Purification and characterisation of an extracellular phytase from Aspergillus niger 11T53A9

Greiner, Ralf; Silva, Lucineia Gomes da; Couri, Sônia

doi:10.1590/s1517-83822009000400010

Cited by 43 publications

(33 citation statements)

References 32 publications

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“…Nonetheless, the final products generated for this enzyme were identical to those of wheat phytase as I(2)P 1 and d/l-I(1)P 1 . Aspergillus niger phytase is considered a 3-phytase (Greiner et al, 2009). Therefore, the major IP 5 product d/l-I(1,2,4,5,6)P 5 should be d-I(1,2,4,5,6)P 5 , with the first dephosphorylation at the C-3 position (Fig.…”

Section: Major and Minor Pathways Of Phytate Degradationmentioning

confidence: 99%

“…9A). According to Greiner et al (2009), pure A. niger phytase is a rather specific phosphatase and degrades phytate stepwise via d-I(1,2,4,5,6)P 5 , d-I(1,2,5,6)P 4 , d-I(1,2,6)P 3 , d-I(1,2)P 2 , and finally to I(2)P 1 . One possible reason for the presence of three degradation pathways instead of one might be the fact that the A. niger phytase used in this study was a commercial enzyme and was used without purification.…”

Section: Major and Minor Pathways Of Phytate Degradationmentioning

confidence: 99%

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Phytate Degradation by Different Phosphohydrolase Enzymes: Contrasting Kinetics, Decay Rates, Pathways, and Isotope Effects

Sun

Alikhani

Massoudieh

et al. 2017

Soil Science Soc of Amer J

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Phytate (IP 6 ) is often the most common organic P compound particularly in agricultural soils. understanding the fate of inositol phosphate (IP x ) in the environment in terms of isomeric composition and concentration and assessing relative resistance to (or preference for) degradation is essential to estimate the potential role of IP x in generating inorganic P (P i ) as well as overall P cycling in the environment. In this study, we analyzed IP 6 degradation by four common phosphohydrolase enzymes (phytase from wheat [Triticum aestivum l.] and Aspergillus niger and acid phosphatase from wheat germ and potato [Solanum tuberosum l.]), with particular focus on degradation pathways, isomer kinetic decay rate, and isotope effects using a combination of high-performance ion chromatography, nuclear magnetic resonance, stable isotopes, and process-based modeling techniques. our results show that the degradation pathways are often distinct among enzymes. The process-based Bayesian inverse modeling was used to capture the trend and magnitude of the measured concentrations for each IP x isomer and to determine the decay constants. Furthermore, o isotope ratios (d 18 o P ) of released P i enabled the identification of isotopically identical phosphate moieties in phytate derived from natural sources. Distinctly different fractionation factors, degradation pathways, and kinetic decay rate coefficients among the enzymes studied could lead to potential discrimination and tracking of phytate sources and products as well as active enzymes present in the environment.Abbreviations: HPIC, high-performance ion chromatography; IP, inositol phosphate; NMR, nuclear magnetic resonance; P i , inorganic phosphorus; pNPP, para-nitrophenyl phosphate.I nositol phosphates are a group of organic P compounds widely present in the natural environment (Turner et al., 2002). Phytate (the salt of myo-inositol 1,2,3,4,5,6-hexakisphosphate or IP 6 ) is a P storage molecule in cereals and grains and represents between 60 and 80% of P in mature seeds (Raboy, 1997). Since it is reported that ?51 million tonnes of phytate is formed in commercially produced fruits and crop seeds every year (Lott et al., 2000), a good fraction of phytate in seeds and grains is released to the soil environment as plant residues and animal manures (Dao, 2007;Gerke, 2015). Phytate readily sorbs onto minerals or precipitates with soil cations and organic matter, and then accumulates to constitute an often dominant class of organic P (Celi and Barberis, 2007;Giles and Cade-Menun, 2014). Although sorption and precipitation immobilizes a large fraction of phytate in soil, there is a potential for its transfer to water bodies with soil particulates and colloids (Turner et al., 2002;Turner and Newman, 2005 Core Ideas• Phytate is degraded through distinct pathways for a particular enzyme.• oxygen isotope ratios of phosphate moieties in phytate are isotopically identical.• These findings bring new insights into tracking phytate sources in the environment.

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Section: Major and Minor Pathways Of Phytate Degradationmentioning

confidence: 99%

Section: Major and Minor Pathways Of Phytate Degradationmentioning

confidence: 99%

Phytate Degradation by Different Phosphohydrolase Enzymes: Contrasting Kinetics, Decay Rates, Pathways, and Isotope Effects

Sun

Alikhani

Massoudieh

et al. 2017

Soil Science Soc of Amer J

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“…We chose pH 5.0 for our standardized assay method as, in general, pH 5.0 is used in the literature for the assay of fungal phytases [27][28][29]. The enzymatic Studies Towards the Stabilisation of a Mushroom Phytase Produced by Submerged Cultivation reaction was started by adding 50 lL of enzyme solution to the assay mixture.…”

Section: Enzymatic Activitymentioning

confidence: 99%

“…It must me noted that the two formulations which presented the highest levels of residual enzyme activity were the formulation containing 1 % NaCl and 20 mM Naacetate and the formulation containing 100 mM Na-acetate. Sodium acetate 100 mM, as used in this work, is also the buffer concentration indicated by the phytase assay methodology [28,30,34] for crude extract preparation of a phytase from Aspergillus niger 11T53A9. The results in the present work corroborate those of Pica et al [35], who found that NaCl had a positive effect on c-glutamyltranspeptidase activity, increasing the activity by around 20 % compared with the absence of NaCl.…”

Section: Studies Of Liquid Formulation Of Phytase To Improve Stabilitmentioning

confidence: 99%

Studies Towards the Stabilisation of a Mushroom Phytase Produced by Submerged Cultivation

et al. 2015

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A novel phytase from Ganoderma australe G24 was produced by submerged cultivation and recovery. Liquid and solid forms of phytase were developed; both types of product were formulated using different additives. Ganoderma australe G24 phytase was very stable in liquid form with NaCl and sodium acetate buffer. Solid form products were obtained by spray-drying using different polymers to encapsulate the phytase and the capsules obtained were analyzed by electron microscopy. Micrographs confirmed micro and nanoparticles formed with maltodextrin (300 nm to 7-8 µm) without the presence of agglomerates. The use of maltodextrin for solid formulation of G. australe G24 phytase is recommended, and resulted in good stability after the drying process and during storage (shelf life). Kinetic models of phytase inactivation in the microencapsulated powders over time were proposed for the different stabilizing additives. Inactivation rate constants, half-lives and D values (decimal reduction time) were obtained. Phytase encapsulated with maltodextrin remained stable after 90 days, with k 0.0019 day(-1) and a half-life (t1/2) of 367.91 days(-1).

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“…KHU-10 (Choi et al 2001), 45 °C for that from Obesumbacterium proteus (Zinin et al, 2004). It was less than that reported as 55C of P. oxalicum (Lee et al 2007;Lee et al 2015), 58 °C of A. niger 11T53A9 (Greiner et al 2009), 60 °C of Bacillus licheniformis (Kumar et al 2014a). Phytase of A. fumigatus and A. niger NRRL 3135 (Howson and Davis 1983) exhibited optimum activity at 37 °C and 55 °C, respectively.…”

Section: +mentioning

confidence: 62%

Production and characterization of a neutral phytase of Penicillium oxalicum EUFR-3 isolated from Himalayan region

et al. 2017

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Abstract. Kaur R, Saxena A, Sangwan P, Yadav AN, Kumar V, Dhaliwal HC. 2017. Production and characterization of a neutral phytase of Penicillium oxalicum EUFR-3 isolated from Himalayan region. Nusantara Bioscience 9: 68-76. Micronutrient bioavailability from cereals is poor to monogastric animals due to presence of phytate as a chelating agent in seeds and an exogenous application of phytases is required to overcome antinutritional effect of phytate. In the present investigation, 40 fungal isolates including Aspergillus, Penicillium, Trichoderma, Toliposporium, Cladosporium, Talaromyces etc. from different habitats were screened positive for phytase activity on specific media. On the basis of phytase production potential in solid state fermentation conditions, plant epiphytic fungi Penicillium oxalicum strain EUFR-3 has been observed with maximum phytase activity of 12.8 U/g. The biochemical properties i.e. activity and stability under optimum pH and temperature, and effect of modulators on phytase activity from this isolate were studied for its prospective application in human food. The P. oxalicum EUFR-3 phytase (PhyP-EUFR3) had maximum activity at pH 7.0 and temperature 40 °C. It was stable in pH range of 3-8 with more than 60 % activity throughout investigation. The thermostability of PhyP-EUFR3 was about 30 % residual activities after 10 min at 80 °C. Further purification, characterization and study of catalytic mechanism will be useful in better utilization of this phytase in human food for increased bioavailability of important metal ions.

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Purification and characterisation of an extracellular phytase from Aspergillus niger 11T53A9

Cited by 43 publications

References 32 publications

Phytate Degradation by Different Phosphohydrolase Enzymes: Contrasting Kinetics, Decay Rates, Pathways, and Isotope Effects

Phytate Degradation by Different Phosphohydrolase Enzymes: Contrasting Kinetics, Decay Rates, Pathways, and Isotope Effects

Studies Towards the Stabilisation of a Mushroom Phytase Produced by Submerged Cultivation

Production and characterization of a neutral phytase of Penicillium oxalicum EUFR-3 isolated from Himalayan region

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