Phytase activity as a novel metabolic feature inBifidobacterium

Abstract

Phytase activity has been detected for the first time in Bifidobacterium spp. These bacteria were able to dephosphorylate phytic acid (myo-inositol hexaphosphate, IP(6)) and generate several myo-inositol phosphate intermediates (IP(3)-IP(5)). B. globosum and B. pseudocatenulatum were optimally active at neutral-alkaline pH and B. adolescentis, B. angulatum and B. longum at acid pH. B. pseudocatenulatum showed the highest levels of phytase activity. This species produced maximum activity in the exponential phase of growth and when fructo-oligosaccharides were used as carbon source in the culture medium. The potential role of phytase activity from Bifidobacterium spp. in the reduction of the antinutritional properties of IP(6) is discussed.

Novel Phytases from Bifidobacterium pseudocatenulatum ATCC 27919 and Bifidobacterium longum subsp. infantis ATCC 15697

“…S2). In bifidobacteria, orthologues of PhypA and PhylA were found only in the genomes of B. longum, B. pseudocatenulatum, and Bifidobacterium dentium isolates (58 to 82% amino acid identity), which correlated with the results for previous enzymatic tests (6,11,12).The PhypA and PhylA genes were amplified by PCR excluding the sequences encoding the N-terminal signal peptides (48 amino acids for PhypA and 31 amino acids for PhylA) and the C-terminal hydrophobic domains (deletion of the 27 and 24 C-terminal amino acids in PhypA and PhylA, respectively) and cloned into the expression vector pQE80 (Qiagen) for their purification as 6ϫHis-tagged proteins (see Fig. S3 and Table S1 in the supplemental material).…”

“…hytases are a special class of phosphatases that catalyze the sequential hydrolysis of myo-inositol hexakis phosphate (InsP 6 ) or phytate, the major form of phosphorous storage in plants, to lower myo-inositol phosphate derivatives. Based on biochemical properties and amino acid sequence, phytases can be categorized into two major classes, the histidine acid phytases and the alkaline phytases (9).…”

“…Based on biochemical properties and amino acid sequence, phytases can be categorized into two major classes, the histidine acid phytases and the alkaline phytases (9). The use of commercial phytases of fungal origin (usually Trichoderma and Aspergillus strains) is a common practice in animal feeding for improving the bioaccessibility of minerals (zinc, iron, calcium, and magnesium) that are otherwise chelated by InsP 6 and InsP 5 and insolubilized (4,13). The presence of phytase activity has recently been reported to occur in the human intestinal Bifidobacterium pseudocatenulatum ATCC 27919 and Bifidobacterium longum subsp.…”

Phytate Solubilizing Microorganisms and Enzyme Phytase to Combat Nutritional Problems in Cereal-Based Foods

“…In vitro experiments found Bifidobacteria as a good phytase producer. Enriching infant foods with fructo-oligoseccharides (FOS) as prebiotic and with selected bacterium strain as probiotics would be a good supplement in phytate rich food [24]. Phytase produced in the digestive tract can be very efficient in degrading phytate and improve availability of plant phosphorus to ruminants as demonstrated by Rodehutscord [25].…”

“…The phytase enzyme produced by bacteria and yeasts are extracellular as well as intracellular, however extracellular are more appropriate [26]. The ability to degrade phytate by five different strains of Bifidobacterial species (Bifidobacterium animalis, B. bifidum, B. infantis, B. longum and B. pseudocatenulatum) isolated from the intestinal tract was evaluated by Haros et al [24]. These organisms exhibited good solubilizing capacity under in vivo conditions [27].…”