Production of D-myo-inositol(1,2,4,5,6)pentakisphosphate using alginate-entrapped recombinant Pantoea agglomerans glucose-1-phosphatase

Greiner, Ralf; Sajidan,

doi:10.1590/s1516-89132008000200002

Cited by 12 publications

(3 citation statements)

References 24 publications

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“…Only trace levels of activity were observed below pH 3.0 and above pH 8.0. The acidic pH optimum also confirms that the purified enzyme belongs to the histidine acid phosphatase family, as most HAP phytases have pH optima ranging from 4.0 to 5.5 (44)(45)(46)(47).…”

Section: Sequence Analysis Of the Agpp Proteinsupporting

confidence: 56%

Novel Glucose-1-Phosphatase with High Phytase Activity and Unusual Metal Ion Activation from Soil Bacterium Pantoea sp. Strain 3.5.1

Suleimanova

Beinhauer

Valeeva

et al. 2015

Appl Environ Microbiol

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Phosphorus is an important macronutrient, but its availability in soil is limited. Many soil microorganisms improve the bioavailability of phosphate by releasing it from various organic compounds, including phytate. To investigate the diversity of phytate-hydrolyzing bacteria in soil, we sampled soils of various ecological habitats, including forest, private homesteads, large agricultural complexes, and urban landscapes. Bacterial isolate Pantoea sp. strain 3.5.1 with the highest level of phytase activity was isolated from forest soil and investigated further. The Pantoea sp. 3.5.1 agpP gene encoding a novel glucose-1-phosphatase with high phytase activity was identified, and the corresponding protein was purified to apparent homogeneity, sequenced by mass spectroscopy, and biochemically characterized. The AgpP enzyme exhibits maximum activity and stability at pH 4.5 and at 37°C. The enzyme belongs to a group of histidine acid phosphatases and has the lowest K m values toward phytate, glucose-6-phosphate, and glucose-1-phosphate. Unexpectedly, stimulation of enzymatic activity by several divalent metal ions was observed for the AgpP enzyme. High-performance liquid chromatography (HPLC) and high-performance ion chromatography (HPIC) analyses of phytate hydrolysis products identify DL-myo-inositol 1,2,4,5,6-pentakisphosphate as the final product of the reaction, indicating that the Pantoea sp. AgpP glucose-1-phosphatase can be classified as a 3-phytase. The identification of the Pantoea sp. AgpP phytase and its unusual regulation by metal ions highlight the remarkable diversity of phosphorus metabolism regulation in soil bacteria. Furthermore, our data indicate that natural forest soils harbor rich reservoirs of novel phytate-hydrolyzing enzymes with unique biochemical features. P hosphorus is one of the most important macroelements of living cells. It is a crucial component of nucleic acids, highenergy compounds, phospholipids, and other molecules and is essential for normal plant growth. Many soil types are naturally low in inorganic phosphorus, and, as the pressure on agriculture to provide food for the growing human population intensifies, so does the need for a massive use of phosphate fertilizers. However, rock phosphate is a nonrenewable natural resource (1). Furthermore, the vast majority of applied phosphate fertilizer quickly interacts with soil components, leading to its rapid transformation into various organic or precipitated compounds inaccessible to plants. Thus, much attention has recently been paid to alternative sources of phosphorus in soil.Organic phosphorus compounds in soil account for 30 to 50% of total soil phosphorus and are often considered natural alternatives to the use of mineral phosphate fertilizer (2). Phytate is a molecule of myo-inositol with six phosphate residues (3). Phytate concentration varies from 3.9% to 25.3% of total extractable P in carbonate-free cambisol soils and calcareous chernozems, respectively (4), suggesting that in some cases phytate can be one of the major for...

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Section: Sequence Analysis Of the Agpp Proteinsupporting

confidence: 56%

Novel Glucose-1-Phosphatase with High Phytase Activity and Unusual Metal Ion Activation from Soil Bacterium Pantoea sp. Strain 3.5.1

Suleimanova

Beinhauer

Valeeva

et al. 2015

Appl Environ Microbiol

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“…It was previously reported that the purified Pantoea agglomerans phytase was entrapped in alginate beads with an efficiency of approximately 80%. [18] Aspergillus ficuum phytase was covalently immobilized onto cross-linked agarose by 55% efficiency. [39] Saccharomyces cerevisiae CY cells immobilized in calcium alginate beads were used for the degradation of phytate.…”

Section: Resistance Of Immobilized Enzymes To Proteolysismentioning

confidence: 99%

“…These problems have been overcome by immobilization of phytases on a variety of matrices. [18] Immobilized enzymes have some advantages. They have high stability than free enzymes and can be easily separated from the reaction mixture.…”

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confidence: 99%

Dephytinization of food stuffs by phytase of Geobacillus sp. TF16 immobilized in chitosan and calcium-alginate

Şirin

Akatin

Çolak

et al. 2017

International Journal of Food Properties

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In this work, Geobacillus sp. TF16 phytase was separately immobilized in chitosan and Ca-alginate with the efficiency of 38% and 42%, respectively. These enzymes exhibited broad substrate specificity. Maximal relative phytase activity was measured at pH 5.0 and 95°C and pH 3.0 and 75°C for chitosan and Ca-alginate, respectively. The enzymes were highly stable in a wide pH and temperature range. Values of K m and V max were determined as 2.38 mM and 3401.36 U/mg protein for chitosan, and 7.5 mM and 5011.12 U/mg protein for Ca-alginate. The immobilized enzymes showed higher resistance to proteolysis. After 4 h incubation, hydrolysis capacities of chitosan-and Ca-alginate immobilized enzymes for soymilk phytate were calculated as 24% and 33%, respectively. The chitosan-and Ca-alginate immobilized phytases conserved its original activity after 8 and 6 cycles of reuse, respectively. The features of the enzymes were very attractive and they might be useful for some industrial applications.

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New Age Agricultural Bioinputs

Mohite

Koli

Borase

et al. 2019

Microbial Interventions in Agriculture and Environment

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Production of D-myo-inositol(1,2,4,5,6)pentakisphosphate using alginate-entrapped recombinant Pantoea agglomerans glucose-1-phosphatase

Abstract: The glucose-1-phosphatase encoding gene (agp) -myo-inositol(1,2,4,5,6)pentakisphosphate, was shown to be feasible by using the enzyme-loaded alginate beads in batch operations. The entrapped enzyme showed a high operational stability by retaining almost full activity even after ten uses.

Cited by 12 publications

References 24 publications

Novel Glucose-1-Phosphatase with High Phytase Activity and Unusual Metal Ion Activation from Soil Bacterium Pantoea sp. Strain 3.5.1

Novel Glucose-1-Phosphatase with High Phytase Activity and Unusual Metal Ion Activation from Soil Bacterium Pantoea sp. Strain 3.5.1

Dephytinization of food stuffs by phytase of Geobacillus sp. TF16 immobilized in chitosan and calcium-alginate

New Age Agricultural Bioinputs

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