Phytase: The Feed Enzyme, an Overview

Singh, Namita; Kuhar, Sonia; Priya, Kanu; Jaryal, Rajneesh; Yadav, Rakesh

doi:10.1007/978-981-10-4702-2_17

Cited by 12 publications

(11 citation statements)

References 250 publications

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“…While the activity of non-phytase phosphomonoesterase in roots of wetland plants was similar to that of phosphodiesterase (Rejmánková et al, 2011), it should be noted that the activity of phosphodiesterases can be easily overestimated by the presence of phosphomonoesterases when using artificial substrate for enzyme activity determinations (Sirová et al, 2013). With a few exceptions, microbes produce only intracellular phytases (Singh et al, 2018). Nevertheless, addition of phytase producing bacteria to model systems, i.e., plants grown on agar with an organic P source, was shown to strongly increase P availability from phytate for plants (Richardson et al, 2000).…”

Section: Enzyme-limited Hydrolysis Of Phytate and Phosphodiesters In mentioning

confidence: 81%

Is the enzymatic hydrolysis of soil organic phosphorus compounds limited by enzyme or substrate availability?

Jarosch

Kandeler

Frossard

et al. 2019

Soil Biology and Biochemistry

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Section: Enzyme-limited Hydrolysis Of Phytate and Phosphodiesters In mentioning

confidence: 81%

Is the enzymatic hydrolysis of soil organic phosphorus compounds limited by enzyme or substrate availability?

Jarosch

Kandeler

Frossard

et al. 2019

Soil Biology and Biochemistry

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“…Due to the enormous potential for application of phytase in the animal feed industry, several researchers have attempted to produce this enzyme cost-effectively. A. niger phyA phytase has been cloned and over expressed in several microbial hosts, including S. cerevisiae (Han et al, 1999), P. pastoris (Han and Lei, 1999), A. niger (Van Dijck, 1999) and E. coli (Singh et al, 2018). The pET prokaryotic expression system is one of the most effective expression systems, possesses high performance and specific interaction between bacteriophage T7 promoter and T7 RNA polymerase to increase the expression efficacy of exogenous gene in bacteria.…”

Section: Discussionmentioning

confidence: 99%

Cloning of phytase gene from Aspergillus niger 563 and its expression in E.coli system

Geetha¹,

Kumar²,

Arul³

et al. 2023

IJEAB

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A phyA was cloned from Aspergillus niger by reverse transcription polymerase chain reaction. The amplified 1404 bp fragment was cloned in a T/A cloning vector and confirmed by sequencing. The isolated phytase gene showed 99.0 % sequence identity at nucleotide and protein level with Aspergillus niger CBS 513.88 phytase. The amino acid sequence from the phyA cDNA contained the consensus motifs, RHGXRXP and HD which are conserved among histidine acid phosphatases. The phytase cDNA was subcloned in pET28a(+) expression vector and expressed in E. coli. The expression of the gene was confirmed through SDS-PAGE analysis. A 52 kDa protein as per the calculated molecular mass of the translational product of phytase gene was observed in crude lysate of E. coli culture induced with IPTG. The protein was purified using nickel based His-bind resin column and checked on SDS-PAGE. The purified recombinant enzyme showed a single band of 52 kDa protein. The phytase activity of pET-phyA IPTG induced E. coli culture and purified phytase was 383.5 U/ml and 826.33 U/ml, respectively.

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“…In plants, phytase may be found in higher concentrations in wheat, barley, and peas, while lower content in soybeans, maize, spinach, and so on. Phytase in the plant was first discovered in rice bran, which formed several phosphatidyl inositols as an intermediate or final product ( Secco et al, 2017 ; Kumar and Sinha, 2018 ; Singh N. et al, 2018 ). Plant phytases can be MINPPs, PAPhys, or, in rare situations, HAPs, which are more similar to fungus HAPs than MINPPs.…”

Section: Source Of Phytasementioning

confidence: 99%

Insight into phytase-producing microorganisms for phytate solubilization and soil sustainability

et al. 2023

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The increasing demand for food has increased dependence on chemical fertilizers that promote rapid growth and yield as well as produce toxicity and negatively affect nutritional value. Therefore, researchers are focusing on alternatives that are safe for consumption, non-toxic, cost-effective production process, and high yielding, and that require readily available substrates for mass production. The potential industrial applications of microbial enzymes have grown significantly and are still rising in the 21st century to fulfill the needs of a population that is expanding quickly and to deal with the depletion of natural resources. Due to the high demand for such enzymes, phytases have undergone extensive research to lower the amount of phytate in human food and animal feed. They constitute efficient enzymatic groups that can solubilize phytate and thus provide plants with an enriched environment. Phytases can be extracted from a variety of sources such as plants, animals, and microorganisms. Compared to plant and animal-based phytases, microbial phytases have been identified as competent, stable, and promising bioinoculants. Many reports suggest that microbial phytase can undergo mass production procedures with the use of readily available substrates. Phytases neither involve the use of any toxic chemicals during the extraction nor release any such chemicals; thus, they qualify as bioinoculants and support soil sustainability. In addition, phytase genes are now inserted into new plants/crops to enhance transgenic plants reducing the need for supplemental inorganic phosphates and phosphate accumulation in the environment. The current review covers the significance of phytase in the agriculture system, emphasizing its source, action mechanism, and vast applications.

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Phytase: The Feed Enzyme, an Overview

Cited by 12 publications

References 250 publications

Is the enzymatic hydrolysis of soil organic phosphorus compounds limited by enzyme or substrate availability?

Is the enzymatic hydrolysis of soil organic phosphorus compounds limited by enzyme or substrate availability?

Cloning of phytase gene from Aspergillus niger 563 and its expression in E.coli system

Insight into phytase-producing microorganisms for phytate solubilization and soil sustainability

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