Effect of citrate on Aspergillus niger phytase adsorption and catalytic activity in soil

Mezeli, Malika M.; George, Timothy S.; Giles, Courtney D.; Neilson, Roy; Haygarth, P. M.

doi:10.1016/j.geoderma.2017.06.015

Cited by 13 publications

(9 citation statements)

References 55 publications

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“…At pH 7.5, repulsive forces between the negatively charged protein and soil surface lead to greater amounts and activities of the enzyme in solution , meaning that phyA should be soluble and available in the transgenic rhizosphere at pH 6.5. However, the pH optima of A. niger phyA activity in solution occurs at approximately pH 2.5 and 5.0 Sariyska et al 2005) and can decrease by more than 60% above pH 6 (Mezeli et al 2015;Naves et al 2012). Naves et al…”

Section: Discussionmentioning

confidence: 99%

Linking the depletion of rhizosphere phosphorus to the heterologous expression of a fungal phytase in Nicotiana tabacum as revealed by enzyme-labile P and solution 31P NMR spectroscopy

et al. 2017

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Root exudation of phytase could improve the ability of plants to access organic forms of soil phosphorus (P), thereby minimizing fertilizer requirements and improving P use efficiency in agroecosystems. After 75 days growth in a high available P soil, shoot biomass and P accumulation, soil pH, and rhizosphere P depletion were investigated in Nicotiana tabacum wild-type and transgenic plant-lines expressing and exuding Aspergillus niger phytase (ex::phyA), or a null-vector control. Solution 31 P NMR analysis revealed a 7% to 11% increase in orthophosphate and a comparable depletion of undefined monoester P compounds (-13 to-18%) in the rhizosphere of tobacco plants relative to the unplanted soil control. Wild-type plants had the greatest impact on the composition of rhizosphere P based on the depletion of other monoester P, polyphosphate, and phosphonate species. The depletion of phytase-labile P by ex::phyA plants was associated with decreased proportions of other monoester P, rather than myo-InsP6 as expected. Rhizosphere pH increased from 6.0 to 6.5-6.7 in transgenic plant soils, beyond the pH optimum for A. niger phyA activity (pH=5), and may explain the limited specificity of ex::phyA plants for phytate in this soil. The efficacy of single exudation traits (e.g., phytase) therefore appear to be limited in P-replete soil conditions and may be improved where soil pH matches the functional requirements of the enzyme or trait of interest.

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Section: Discussionmentioning

confidence: 99%

Linking the depletion of rhizosphere phosphorus to the heterologous expression of a fungal phytase in Nicotiana tabacum as revealed by enzyme-labile P and solution 31P NMR spectroscopy

et al. 2017

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“…Optimization of pH depicted that fungal strain (UJIIB-29) producing phytase grow at slightly acidic pH 5.5 (23.75±0.02 U/mL/min). The comparison of research and results of Qasim et al (2017), using Aspergillus tubingensis SKA (pH 5) and Mezeli et al (2017) who obtained maximum activity at pH 4.5-5.5 by Aspergillus niger showed that strains were isolated from acidic environment that is why they gave optimal results at acidic pH.…”

Section: Phmentioning

confidence: 98%

Biosynthesis, purification, kinetic and thermodynamic analysis of phytase from Aspergillus oryzae

Haq¹,

Javed²,

Nawaz³

et al. 2020

Rev.Mex.Ing.Quim.

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“…There is a tradeoff between phytase retention to the soil matrix and phytase activity, whose outcome would determine the real contribution of the enzyme to soil P availability. A low retention of phytases implies more enzyme in the soil solution and eventually a faster release of soil organic P. On the other side, phytases in soil solution could be denatured by soil microorganisms (Yang and Chen, 2017), whereas retained phytases would be released gradually, providing additional available P at later stages (Mezeli et al, 2017). 180…”

Section: Phytase Adsorption On Soilsmentioning

confidence: 99%

Adsorption to soils and biochemical characterization of purified phytases

Caffaro¹,

Balestrasse²,

Rubio³

2019

Preprint

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Abstract. Four purified phytases isolated from Aspergillus niger and Escherichia coli were characterized biochemically and in terms of their adsorption to soils belonging to the Mollisol order. Three different organic P substrates were used to measure enzyme activity in a wide range of pH (2.3 to 9) and temperatures (−10° to 70 °C): p-nitrophenyl-phosphate, glyceraldehyde-3-phosphate and phytic acid. Phytases from A. niger showed a higher capacity to release P (36 to 50 % of P contained in the substrates, 44 to 62 μg P), than phytases from E. coli (24 to 36 %, 20 to 44 μg P). The amount of P released from organic P substrates by A. niger phytases followed the following range: p-nitrophenyl-phosphate > glyceraldehyde-3-phosphate > phytic acid whereas in E. coli phytases the order was p-nitrophenyl-phosphate/glyceraldehyde-3-phosphate > phytic acid. All phytases were active throughout the pH and temperature ranges for optimum crop production. The proportion of phytases found in the solid phase of the soil 60 minutes after addition was lower than that found in the liquid phase (23–34 % vs. 66–77 %). Obtained results are promising in terms of the use of phytases as a complement to P fertilization in agricultural settings and encourages further studies under field conditions.

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Effect of citrate on Aspergillus niger phytase adsorption and catalytic activity in soil

Cited by 13 publications

References 55 publications

Linking the depletion of rhizosphere phosphorus to the heterologous expression of a fungal phytase in Nicotiana tabacum as revealed by enzyme-labile P and solution 31P NMR spectroscopy

Linking the depletion of rhizosphere phosphorus to the heterologous expression of a fungal phytase in Nicotiana tabacum as revealed by enzyme-labile P and solution 31P NMR spectroscopy

Biosynthesis, purification, kinetic and thermodynamic analysis of phytase from Aspergillus oryzae

Adsorption to soils and biochemical characterization of purified phytases

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