title: Novel phytases from Bifidobacterium pseudocatenulatum ATCC 27919 and Bifidobacterium longum subsp. infantis ATCC 15697.
abstract: Two  novel phytases have been characterized from Bifidobacterium pseudocatenulatum and Bifidobacterium longum subsp. infantis. The enzymes belong to a new subclass within the histidine acid phytases, are highly specific for the hydrolysis of phytate, and render myo-inositol triphosphate as the final hydrolysis product. They represent the first phytases characterized from this group of probiotic microorganisms, opening the possibilities for their use in the processing of high-phytate-content foods.
authors.affiliation: Grupo de Cereales, Instituto de Agroquímica y Tecnología de Alimentos (IATA-CSIC), Paterna, Valencia, Spain.
authors.forename: Juan Antonio
authors.initials: JA
authors.lastname: Tamayo-Ramos
authors.forename: Juan Mario
authors.initials: JM
authors.lastname: Sanz-Penella
authors.forename: María J
authors.initials: MJ
authors.lastname: Yebra
authors.forename: Vicente
authors.initials: V
authors.lastname: Monedero
authors.forename: Monika
authors.initials: M
authors.lastname: Haros
mesh_terms: D010832:6-Phytase / Q000235:genetics* / Q000378:metabolism; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D001644:Bifidobacterium / Q000145:classification* / Q000201:enzymology* / Q000235:genetics; D006801:Humans; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D010833:Phytic Acid / Q000378:metabolism*; D016133:Polymerase Chain Reaction; D019936:Probiotics; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D001426:Bacterial Proteins; D010833:Phytic Acid; D010832:6-Phytase