A novel protein tyrosine phosphatase like phytase from Lactobacillus fermentum NKN51: Cloning, characterization and application in mineral release for food technology applications

Sharma, Rekha; Kumar, P. V. Hareesh; Kaushal, Vikas; Das, Rahul; Navani, Naveen Kumar

doi:10.1016/j.biortech.2017.10.106

Cited by 27 publications

(22 citation statements)

References 46 publications

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“…The phosphorus release from soybean meal after digestion of different amounts of r-Aophytase (0.5 U-2.5 U) was measured [26]. One gram of soybean meal was dispersed in 9 mL of 100 mM Tris-HCl (pH 7.5) in 50 mL centrifuge tubes, followed by incubation at 37 °C for 60 min in a shaker of 150 rpm.…”

Section: Hydrolysis Of Phytate Phosphorus In Soybean Meal With R-aophmentioning

confidence: 99%

“…The total amount of minerals was first determined according to the procedure as previously described [26]. One gram of durum wheat and finger millet flour was dispersed in 5 mL of ddH 2 O, and was incubated at 50 °C for 2 h, respectively.…”

Section: Mineral Release From Durum Wheat and Finger Millet Flourmentioning

confidence: 99%

“…The released minerals was then determined following the previous procedure [26]. One gram of durum wheat flour and finger millet flour was dispersed in 6 mL buffer (140 mM NaCl and 5 mM KCl), respectively.…”

Section: Mineral Release From Durum Wheat and Finger Millet Flourmentioning

confidence: 99%

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A novel fungal beta-propeller phytase from nematophagous Arthrobotrys oligospora: characterization and potential application in phosphorus and mineral release for feed processing

Hou

Shen

et al. 2020

Microb Cell Fact

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Phytases are widely utilized in feed industry to increase the utilization of phosphorus, minerals, and amino acids for improvement of animal and human nutrition. At present, all known β-propeller phytases (BPP) have been generated from bacteria, particularly Bacillus. In this work we report for the first time a new fungal-derived BPP phytase. We identified a phytase highly differentially expressed only in the parasitic stage of a nematophagous fungus, Arhtrobotrys oliogospora, during the development of the 3D traps. We found that this phytase was homologous to the known bacterial BPP phytase, thus we referred the new phytase to Aophytase. The heterologous expression of codon-optimized Aophytase gene in Pichia pastoris was successfully investigated to yield recombinant Aophytase (r-Aophytase) with high specific enzyme activity of 74.71 U/mg, much higher than those of recombinant BPP phytases derived bacteria. The kinetic parameters of the r-Aophytase, the optimum pH and temperature, as well as the effects of surfactant, EDTA and different ions on its enzyme activity were further investigated. The potential utilization of r-Aophytase in feed processing was finally explored. We found that the optimal pH value was about 7.5, and the optimal temperature was 50 °C.; r-Aophytase significantly increased the release of inorganic phosphorus from soybean meal, and improved the release of soluble minerals from the durum wheat flour and finger millet flour. The findings indicate its potential utilization in the feed processing to ameliorate nutritional value of cereals and animal feed in the future.

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Section: Hydrolysis Of Phytate Phosphorus In Soybean Meal With R-aophmentioning

confidence: 99%

Section: Mineral Release From Durum Wheat and Finger Millet Flourmentioning

confidence: 99%

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A novel fungal beta-propeller phytase from nematophagous Arthrobotrys oligospora: characterization and potential application in phosphorus and mineral release for feed processing

Hou

Shen

et al. 2020

Microb Cell Fact

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“…Nevertheless, microbial sources are more promising candidates for producing phytases in a commercial scale [14]. Phytase enzymes from intestinal microbes including bifidobacteria were studied; however, its industrial production is not economically profitable [5,15,16]. Nonetheless, phytases can be produced naturally by microbial strains such as Bacillus subtilis, B. amyloliquefaciens, Klebsiella aerogenes, K. pneumoniae; yeasts such as Saccharomyces cerevisiae, S. pastorianus, S. bayanus, and Pichia pastoris; and fungi such as Aspergillus niger, Fusarium verticillioides, and Penicillium griseoroseum.…”

Section: Introductionmentioning

confidence: 99%

“…Lactic acid fermentation modifies the physicochemical and functional composition of plant substrates by changing the ratio of antinutritive/nutritive components. In recent years, many phosphatases and phytases of LAB (L. fermentum [16]; L. sanfranciscensis [19]; L. pentosus [20,21]; L. coryniformis [22]) isolated from different sources, have been purified and characterized. In previous studies, LAB microbiota of grains and spontaneous sourdough of quinoa and amaranth was evaluated [23,24].…”

Section: Introductionmentioning

confidence: 99%

Partial characterization and purification of phytase from Lactobacillus plantarum CRL1964 isolated from pseudocereals

et al. 2020

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Cereals and pseudocereals are a rich source of nutrients and trace elements, but their dietary bioavailability is low due to the presence of phytate (IP6), an antinutritional compound with the ability to chelate cations and proteins. Phytase is an enzyme that catalyzes the hydrolysis of IP6 and it is used as an additive improving the nutritional quality of grain‐based foods. The aim of this study was to select lactic acid bacteria (LAB) isolated from pseudocereals with phytase activity, characterize their production and activity, and purify the enzyme. LAB strains isolated from grains and spontaneous sourdough of quinoa and amaranth were grown in the Man Rogosa and Sharpe medium where the inorganic phosphate (Pi) was replaced by 1% of IP6. Phytase activity was determined by measuring the Pi released from IP6. Phytase of Lactobacillus (L.) plantarum CRL1964 (PhyLP) showed the highest specific activity from 73 LAB evaluated. IP6 induces PhyLP production, which is at its maximum at the end of the exponential phase. PhyLP was thermostable and maintained its activity under acidic conditions. The enzymatic activity is stimulated by ethylenediaminetetraacetic acid, Co2+, and ascorbic acid. PhyLP was partially purified and showed a molecular mass of 55 kDa. L. plantarum CRL1964 and/or PhyLP have the potential to be included in the processing of cereal/pseudocereals based products for animal feed and/or the food industry improving its nutritional value.

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Unraveling the potential of bacterial phytases for sustainable management of phosphorous

Vashishth

Tehri

Tehri³

et al. 2023

Biotech and App Biochem

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Phosphorous actively participates in numerous metabolic and regulatory activities of almost all living organisms including animals and humans. Therefore, it is considered as an essential macronutrient required supporting their proper growth. On contrary, phytic acid (PA), an antinutritional substance, is widely known for its strong affinity to chelate essential mineral ions including PO43−, Ca2+, Fe2+, Mg2+, and Zn2+. Being one the major reservoir of PO43− ions, PA has great potential to bind PO43− ions in diverse range of foods. Once combined with P, PA transforms into an undigested and insoluble complex namely phytate. Produced phytate leads to a notable reduction in the bioavailability of P due to negligible activity of phytases in monogastric animals and humans. This highlights the importance and consequent need of enhancement of phytase level in these life forms. Interestingly, phytases, catalyzing the breakdown of phytate complex and recycling the phosphate into ecosystem to its available form, have naturally been reported in a variety of plants and microorganisms over past few decades. In pursuit of a reliable solution, the focus of this review is to explore the keynote potential of bacterial phytases for sustainable management of phosphorous via efficient utilization of soil phytate. The core of the review covers detailed discussion on bacterial phytases along with their widely reported applications viz. biofertilizers, phosphorus acquisition, and plant growth promotion. Moreover, meticulous description on fermentation‐based strategies and future trends on bacterial phytases have also been included.

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A novel protein tyrosine phosphatase like phytase from Lactobacillus fermentum NKN51: Cloning, characterization and application in mineral release for food technology applications

Cited by 27 publications

References 46 publications

A novel fungal beta-propeller phytase from nematophagous Arthrobotrys oligospora: characterization and potential application in phosphorus and mineral release for feed processing

A novel fungal beta-propeller phytase from nematophagous Arthrobotrys oligospora: characterization and potential application in phosphorus and mineral release for feed processing

Partial characterization and purification of phytase from Lactobacillus plantarum CRL1964 isolated from pseudocereals

Unraveling the potential of bacterial phytases for sustainable management of phosphorous

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