR, cloned, and expressed in pET 20b with pelB leader sequence and 6× Histidine tag at the C-terminal end. The active protein from the soluble sonicated fraction was purified through nickel affinity chromatography. After characterization, the purified protein showed optimum activities at a temperature of 37 °C and in a buffer system of pH 6 to 7. The enzyme exhibited thermostability at 50 °C with a 33% and 28% of activity retention after 45 and 60 min. The kinetic parameters for the enzyme were calculated from Lineweaver–Burk plot,and Km and Vmax were 0.89 mM and 0.18 U/mg, respectively
URI: http://hdl.handle.net/123456789/408
Appears in Collections:2012

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