<i>In silico</i> analysis of insect-associated bacterial phytases reveals optimal biochemical properties and function in poultry gut condition

Twenty-six phytases from bacteria associated with the guts of black soldier fly larvae, fruit flies, and honey bees were identified. The mature chains of these phytases, except for the 4-phytase of <i>Bartocella apis</i> PEB0150, were predicted to carry a positive charge under the acidic conditions of the poultry upper gastrointestinal tract. They are stable (instability indices <40) and belong to histidine acid phosphatase family, which has been proven to be an effective poultry feed additive. The three-dimensional structure of the mature histidine-type phosphatase of <i>Tatumella</i> sp. JGM130 demonstrated the best quality and was found to be a homo-tetrameric protein. Molecular docking confirmed phytate binding at the catalytic motif of the histidine acid phosphatase family, RHGVRPP/AP/Q and HD.