Cloning and characterization of thermostable-deoxy-D-ribose-5-phosphate aldolase from Hyperthermus butylicus
The 2-deoxy-D-ribose-5-phosphate aldolase gene from Hyperthermus butylicus was subcloned, overexpressed in Escherichia coli and purified to apparent homogeneity. Analysis of the sequence of gene revealed an open reading frame (ORF) of 672 base pairs encoding 237 amino acids predicted to yield a protein of molecular mass 26.4 kDa. The encoded protein was overexpressed in E. coli and purified to apparent homogeneity. The enzyme activity is optimal at pH 5.5 and 80°C. For...[Show more]
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|Source:||African Journal of Biotechnology|
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