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Updated: Jun 17, 2026
Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG
Published on: May 16, 2017
Cloning, purification and characterisation of a recombinant purine nucleoside phosphorylase from Bacillus halodurans
Daniel F Visser1, Fritha Hennessy, Konanani Rashamuse
1Enzyme Technologies Group, CSIR Biosciences, Private Bag X2, Modderfontein, Johannesburg, 1645, South Africa.
Abstract:
A purine nucleoside phosphorylase from the alkaliphile Bacillus halodurans Alk36 was cloned and overexpressed in Escherichia coli. The enzyme was purified fivefold by membrane filtration and ion exchange. The purified enzyme had a V (max) of 2.03 x 10(-9) s (-1) and a K (m) of 206 microM on guanosine. The optimal pH range was between 5.7 and 8.4 with a maximum at pH 7.0. The optimal temperature for activity was 70 degrees C and the enzyme had a half life at 60 degrees C of 20.8 h.
