Journal articles: 'Myo-inositol hexakisphosphate (phytate)'

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Greiner, Ralf, and Nils-Gunnar Carlsson. "myo-Inositol phosphate isomers generated by the action of a phytate-degrading enzyme from Klebsiella terrigena on phytate." Canadian Journal of Microbiology 52, no. 8 (August 1, 2006): 759–68. http://dx.doi.org/10.1139/w06-028.

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For the first time a dual pathway for dephosphorylation of myo-inositol hexakisphosphate by a histidine acid phytase was established. The phytate-degrading enzyme of Klebsiella terrigena degrades myo-inositol hexakisphosphate by stepwise dephosphorylation, preferably via D-Ins(1,2,4,5,6)P5, D-Ins(1,2,5,6)P4, D-Ins(1,2,6)P3, D-Ins(1,2)P2 and alternatively via D-Ins(1,2,4,5,6)P5, Ins(2,4,5,6)P4, D-Ins(2,4,5)P3, D-Ins(2,4)P2 to finally Ins(2)P. It was estimated that more than 98% of phytate hydrolysis occurs via D-Ins(1,2,4,5,6)P5. Therefore, the phytate-degrading enzyme from K. terrigena has to be considered a 3-phytase (EC 3.1.3.8). A second dual pathway of minor importance could be proposed that is in accordance with the results obtained by analysis of the dephosphorylation products formed by the action of the phytate-degrading enzyme of K. terrigena on myo-inositol hexakisphosphate. It proceeds preferably via D-Ins(1,2,3,5,6)P5, D-Ins(1,2,3,6)P4, Ins(1,2,3)P3, D-Ins(2,3)P2 and alternatively via D-Ins(1,2,3,5,6)P5, D-Ins(2,3,5,6)P4, D-Ins(2,3,5)P3, D-Ins(2,3)P2 to finally Ins(2)P. D-Ins(2,3,5,6)P4, D-Ins(2,3,5)P3, and D-Ins(2,4)P2 were reported for the first time as intermediates of enzymatic phytate dephosphorylation. A role of the phytate-degrading enzyme from K. terrigena in phytate breakdown could not be ruled out. Because of its cytoplasmatic localization and the suggestions for substrate recognition, D-Ins(1,3,4,5,6)P5 might be the natural substrate of this enzyme and, therefore, may play a role in microbial pathogenesis or cellular myo-inositol phosphate metabolism.Key words: myo-inositol phosphate isomers, phytate-degrading enzyme, phytate, phytase, Klebsiella terrigena.

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Greiner, Ralf, Adelazim Farouk, Marie Larsson Alminger, and Nils-Gunnar Carlsson. "The pathway of dephosphorylation of myo-inositol hexakisphosphate by phytate-degrading enzymes of different Bacillus spp." Canadian Journal of Microbiology 48, no. 11 (November 1, 2002): 986–94. http://dx.doi.org/10.1139/w02-097.

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The pathway of dephosphorylation of myo-inositol hexakisphosphate by the phytate-degrading enzymes of Bacillus subtilis 168, Bacillus amyloliquefaciens ATCC 15841, and Bacillus amyloliquefaciens 45 was established using a combination of high-performance ion chromatography analysis and kinetic studies. The data demonstrate that all the Bacillus phytate-degrading enzymes under investigation dephosphorylate myo-inositol hexakisphosphate by sequential removal of phosphate groups via two independent routes; the routes proceed via D-Ins(1,2,4,5,6)P5 to Ins(2,4,5,6)P4 to finally Ins(2,4,6)P3 or D-Ins(2,5,6)P3 and via D-Ins(1,2,4,5,6)P5 to D-Ins(1,2,5,6)P4 to finally D-Ins(1,2,6)P3. The resulting myo-inositol trisphosphate D-Ins(1,2,6)P3 was degraded via D-Ins(2,6)P2 to finally Ins(2)P after prolonged incubation times in combination with increased enzyme concentration. Key words: Bacillus spp., myo-inositol phosphate isomers, phytase, phytate degradation.

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Lassen, Søren F., Jens Breinholt, Peter R. Østergaard, Roland Brugger, Andrea Bischoff, Markus Wyss, and Claus C. Fuglsang. "Expression, Gene Cloning, and Characterization of Five Novel Phytases from Four Basidiomycete Fungi: Peniophora lycii, Agrocybe pediades, a Ceriporia sp., and Trametes pubescens." Applied and Environmental Microbiology 67, no. 10 (October 1, 2001): 4701–7. http://dx.doi.org/10.1128/aem.67.10.4701-4707.2001.

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ABSTRACT Phytases catalyze the hydrolysis of phosphomonoester bonds of phytate (myo-inositol hexakisphosphate), thereby creating lower forms of myo-inositol phosphates and inorganic phosphate. In this study, cDNA expression libraries were constructed from four basidiomycete fungi (Peniophora lycii, Agrocybe pediades, a Ceriporia sp., and Trametes pubescens) and screened for phytase activity in yeast. One full-length phytase-encoding cDNA was isolated from each library, except for the Ceriporia sp. library where two different phytase-encoding cDNAs were found. All five phytases were expressed inAspergillus oryzae, purified, and characterized. The phytases revealed temperature optima between 40 and 60°C and pH optima at 5.0 to 6.0, except for the P. lycii phytase, which has a pH optimum at 4.0 to 5.0. They exhibited specific activities in the range of 400 to 1,200 U · mg, of protein−1 and were capable of hydrolyzing phytate down tomyo-inositol monophosphate. Surprisingly, 1H nuclear magnetic resonance analysis of the hydrolysis of phytate by all five basidiomycete phytases showed a preference for initial attack at the 6-phosphate group of phytic acid, a characteristic that was believed so far not to be seen with fungal phytases. Accordingly, the basidiomycete phytases described here should be grouped as 6-phytases (EC 3.1.3.26 ).

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Greiner, Ralf, Boon L. Lim, Chiwai Cheng, and Nils-Gunnar Carlsson. "Pathway of phytate dephosphorylation by β-propeller phytases of different origins." Canadian Journal of Microbiology 53, no. 4 (April 2007): 488–95. http://dx.doi.org/10.1139/w07-015.

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Using a combination of high-performance ion chromatography analysis and kinetic studies, the pathway of myo-inositol hexakisphosphate dephosphorylation by the β-propeller phytase of Shewanella oneidensis was established, which was then compared with that of Bacillus subtilis 168, Bacillus amyloliquefaciens ATCC 15841, and B. amyloliquefaciens 45 β-propeller phytases. The data demonstrate that all of these β-propeller phytases dephosphorylate myo-inositol hexakisphosphate in a stereospecific way by sequential removal of phosphate groups via d-Ins(1,2,4,5,6)P5, Ins(2,4,5,6)P4 to finally Ins(2,4,6)P3. Thus, the β-propeller phytases prefer the hydrolysis of every second phosphate over that of adjacent ones. This finding does not support previous phytate degradation models proposed by J. Kerovuo, J. Rouvinen, and F. Hatzack (2000. Biochem. J. 352: 623–628) and R. Greiner, A. Farouk, M. Larsson Alminger, and N.G. Carlsson (2002. Can. J. Microbiol. 48: 986–994) , but seems to fit with the structural model given by S. Shin, N.C. Ha, B.C. Oh, T.K. Oh, and B.H. Oh (2001. Structure, 9: 851–858) .

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Quiñone, D., N. Veiga, J. Torres, J. Castiglioni, C. Bazzicalupi, A. Bianchi, and C. Kremer. "Synthesis, solid-state characterization and solution studies of new phytate compounds with Cu(ii) and 1,10-phenanthroline: progress in the structural elucidation of phytate coordinating ability." Dalton Transactions 45, no. 30 (2016): 12156–66. http://dx.doi.org/10.1039/c6dt01460g.

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Torres, Julia, Claudia Giorgi, Nicolás Veiga, Carlos Kremer, and Antonio Bianchi. "Interaction of myo-inositol hexakisphosphate with biogenic and synthetic polyamines." Organic & Biomolecular Chemistry 13, no. 27 (2015): 7500–7512. http://dx.doi.org/10.1039/c5ob00900f.

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Lee, Minji, Jong Hun Moon, Eun Jin Jun, Gyoungmi Kim, Yong-Uk Kwon, Jin Yong Lee, and Juyoung Yoon. "A tetranaphthoimidazolium receptor as a fluorescent chemosensor for phytate." Chem. Commun. 50, no. 44 (2014): 5851–53. http://dx.doi.org/10.1039/c4cc02036g.

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Laboure, A. M., J. Gagnon, and A. M. Lescure. "Purification and characterization of a phytase (myo-inositol-hexakisphosphate phosphohydrolase) accumulated in maize (Zea mays) seedlings during germination." Biochemical Journal 295, no. 2 (October 15, 1993): 413–19. http://dx.doi.org/10.1042/bj2950413.

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Phytase (myo-inositol-hexakisphosphate phosphohydrolase, EC 3.1.3.8) has been purified from 5-7-day-old maize (Zea mays) seedlings, using a four-step purification procedure. The native protein has a molecular mass of about 76 kDa and is built up from two 38 kDa subunits. The pH and temperature optima of the purified enzyme were respectively 4.8 and 55 degrees C. The apparent Km for phytate was estimated to be 117 microM. Like other acidic phytases, the maize seedling enzyme exhibited a broad affinity for various phosphorylated substrates and especially for penta- and tri-phosphate esters of myo-inositol. The amino acid composition of the h.p.l.c.-purified protein indicated a high hydrophobicity (44% non-polar amino acids). Rabbit antibodies were produced in response to maize seedling phytase. Western-blot analyses clearly demonstrate that the increase of phytase activity observed during the first 7 days of germination corresponded to an accumulation of the protein in maize seedlings. Phytase accumulated essentially in the shoots (mesocotyl plus coleoptiles.

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Axambayeva, Altynay Seitkhanovna, and Alexander Vyacheslavovich Shustov. "RECOMBINANT THERMOTOLERANT PHYTASE PRODUCED IN E.COLI." CBU International Conference Proceedings 3 (September 19, 2015): 412–18. http://dx.doi.org/10.12955/cbup.v3.631.

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Abstract: Phytic acid (myo-inositol hexakisphosphate) and its salts (phytates) are the major storage form of phosphorus in plants. Monogastric animals including hogs, poultry, and fish cannot utilize phytates as a source of phosphorus unless they are enzymatically destroyed with exogenous enzyme—phytase. Phytases are added to fodder in ever increasing dosage to improve utilization of plant-derived phosphorus because this reduces dependence of farms on inorganic fodder phosphates. Because of technological considerations, feed phytases have to withstand elevated temperatures (60-80°C), which are used during preparation of fodder. Enzymatic feed additives are becominutesg of high demand in Kazakhstan, and development of domestic technologies for production of agricultural enzymes is an ongoing challenge to the country’s biotechnology.Objectives: To develop a system for recombinant expression of industrially important thermotolerantphytase and confirm activity and thermal stability of the recombinantly expressed enzyme.Methods: De novo gene synthesis, expression of 6xHis-tagged protein in E.coli, immobilized metal affinity chouromatography, biochemical tests for activities of phosphatase and phytase.Results: Thermotolerantphytase was produced in E.coli using recombinant expression system. The obtained enzyme had phosphatise activity (hydrolyzed p-nitrophenyl phosphate) and phytase activity (hydrolyzed sodium phytate). The recombinant phytase tolerated increase of incubation temperature up to 70°C and demonstrated increase in activity towards phytate with increase in the reaction temperature in the range 30°C-70°C.Conclusion: Described gene and expression system have prospects of utilization in development of pilot industrial production of phytase in the country.

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Grases, Felix. "Phytate (Myo-inositol hexakisphosphate) inhibits cardiovascular calcifications in rats." Frontiers in Bioscience 11, no. 1 (2006): 136. http://dx.doi.org/10.2741/1786.

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Cottrill, Michael A., Serguei P. Golovan, John P. Phillips, and Cecil W. Forsberg. "Inositol phosphatase activity of theEscherichia coli agp-encoded acid glucose-1-phosphatase." Canadian Journal of Microbiology 48, no. 9 (September 1, 2002): 801–9. http://dx.doi.org/10.1139/w02-076.

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When screening an Escherichia coli gene library for myo-inositol hexakisphosphate (InsP6) phosphatases (phytases), we discovered that the agp-encoded acid glucose-1-phosphatase also possesses this activity. Purified Agp hydrolyzes glucose-1-phosphate, p-nitrophenyl phosphate, and InsP6with pH optima, 6.5, 3.5, and 4.5, respectively, and was stable when incubated at pH values ranging from 3 to 10. Glucose-1-phosphate was hydrolyzed most efficiently at 55°C, while InsP6and p-nitrophenyl phosphate were hydrolyzed maximally at 60°C. The Agp exhibited Kmvalues of 0.39 mM, 13 mM, and 0.54 mM for the hydrolysis of glucose-1-phosphate, p-nitrophenyl phosphate, and InsP6, respectively. High-pressure liquid chromatography (HPLC) analysis of inositol phosphate hydrolysis products of Agp demonstrated that the enzyme catalyzes the hydrolysis of phosphate from each of InsP6, D-Ins(1,2,3,4,5)P5, Ins(1,3,4,5,6)P5, and Ins(1,2,3,4,6)P5, producing D/L-Ins(1,2,4,5,6)P5, D-Ins(1,2,4,5)P4, D/L-Ins(1,4,5,6)P4and D/L-Ins(1,2,4,6)P4, respectively. These data support the contention that Agp is a 3-phosphatase. Key words: phosphatase, phytate, bacteria, inositol phosphate, phytase.

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Zamudio, Marcela, Aracely González, and Fernando Bastarrachea. "Regulation ofRaoultella terrigenacomb.nov. phytase expression." Canadian Journal of Microbiology 48, no. 1 (January 1, 2002): 71–81. http://dx.doi.org/10.1139/w01-134.

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Phytases catalyze the release of phosphate from phytate (myo-inositol hexakisphosphate) to inositol polyphosphates. Raoultella terrigena comb.nov. phytase activity is known to increase markedly after cells reach the stationary phase. In this study, phytase activity measurements made on single batch cultures indicated that specific enzyme activity was subject to catabolite repression. Cyclic AMP (cAMP) showed a positive effect in expression during exponential growth and a negative effect during stationary phase. RpoS exhibited the opposite effect during both growth phases; the induction to stationary phase decreased twofold in the rpoS::Tn10 mutant, but the effect of RpoS was not clearly determined. Two phy::MudI1734 mutants, MW49 and MW52, were isolated. These formed small colonies in comparison with the MW25 parent strain when plated on Luria-Bertani (LB) or LB supplemented with glucose. They did not grow in minimal media or under anaerobiosis, but did grow aerobically on LB and LB glucose at a lower rate than did MW25. The β-galactosidase activity level in these mutants increased three to four fold during stationary growth in LB glucose and during anaerobiosis. Addition of cAMP during the exponential growth of MW52 on LB glucose provoked a decrease in β-galactosidase activity during the stationary phase, confirming its negative effect on phytase expression during stationary growth.Key words: phytase activity, expression regulation, Raoultella terrigena.

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Greiner, Ralf. "Degradation of myo-inositol Hexakisphosphate by a Phytate-degrading Enzyme from Pantoea agglomerans." Protein Journal 23, no. 8 (November 2004): 577–85. http://dx.doi.org/10.1007/s10930-004-7884-0.

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Hanke, David E., Paroo N. Parmar, Samuel E. K. Caddick, Porntip Green, and Charles A. Brearley. "Synthesis of inositol phosphate ligands of plant hormone–receptor complexes: pathways of inositol hexakisphosphate turnover." Biochemical Journal 444, no. 3 (May 29, 2012): 601–9. http://dx.doi.org/10.1042/bj20111811.

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Reduction of phytate is a major goal of plant breeding programs to improve the nutritional quality of crops. Remarkably, except for the storage organs of crops such as barley, maize and soybean, we know little of the stereoisomeric composition of inositol phosphates in plant tissues. To investigate the metabolic origins of higher inositol phosphates in photosynthetic tissues, we have radiolabelled leaf tissue of Solanum tuberosum with myo-[2-3H]inositol, undertaken a detailed analysis of inositol phosphate stereoisomerism and permeabilized mesophyll protoplasts in media containing inositol phosphates. We describe the inositol phosphate composition of leaf tissue and identify pathways of inositol phosphate metabolism that we reveal to be common to other kingdoms. Our results identify the metabolic origins of a number of higher inositol phosphates including ones that are precursors of cofactors, or cofactors of plant hormone–receptor complexes. The present study affords alternative explanations of the effects of disruption of inositol phosphate metabolism reported in other species, and identifies different inositol phosphates from that described in photosynthetic tissue of the monocot Spirodela polyrhiza. We define the pathways of inositol hexakisphosphate turnover and shed light on the occurrence of a number of inositol phosphates identified in animals, for which metabolic origins have not been defined.

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Hardy, Rachael, Yueming Dersjant-Li, Trine Christensen, Deepak Velayudhan, and Janet C. Remus. "115 Functionality of a novel consensus bacterial 6-phytase variant on ileal phytate degradation in weaned piglets fed diets without inorganic phosphate." Journal of Animal Science 98, Supplement_4 (November 3, 2020): 104–5. http://dx.doi.org/10.1093/jas/skaa278.191.

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Abstract Microbial phytases are used in animal feed to hydrolyze phytic acid (myo-inositol hexakisphosphate, IP6) and phytate (salt of phytic acid), to improve phosphorus (P) bioavailability. This study evaluated the efficacy of a novel consensus bacterial 6-phytase variant (PhyG) on ileal IP6 degradation in piglets. A positive control diet was formulated based on corn and soybean meal with adequate digestible P (2.9g/kg) and calcium (Ca, 7.0g/kg). A negative control (NC) diet was formulated without inorganic P (1.1 g digestible P/kg), reduced in Ca (5.0 g/kg) with analyzed phytate P of 2.6g/kg. This diet was supplemented with PhyG at 250, 500 and 1,000 FTU/kg. A total of 90 crossed Pietrain x (large White x Landrace) 21-d-old piglets were fed adaptation diets until 42 d old and then assigned to pens (2 pigs/pen and 9 pens/treatment) in a completely randomized block design. Piglets were fed mash diets ad libitum for 28 d, at the end of the study 1 piglet/pen was euthanized for collecting ileal digesta samples for determination of IP6 digestibility, using TiO2 as a marker. Data was analyzed by one-way ANOVA using JMP 14.0 with treatment comparison by Tukey test and dose response by curve fitting. The ileal IP6 content was reduced with increasing phytase dose in a dose dependent manner (Plinear < 0.0001; Pexponential = 0.08). Similarly, the ileal IP6 digestibility increased exponentially (P < 0.05) with increasing phytase dose (49.1% for NC and 89.3% for PhyG at 1,000 FTU/kg). Improved ileal IP6 digestibility is closely related to improved bone ash, body weight gain and feed conversion ratio (R2 > 0.91). The in vitro IP6 degradation profile supports these in vivo observations. The results demonstrated that the novel consensus phytase variant is highly efficient in hydrolyzing phytate and increasing the bio-availability of phytate bound P in piglets fed diets without inorganic phosphate.

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Greiner, Ralf, Nils-Gunnar Carlsson, and Marie Larsson Alminger. "Stereospecificity of myo-inositol hexakisphosphate dephosphorylation by a phytate-degrading enzyme of Escherichia coli." Journal of Biotechnology 84, no. 1 (November 2000): 53–62. http://dx.doi.org/10.1016/s0168-1656(00)00331-x.

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TANG, HUACHENG, DONGJIE ZHANG, CHANGYUAN WANG, and ZHIJIANG LI. "Optimization of Myo-inositol hexakisphosphate phosphohydrolase (MIPH) production and enhancement of hydrocarbons degradation by purified MIPH." Romanian Biotechnological Letters 26, no. 1 (January 1, 2021): 2236–43. http://dx.doi.org/10.25083/rbl/26.1/2236.2243.

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Objective: The present study characterizes bacteria with biodegradation ability and optimize the growth conditions of Myo-inositol hexakisphosphate phosphohydrolase (MIPH). Methods: Out of the 15 bacterial isolates, one strain SM01 showed the highest MIPH activity was selected based on the diameter of halo zone formation on calcium phytate plates. SM01 strain was identified as a Serratia marcescens with the highest phytate activity which was further confirmed by partial sequencing of the 16S rRNA gene. Results: MIPH enzyme was purified from Serratia strain which was found to exhibit a highly-specific MIPH activity and high specificity to the phytic acid but negligible activity against the other substrates tested. The purified MIPH enzyme had an isoelectric point of 6.8 and Molecular weight to 60 kDa. The degradative ability of Serratia marscescens shown that both the culture and the purified enzyme had maximum MIPH activity at the 36 h of incubation. 0.5 U/ml concentration of the purified MIPH enzyme was found to show similar activity as the 108 cfu/ml culture tested. Conclusion: Serratia marcescens SM01 strain was capable of degrading hydrocarbons due to their varied strategies to produce the MIPH enzyme. This could be made useful in the biodegradation of polluted soils and the environment.

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Pujol, Antelm, Pilar Sanchis, Felix Grases, and Luis Masmiquel. "Phytate Intake, Health and Disease: “Let Thy Food Be Thy Medicine and Medicine Be Thy Food”." Antioxidants 12, no. 1 (January 7, 2023): 146. http://dx.doi.org/10.3390/antiox12010146.

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Phytate (myo-inositol hexakisphosphate or InsP6) is the main phosphorus reservoir that is present in almost all wholegrains, legumes, and oilseeds. It is a major component of the Mediterranean and Dietary Approaches to Stop Hypertension (DASH) diets. Phytate is recognized as a nutraceutical and is classified by the Food and Drug Administration (FDA) as Generally Recognized As Safe (GRAS). Phytate has been shown to be effective in treating or preventing certain diseases. Phytate has been shown to inhibit calcium salt crystallization and, therefore, to reduce vascular calcifications, calcium renal calculi and soft tissue calcifications. Moreover, the adsorption of phytate to the crystal faces can inhibit hydroxyapatite dissolution and bone resorption, thereby playing a role in the treatment/prevention of bone mass loss. Phytate has a potent antioxidation and anti-inflammatory action. It is capable of inhibiting lipid peroxidation through iron chelation, reducing iron-related free radical generation. As this has the effect of mitigating neuronal damage and loss, phytate shows promise in the treatment/prevention of neurodegenerative disease. It is reported that phytate improves lipid and carbohydrate metabolism, increases adiponectin, decreases leptin and reduces protein glycation, which is linked with macrovascular and microvascular diabetes complications. In this review, we summarize the benefits of phytate intake as seen in in vitro, animal model, epidemiological and clinical trials, and we also identify questions to answer in the future.

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Grases, F., J. Perelló, B. Isern, and R. M. Prieto. "Determination of myo-inositol hexakisphosphate (phytate) in urine by inductively coupled plasma atomic emission spectrometry." Analytica Chimica Acta 510, no. 1 (May 2004): 41–43. http://dx.doi.org/10.1016/j.aca.2003.12.061.

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Yan, Yupeng, Biao Wan, Yanyi Zhang, Limei Zhang, Fan Liu, and Xionghan Feng. "In situ ATR-FTIR spectroscopic study of the co-adsorption of myo-inositol hexakisphosphate and Zn(II) on goethite." Soil Research 56, no. 5 (2018): 526. http://dx.doi.org/10.1071/sr17333.

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The coexistence of myo-inositol hexakisphosphate (IHP; phytate) and aqueous Zn(II) may affect the adsorbed amounts and speciation of each other on minerals, which can further influence the transport and fate of IHP and Zn(II) in soils and sediments. The objective of this study was to investigate the co-adsorption mechanism of IHP and Zn(II) on goethite (Gt). A combination of macroscopic experiments and in situ attenuated total reflectance Fourier transform infrared spectroscopy (ATR-FTIR) was used to investigate the co-adsorption of IHP and Zn(II) at the Gt–water interface in the pH range of 3.0–7.0. Adsorption experiments showed that the presence of IHP promoted Zn(II) adsorption, and vice versa, on the surface of Gt. The ATR-FTIR spectra of IHP adsorbed on Gt in the presence of Zn(II) differed from the spectra of IHP adsorbed without co-adsorbed Zn(II) and of zinc phytate (Zn-IHP) precipitates, suggesting that the formation of Gt–IHP–Zn ternary surface complexes was the most likely mechanism for the co-adsorption of IHP and Zn(II) on Gt. The results show that the coexistence of IHP and Zn(II) may have altered both the extent and mechanism of IHP and metal adsorption on Gt, with respect to binary Gt–IHP and Gt–Zn(II) systems. These findings indicate that the coexistence of IHP and heavy metals significantly affects the adsorbed amounts and speciation of these compounds in the natural environment, where the aqueous concentrations of reactants are below saturation with respect to metal phytate precipitates.

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Raghavendra, P., T. Rao, and P. Halami. "Evaluation of beneficial attributes for phytate-degrading Pediococcus pentosaceus CFR R123." Beneficial Microbes 1, no. 3 (September 1, 2010): 259–64. http://dx.doi.org/10.3920/bm2009.0042.

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In this study we have screened and selected potent phytate-degrading lactic acid bacteria (LAB), and evaluated their beneficial attributes. Around 60 LAB strains were isolated from several cereal- and pulse-based conventional fermented preparations. They were screened for their ability to degrade myo-inositol hexakisphosphate (IP6) by cobalt chloride qualitative staining method (plate assay). One of the cultures, Pediococcus pentosaceus CFR R123, was capable of degrading both calcium and sodium salts of phytic acid. Additionally, we have carried out an in vitro evaluation for the beneficial attributes of phytate degrading CFR R123. P. pentosaceus CFR R123 showed 53% survivability at pH 2 and 62% at pH 2.5, whereas cultures of Lactobacillus rhamnosus GG showed a survivability of 55% and 82%, respectively. CFR R123 could also withstand 0.3% ox-bile, whereas no growth was observed for GG. The strain CFR R123 exhibited 62.8% hydrophobicity to xylene whereas 59% was found for GG. Both the tested strains showed a good spectrum of antibacterial activity against food-borne pathogens like Escherichia coli, Listeria monocytogenes Scott A, etc. P. pentosaceus CFR R123 possessed β-galactosidase activity and cholesterol reduction ability. In conclusion, LAB with phytate degrading ability and several beneficial attributes could potentially be used as a starter culture to improve the nutritional security of functional food.

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Dersjant-Li, Yueming, Roger Davin, Trine Christensen, and Cees Kwakernaak. "Effect of two phytases at two doses on performance and phytate degradation in broilers during 1–21 days of age." PLOS ONE 16, no. 3 (March 25, 2021): e0247420. http://dx.doi.org/10.1371/journal.pone.0247420.

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The effect of two microbial phytases at two dose-levels on performance and apparent ileal digestibility (AID) of nutrients in broilers fed European-type diets was studied. A total of 1,200 d-old Ross 308 male broilers were randomly assigned to 5 treatments with 30 birds/pen and 8 pens/treatment. A nutritionally adequate positive control (PC) diet was tested against 4 experimental diets containing reduced total P, retainable P, Ca and Na as per the recommended nutritional contribution for Buttiauxella phytase (Phy B) at 1,000 FTU/kg (-1.87 g/kg, -1.59 g/kg, -1.99 g/kg and -0.4 g/kg vs. PC, respectively). Experimental diets were supplemented with Phy B at 500 FTU/kg or 1,000 FTU/kg, or Citrobacter phytase (Phy C) at 1,000 FTU/kg or 2,000 FTU/kg. Diets were based on corn, soybean meal, rapeseed meal and sunflower meal and formulated by phase (starter 1–10 d, grower 11–21 d) in crumbled or pelleted form. Overall (d 1–21), at 1,000 FTU/kg, birds fed Phy C exhibited lower BWG (-2.7%), FI (-3.4%) and tibia ash (-2.2%) vs. PC (P < 0.05), and reduced BWG (-3.6%), FI (-3.9%) and tibia ash (-1.8%) vs. Phy B (P < 0.05). Phy B at 1,000 FTU/kg and Phy C at 2,000 FTU/kg maintained performance equivalent to the PC. Digestibility of Ca did not differ among phytase treatments but at 1,000 FTU/kg AID P was greater with Phy B than Phy C (72.3% vs. 62.7%, P < 0.05). Ileal phytate (myo-inositol hexakisphosphate, IP6) digestibility was greatest with Phy B at 1,000 FTU/kg which was higher than Phy C at 1,000 FTU/kg (87.6 vs. 60.6%, P < 0.05). The findings indicate a higher phytate degradation rate of Phy B than Phy C at equivalent dose-level and this is correlated to the performance of the broilers.

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Grases, Felix,. "Absorption of myo-inositol hexakisphosphate (InsP6) through the skin: study of the matrix effects. mechanism of phytate topical absorption." Frontiers in Bioscience 10, no. 1-3 (2005): 799. http://dx.doi.org/10.2741/1573.

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Makarewicz, Oliwia, Sarah Dubrac, Tarek Msadek, and Rainer Borriss. "Dual Role of the PhoP∼P Response Regulator: Bacillus amyloliquefaciens FZB45 Phytase Gene Transcription Is Directed by Positive and Negative Interactions with the phyC Promoter." Journal of Bacteriology 188, no. 19 (October 1, 2006): 6953–65. http://dx.doi.org/10.1128/jb.00681-06.

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ABSTRACT Several Bacillus strains secrete phytase, an enzyme catalyzing dephosphorylation of myo-inositol hexakisphosphate (phytate). We identified the phyC (phytase) gene from environmental Bacillus amyloliquefaciens FZB45 as a member of the phosphate starvation-inducible PhoPR regulon. In vivo and in vitro assays revealed that PhoP∼P is essential for phyC transcription. The transcriptional start site was identified downstream of a σA-like promoter region located 27 bp upstream of the probable translation ATG start codon. Inspection of the phyC promoter sequence revealed an unusual structure. The− 35 and −10 regions are separated by a window of 21 bp. A pair of tandemly repeated PhoP TT(T/A/C)ACA binding boxes was located within and upstream of the −35 consensus promoter region. A single PhoP box was found within the −10 consensus promoter region. DNase I footprinting experiments performed with isolated PhoP confirmed that PhoP∼P binds at two sites overlapping with the phyC −35 and −10 consensus promoter region. While binding of dimeric PhoP∼P at −35 is essential for activation of the phyC promoter, binding of PhoP∼P at− 10 suppresses promoter activity. A sixfold enhancement of phyC gene expression was registered after T:G substitution of nucleotide −13 (mutant MUT13), which eliminates PhoP binding at the single PhoP box without impairing the −10 consensus sequence. Moreover, MUT13 also expressed phyC during phosphate-replete growth, suggesting that the repressing effect due to binding of PhoP∼P at −10 was abolished. A model is presented in which transcription initiation of phyC is positively and negatively affected by the actual concentration of the PhoP∼P response regulator.

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Wyss, Markus, Roland Brugger, Alexandra Kronenberger, Roland Rémy, Rachel Fimbel, Gottfried Oesterhelt, Martin Lehmann, and Adolphus P. G. M. van Loon. "Biochemical Characterization of Fungal Phytases (myo-Inositol Hexakisphosphate Phosphohydrolases): Catalytic Properties." Applied and Environmental Microbiology 65, no. 2 (February 1, 1999): 367–73. http://dx.doi.org/10.1128/aem.65.2.367-373.1999.

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ABSTRACT Supplementation with phytase is an effective way to increase the availability of phosphorus in seed-based animal feed. The biochemical characteristics of an ideal phytase for this application are still largely unknown. To extend the biochemical characterization of wild-type phytases, the catalytic properties of a series of fungal phytases, as well as Escherichia coli phytase, were determined. The specific activities of the fungal phytases at 37°C ranged from 23 to 196 U · (mg of protein)−1, and the pH optima ranged from 2.5 to 7.0. When excess phytase was used, all of the phytases were able to release five phosphate groups of phytic acid (myo-inositol hexakisphosphate), which leftmyo-inositol 2-monophosphate as the end product. A combination consisting of a phytase and Aspergillus nigerpH 2.5 acid phosphatase was able to liberate all six phosphate groups. When substrate specificity was examined, the A. niger,Aspergillus terreus, and E. coli phytases were rather specific for phytic acid. On the other hand, theAspergillus fumigatus, Emericella nidulans, andMyceliophthora thermophila phytases exhibited considerable activity with a broad range of phosphate compounds, including phenyl phosphate, p-nitrophenyl phosphate, sugar phosphates, α- and β-glycerophosphates, phosphoenolpyruvate, 3-phosphoglycerate, ADP, and ATP. Both phosphate liberation kinetics and a time course experiment in which high-performance liquid chromatography separation of the degradation intermediates was used showed that all of themyo-inositol phosphates from the hexakisphosphate to the bisphosphate were efficiently cleaved by A. fumigatusphytase. In contrast, phosphate liberation by A. niger orA. terreus phytase decreased with incubation time, and themyo-inositol tris- and bisphosphates accumulated, suggesting that these compounds are worse substrates than phytic acid is. To test whether broad substrate specificity may be advantageous for feed application, phosphate liberation kinetics were studied in vitro by using feed suspensions supplemented with 250 or 500 U of eitherA. fumigatus phytase or A. niger phytase (Natuphos) per kg of feed. Initially, phosphate liberation was linear and identical for the two phytases, but considerably more phosphate was liberated by the A. fumigatus phytase than by the A. niger phytase at later stages of incubation.

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KEROVUO, Janne, Juha ROUVINEN, and Frank HATZACK. "Analysis of myo-inositol hexakisphosphate hydrolysis by Bacillus phytase: indication of a novel reaction mechanism." Biochemical Journal 352, no. 3 (December 8, 2000): 623–28. http://dx.doi.org/10.1042/bj3520623.

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Phytic acid (myo-inositol hexakisphosphate, InsP6) hydrolysis by Bacillus phytase (PhyC) was studied. The enzyme hydrolyses only three phosphates from phytic acid. Moreover, the enzyme seems to prefer the hydrolysis of every second phosphate over that of adjacent ones. Furthermore, it is very likely that the enzyme has two alternative pathways for the hydrolysis of phytic acid, resulting in two different myo-inositol trisphosphate end products: Ins(2,4,6)P3 and Ins(1,3,5)P3. These results, together with inhibition studies with fluoride, vanadate, substrate and a substrate analogue, indicate a reaction mechanism different from that of other phytases. By combining the data presented in this study with (1) structural information obtained from the crystal structure of Bacillus amyloliquefaciens phytase [Ha, Oh, Shin, Kim, Oh, Kim, Choi and Oh (2000) Nat. Struct. Biol. 7, 147Ő153], and (2) computer-modelling analyses of enzymeŐsubstrate complexes, a novel mode of phytic acid hydrolysis is proposed.

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Wyss, Markus, Luis Pasamontes, Arno Friedlein, Roland Rémy, Michel Tessier, Alexandra Kronenberger, Anke Middendorf, et al. "Biophysical Characterization of Fungal Phytases (myo-Inositol Hexakisphosphate Phosphohydrolases): Molecular Size, Glycosylation Pattern, and Engineering of Proteolytic Resistance." Applied and Environmental Microbiology 65, no. 2 (February 1, 1999): 359–66. http://dx.doi.org/10.1128/aem.65.2.359-366.1999.

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ABSTRACT Phytases (myo-inositol hexakisphosphate phosphohydrolases) are found naturally in plants and microorganisms, particularly fungi. Interest in these enzymes has been stimulated by the fact that phytase supplements increase the availability of phosphorus in pig and poultry feed and thereby reduce environmental pollution due to excess phosphate excretion in areas where there is intensive livestock production. The wild-type phytases from six different fungi, Aspergillus niger, Aspergillus terreus, Aspergillus fumigatus, Emericella nidulans, Myceliophthora thermophila, andTalaromyces thermophilus, were overexpressed in either filamentous fungi or yeasts and purified, and their biophysical properties were compared with those of a phytase from Escherichia coli. All of the phytases examined are monomeric proteins. WhileE. coli phytase is a nonglycosylated enzyme, the glycosylation patterns of the fungal phytases proved to be highly variable, differing for individual phytases, for a given phytase produced in different expression systems, and for individual batches of a given phytase produced in a particular expression system. Whereas the extents of glycosylation were moderate when the fungal phytases were expressed in filamentous fungi, they were excessive when the phytases were expressed in yeasts. However, the different extents of glycosylation had no effect on the specific activity, the thermostability, or the refolding properties of individual phytases. When expressed in A. niger, several fungal phytases were susceptible to limited proteolysis by proteases present in the culture supernatant. N-terminal sequencing of the fragments revealed that cleavage invariably occurred at exposed loops on the surface of the molecule. Site-directed mutagenesis of A. fumigatus andE. nidulans phytases at the cleavage sites yielded mutants that were considerably more resistant to proteolytic attack. Therefore, engineering of exposed surface loops may be a strategy for improving phytase stability during feed processing and in the digestive tract.

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Greiner, R., K. D. Jany, and M. Larsson Alminger. "Identification and Properties of myo -Inositol Hexakisphosphate Phosphohydrolases (Phytases) from Barley (Hordeum vulgare)." Journal of Cereal Science 31, no. 2 (March 2000): 127–39. http://dx.doi.org/10.1006/jcrs.1999.0254.

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Borlini, Giulia, Cesare Rovera, Michela Landoni, Elena Cassani, and Roberto Pilu. "lpa1-5525: A New lpa1 Mutant Isolated in a Mutagenized Population by a Novel Non-Disrupting Screening Method." Plants 8, no. 7 (July 6, 2019): 209. http://dx.doi.org/10.3390/plants8070209.

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Phytic acid, or myo-inositol 1,2,3,4,5,6-hexakisphosphate, is the main storage form of phosphorus in plants. It is localized in seeds, deposited as mixed salts of mineral cations in protein storage vacuoles; during germination, it is hydrolyzed by phytases to make available P together with all the other cations needed for seed germination. When seeds are used as food or feed, phytic acid and the bound cations are poorly bioavailable for human and monogastric livestock due to their lack of phytase activity. Therefore, reducing the amount of phytic acid is one strategy in breeding programs aimed to improve the nutritional properties of major crops. In this work, we present data on the isolation of a new maize (Zea mays L.) low phytic acid 1 (lpa1) mutant allele obtained by transposon tagging mutagenesis with the Ac element. We describe the generation of the mutagenized population and the screening to isolate new lpa1 mutants. In particular, we developed a fast, cheap and non-disrupting screening method based on the different density of lpa1 seed compared to the wild type. This assay allowed the isolation of the lpa1-5525 mutant characterized by a new mutation in the lpa1 locus associated with a lower amount of phytic phosphorus in the seeds in comparison with the wild type.

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30

KEROVUO, Janne, Juha ROUVINEN, and Frank HATZACK. "Analysis of myo-inositol hexakisphosphate hydrolysis by Bacillus phytase: indication of a novel reaction mechanism." Biochemical Journal 352, no. 3 (December 15, 2000): 623. http://dx.doi.org/10.1042/0264-6021:3520623.

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31

Ragon, Mélanie, André Aumelas, Patrick Chemardin, Santiago Galvez, Guy Moulin, and Hélène Boze. "Complete hydrolysis of myo-inositol hexakisphosphate by a novel phytase from Debaryomyces castellii CBS 2923." Applied Microbiology and Biotechnology 78, no. 1 (February 2008): 47–53. http://dx.doi.org/10.1007/s00253-007-1275-3.

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von Sperber, C., F. Tamburini, B. Brunner, S. M. Bernasconi, and E. Frossard. "The oxygen isotope composition of phosphate released from phytic acid by the activity of wheat and <i>Aspergillus niger</i> phytase." Biogeosciences 12, no. 13 (July 14, 2015): 4175–84. http://dx.doi.org/10.5194/bg-12-4175-2015.

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Abstract. Phosphorus (P) is an essential nutrient for living organisms. Under P-limiting conditions plants and microorganisms can exude extracellular phosphatases that release inorganic phosphate (Pi) from organic phosphorus compounds (Porg). Phytic acid (myo-inositol hexakisphosphate, IP6) is an important form of Porg in many soils. The enzymatic hydrolysis of IP6 by phytase yields available Pi and less phosphorylated inositol derivates as products. The hydrolysis of organic P compounds by phosphatases leaves an isotopic imprint on the oxygen isotope composition (δ18O) of released Pi, which might be used to trace P in the environment. This study aims at determining the effect of phytase on the oxygen isotope composition of released Pi. For this purpose, enzymatic assays with histidine acid phytases from wheat and Aspergillus niger were prepared using IP6, adenosine 5'-monophosphate (AMP) and glycerophosphate (GPO4) as substrates. For a comparison to the δ18O of Pi released by other extracellular enzymes, enzymatic assays with acid phosphatases from potato and wheat germ with IP6 as a substrate were prepared. During the hydrolysis of IP6 by phytase, four of the six Pi were released, and one oxygen atom from water was incorporated into each Pi. This incorporation of oxygen from water into Pi was subject to an apparent inverse isotopic fractionation (&varepsilon; ~ 6 to 10 ‰), which was similar to that imparted by acid phosphatase from potato during the hydrolysis of IP6 (&varepsilon; ~ 7 ‰), where less than three Pi were released. The incorporation of oxygen from water into Pi during the hydrolysis of AMP and GPO4 by phytase yielded a normal isotopic fractionation (&varepsilon; ~ −12 ‰), similar to values reported for acid phosphatases from potato and wheat germ. We attribute this similarity in &varepsilon; to the same amino acid sequence motif (RHGXRXP) at the active site of these enzymes, which leads to similar reaction mechanisms. We suggest that the striking substrate dependency of the isotopic fractionation could be attributed to a difference in the δ18O values of the C–O–P bridging and non-bridging oxygen atoms in organic phosphate compounds.

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Davin, R., C. Kwakernaak, and Y. Dersjant-Li. "Effect of two commercial limestone sources with different solubility on the efficacy of two phytases in 0-21 d old broilers." Journal of Applied Animal Nutrition 8, no. 2 (August 21, 2020): 61–73. http://dx.doi.org/10.3920/jaan2020.0003.

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A study evaluated the effects of limestone sources with different solubility on the efficacy of two phytases in broilers. A 2×5 factorial arrangement was employed with two commercial limestone sources and five diet treatments; a positive control (PC) diet with 7.2 g/kg P and 9.6 g/kg Ca, and a negative control diet containing reductions of 1.87 g/kg available P, 1.99 g/kg Ca and 0.4 g/kg Na, supplemented with either Buttiauxella phytase (PhyB) or Escherichia coli phytase (PhyE) at 500 or 1000 FTU/kg diet. The two limestone sources were feed-grade commercial products with different particle sizes and solubility (fast-soluble (FS) 100%; slow-soluble (SS) 26% soluble after 30 minutes at pH 3) containing similar levels of Ca. Diets were fed to one-day-old Ross 308 males (n=2,400) with 30 birds/pen and eight pens/treatment in two phases (starter 0-10 d and grower 10-21 d). On d 21, ileal digesta was collected from 12 birds/pen to determine apparent ileal digestibility (AID) of P and Ca, and myo-inositol hexakisphosphate (IP6) disappearance, and tibias from four birds/pen for ash determination. The SS limestone improved body weight gain (BWG), feed intake (FI) and FCR vs FS limestone in starter/grower phases (P<0.05), and improved AID of P (P<0.05) and IP6 disappearance (P<0.05) at d 21. There was an interaction between limestone and phytase on BWG, FI and FCR in the grower phase (P≤0.05) whereby FS (vs SS) limestone reduced BWG at either dose of PhyE, but only at 500 FTU/kg of PhyB. At an equivalent dose, PhyB had higher BWG and feed intake than PhyE (P<0.05). At 1000 FTU/kg, performance was equivalent (BWG and FI) or superior (FCR) to the PC, PhyB produced greater tibia ash, AID of P and IP6 disappearance (P<0.05). The findings showed that the effects of limestone particle size on phytase efficacy varied with phytase source and dose.

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Quan, Chunshan, Shengdi Fan, and Yoshiyuki Ohta. "Pathway of dephosphorylation of myo-inositol hexakisphosphate by a novel phytase from Candida krusei WZ-001." Journal of Bioscience and Bioengineering 95, no. 5 (January 2003): 530–33. http://dx.doi.org/10.1016/s1389-1723(03)80056-7.

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Heyer, Charlotte M. E., Li F. Wang, Eduardo Beltranena, Michael G. Gänzle, and Ruurd T. T. Zijlstra. "PSIV-B-28 Effect of feeding acidified or fermented barley grain using Limosilactobacillus reuteri with or without supplemental phytase on diet nutrient digestibility in growing pigs." Journal of Animal Science 99, Supplement_3 (October 8, 2021): 391–92. http://dx.doi.org/10.1093/jas/skab235.713.

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Abstract Fermentation of cereal grains may degrade myo-inositol hexakisphosphate (InsP6) thereby increasing nutrient digestibility. Effects of chemical acidification or fermentation with Limosilactobacillus (Lm.) reuteri TMW 1.656 with or without phytase on nutrient digestibility of diets composed of high β-glucan hull-less barley grain were assessed in growing pigs. Four mash diets contained 50% barley grain: 1) unfermented barley (Control); 2) chemically-acidified barley (ACD) with lactic and acidic acid [0.02 L/kg barley grain, 4:1 (v/v)]; 3) barley fermented with Lm. reuteri (Fermented without phytase); and 4) barley fermented with Lm. reuteri and phytase (Fermented with phytase; 500 FYT/kg barley grain). The 4 diets were fed to 8 ileal-cannulated barrows (initial BW, 17.4 kg) for four 11-d periods in a double 4 × 4 Latin square. The InsP6 content of barley grain in Control, ACD, Fermented without phytase, or Fermented with phytase was 1.12, 0.59, 0.52% dry matter, or not detectable, respectively. Diet apparent total tract digestibility (ATTD) of crude protein (CP), Ca, gross energy and digestible energy and predicted net energy values were greater (P < 0.05) for ACD and Fermented without phytase than Control. Diet apparent ileal digestibility (AID) of Ca and standardized total tract digestibility (STTD) of P tended to be greater (P < 0.10) for Fermented without phytase than Control. Diet STTD of P, AID and ATTD of Ca was greater (P < 0.05) for Fermented with phytase than Fermented without phytase. Acidification or fermentation with/without phytase did not affect diet standardized ileal digestibility of CP and AA. In conclusion, fermentation with phytase completely degraded InsP6 in barley grain and maximized P and Ca digestibility, thereby reducing the need to provide inorganic P to meet P requirements of growing pigs.

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McKie, Vincent A., and Barry V. McCleary. "A Novel and Rapid Colorimetric Method for Measuring Total Phosphorus and Phytic Acid in Foods and Animal Feeds." Journal of AOAC INTERNATIONAL 99, no. 3 (May 1, 2016): 738–43. http://dx.doi.org/10.5740/jaoacint.16-0029.

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Abstract Phytic acid, or myo-inositol hexakisphosphate, is the primary source of inositol and storage phosphorus in plant seeds and has considerable nutritional importance. In this form, phosphorus is unavailable for absorption by monogastric animals, and the strong chelating characteristic of phytic acid reduces the bioavailability of multivalent minerals such as iron, zinc, and calcium. Currently, there is no simple quantitative method for phytic acid; existing methods are complex, and the most commonly accepted method, AOAC Official MethodSM 986.11, has limitations. The aim of this work was to develop and validate a simple, high-throughput method for the measurement of total phosphorus and phytic acid in foods and animal feeds. The method described here involves acid extraction of phytic acid, followed by dephosphorylation with phytase and alkaline phosphatase. The phosphate released from phytic acid is measured using a modified colorimetric molybdenum blue assay and calculated as total phosphorus or phytic acid content of the original sample. The method was validated to a maximum linearity of 3.0 g phytic acid/100 g sample. Accuracy ranged from 98 to 105% using pure phytic acid and from 97 to 115% for spiked samples. Repeatability ranged from 0.81 to 2.32%, and intermediate precision was 2.27%.

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Vats, Purva, and U. C. Banerjee. "Biochemical characterisation of extracellular phytase (myo-inositol hexakisphosphate phosphohydrolase) from a hyper-producing strain of Aspergillus niger van Teighem." Journal of Industrial Microbiology & Biotechnology 32, no. 4 (March 18, 2005): 141–47. http://dx.doi.org/10.1007/s10295-005-0214-5.

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Grases, Félix, Joan Perelló, Bernat Isern, and Antonia Costa-Bauzá. "Myo-inositol hexakisphosphate (phytate) inhibits calcium carbonate crystallisation in hard water." Water SA 33, no. 5 (March 2, 2019). http://dx.doi.org/10.4314/wsa.v33i5.184098.

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Suryani, Ade Erma, AYU SEPTI ANGGRAENI, LUSTY ISTIQOMAH, EMA DAMAYANTI, and MOHAMMAD FAIZ KARIMY. "Isolation and identification of phytate-degrading yeast from traditional fermented food." Biodiversitas Journal of Biological Diversity 22, no. 2 (January 27, 2021). http://dx.doi.org/10.13057/biodiv/d220241.

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Abstract. Suryani AE, Anggraeni AS, Istiqomah L, Damayanti E, Karimy MF. 2021. Isolation and identification of phytate-degrading yeast from traditional fermented food. Biodiversitas 22: 866-873. Application of phytase (myo-inositol hexakisphosphate phosphohydrolase) to catalyze the release of phosphate from phytates contained on grain-based feed has been used widely in poultry feed industry. In this study, yeast as phytase producer from traditional fermented food was isolated, screened and identified their morphological, biochemical, and molecular characteristics. Production of extracellular phytase from yeast was quantified using spectrophotometer. The results showed that among 8 yeast isolates that had phytase activity, there were two isolates with the highest phytase activity and specific activity which were TKd3 isolate (6.57 U/mL and 54.230 U/mg) and GF1 (6.07 U/mL and 53.68 U/mg). Morphological identification using Scanning Electron Microscope revealed that TKd3 cells isolated from soybean tempeh had an elongated oval cell structure, whereas the GF1 isolated from fresh gatot had a rounder cell structure. TKd3 isolate with accession number MW131530 had homology with Candida tropicalis ATCC 750 28S rRNA with 99.83% similarity and GF1 isolate with accession number MW131531 had homology with Candida tropicalis ATCC 750 28S rRNA with 100% similarity. It could be concluded that C. tropicalis yeast from traditional fermented food produced the extracellular phytase for further use of phytase in poultry feed additive.

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Li, Qi, Xiaolei Yang, Jianhong Li, Mingyuan Li, Changning Li, and Tuo Yao. "In-depth characterization of phytase-producing plant growth promotion bacteria isolated in alpine grassland of Qinghai-Tibetan Plateau." Frontiers in Microbiology 13 (January 4, 2023). http://dx.doi.org/10.3389/fmicb.2022.1019383.

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The use of plant growth promoting bacteria (PGPB) express phytase (myo-inositol hexakisphosphate phosphohydrolase) capable of hydrolyzing inositol phosphate in soil was a sustainable approach to supply available phosphorus (P) to plants. A total of 73 bacterial isolates with extracellular phytase activity were selected from seven dominant grass species rhizosphere in alpine grassland of Qinghai-Tibetan Plateau. Then, the plant growth promoting (PGP) traits of candidate bacteria were screened by qualitative and quantitative methods, including organic/inorganic Phosphorus solubilization (P. solubilization), plant hormones (PHs) production, nitrogen fixation, 1-aminocyclopropane-1-carboxylic acid (ACC) deaminase activity and antimicrobial activity. Further experiment were conducted to test their growth promoting effect on Lolium perenne L. under P-limitation. Our results indicated that these bacteria as members of phyla Proteobacteria (90.41%) and Actinobacteria (9.59%) were related to 16 different genera. The isolates of Pseudomonas species showed the highest isolates number (36) and average values of phytase activity (0.267 ± 0.012 U mL–1), and showed a multiple of PGP traits, which was a great candidate for PGPBs. In addition, six strains were positive in phytase gene (β-propeller phytase, bpp) amplification, which significantly increased the shoot length, shoot/root fresh weight, root average diameter and root system phytase activity of Lolium perenne L. under P-limitation, and the expression of phytase gene (bppP) in root system were verified by qPCR. Finally, the PHY101 gene encoding phytase from Pseudomonas mandelii GS10-1 was cloned, sequenced, and recombinantly expressed in Escherichia coli. Biochemical characterization demonstrated that the recombinant phytase PHY101 revealed the highest activity at pH 6 and 40°C temperature. In particular, more than 60% of activity was retained at a low temperature of 15°C. This study demonstrates the opportunity for commercialization of the phytase-producing PGPB to developing localized microbial inoculants and engineering rhizobacteria for sustainable use in alpine grasslands.

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Journal articles on the topic 'Myo-inositol hexakisphosphate (phytate)'

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