Abstract

Inkyung Park and Jaiesoon Cho

Intracellular phytase activity was found in the Antarctic bacterial isolate, JPK1. Based on 16S rRNA gene sequence analysis, the strain was related to Pseudomonas sp. The optimal activity of JPK1 phytase occurred at 50�?�C and pH 5.0 to 5.5. The enzyme was highly specific for phytate with little or no other phosphate conjugates. Enzyme activity was strongly inhibited by Cu 2+ and Zn2+, and completely inactivated by sodium dodecyl sulfate. The enzyme effectively liberated inorganic phosphate from wheat bran, a main feedstuff with high phytate content. The enzyme may be a good candidate for use as an environmental-friendly feed additive to enhance the nutritive value of phytate and reduce phosphorus pollution.