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The phytase gene appA S  was isolated from  Shigella  sp. CD2 genomic library. The 3.8 kb DNA fragment contained 1299 bp open reading frame encoding 432 amino acid protein (AppA S ) with 22 amino acid signal peptide at N-terminal and three sites of N-glycosylation. AppA S  contained the active site RHGXRXP and HDTN sequence motifs, which are conserved among histidine acid phosphatases. It showed maximum identity with phytase AppA of  Escherichia coli  and  Citrobacter braakii . The appA S  was expressed in  Pichia pastoris  and  E .  coli  to produce recombinant phytase rAppA P  and rAppA E , respectively. Purified glycosylated rAppA P  and nonglycosylated rAppA E  had specific activity of 967 and 2982 U mg -1 , respectively. Both had pH optima of 5.5 and temperature optima of 60°C. Compared with rAppA E , rAppA P  was 13 and 17% less active at pH 3.5 and 7.5 and 11 and 18% less active at temperature 37 and 50°C, respectively; however, it was more active at higher incubation temperatures. Thermotolerance of rAppA P  was 33% greater at 60°C and 24% greater at 70°C, when compared with rAppA E . Both the recombinant enzymes showed high specificity to phytate and resistance to trypsin. To our knowledge, this is the first report on cloning and expression of phytase from  Shigella  sp.

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Cloning and Expression of Phytase appA Gene from Shigella sp. CD2 in Pichia pastoris and Comparison of Properties with Recombinant Enzyme Expressed in E. coli