Phytic acid (myo-inositol 1,2,3,4,5,6-hexakis dihydrogen phosphate) and its mixed cationic salts, termed as phytate, are naturally found in plants and accumulates in seeds. When monogastric animals take such plants based food, tremendous amount of organic phosphorus is released through excreta, causing several environmental problems and economic losses. Phytases are enzymes that dephosphorylate the phytate (myo-inositol hexakisinositolphosphate to myo inositol) and release inorganic phosphate plus free inositol, makes phosphorus available for absorption. In recent years, microbial phytases are being applied to animal and human food stuffs to improve food processing and mineral bioavailability. For the production of phytases, variety of natural and recombinant expression systems employing bacteria, yeast and fungi are exploited to enhance the overall productivity. This paper summarizes the information on natural and genetically modified sources of phytases along with main focus on their relative productivity and their associated role towards removal of phosphorus from environment.
Keywords: Phytic acid; monogastric; dephosphorylate; phytase; expression systems; recombinant
How to cite: Batool, S., Sardar, F., 2017: Biotechnological production and applications of phytases for removal of phosphorus from environment. Bulletin of Environmental Studies 2(1): 24-36
Copyright © 2017 Batool, and Sardar. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
Edited by: Mariam Sabeeh, UET, Taxila, Pakistan
Reviewed by: Rizwan Ashraf (UAF, Faisalabad, Pakistan) & Sudibiyo bin Solikan (KFUPM, Saudi Arabia)
Published Online: 01/12/2017
Phytic acid and phytate are synthesized in plants and accumulated in ripening seeds. These are essential nutrient source of organic phosphorus in plants for proper growth. Natural phytases are present in plants to carry out the dephosphorylation of phytate complexes (Jorquera et al., 2008). Mono-gastric animals (e.g., pigs, poultry and fish) are unable to digest phytate because these animals lack the enzymes in gastrointestinal tract required for dephosphorylation of the phytate complex (Coffey and Cromwell, 1995) The phytate is an anti-nutrient which forms complex with a number of proteins and bivalent metallic cations, hence decreasing the availability of these nutrients in animals (Soetan and Oyewole, 2009).
Ultimately, phytate accumulates in animals manure which leads to phosphorus pollution in the environment. Plenty of phosphorus is released into the environment causing serious environmental issues, e.g., eutrophication and algal blooms in water bodies and consequential ecological problems (Olstorpe et al., 2009). Sustainable farming requires a reduction in the environmental burden caused by agricultural practices. Animals generate manure in large quantity, particularly phosphorus as major pollutant (Poutanen et al., 2009). Animal feed has to be supplemented with inorganic phosphate to meet the nutritional requirements (Greiner et al., 2013).
The enzyme industry today is the result of rapid development in the field of modern biotechnology (Beilen and Li, 2002). Since ancient times, naturally derived enzymes have been used for variety of purposes such as production of food products (e.g., cheese, wine, vinegar, beer, etc.), industrial products (e.g., manufacturing of leather, linen, etc.) and other items of household usage (Buchholz et al., 2012).
Recombinant DNA technology has further enabled the commercialization of these enzymes, playing a vital role in the improvement of overall yield (Lynd et al., 1999). This has been achieved by unraveling the effective catalytic properties of enzyme systems (Schallmey et al., 2004). In recent years, phytase industry has grown significantly due to its importance in food biotechnology. Phytases, a subclass of phosphatases, are phosphomonoesterase enzymes that accomplish the hydrolysis of phytate into inorganic orthiophosphate (Nielsen et al., 2008). Nomenclature committee of the international Union of Biochemistry and Molecular biology has recognized two types of phytases namely 3-phytase (E.C. 22.214.171.124) and 6-phytase (E.C. 126.96.36.199) (Dvořáková, 1998). The differentiation is devised on their mode of hydrolyzing the phytate as well as their occurrence.
Briefly, the 3-phytase attacks on phytate at the 3rd position of carbon, while 6-phytase targets the 6th position in the ring (Turner et al., 2001). Moreover, phytase 3 belongs to the animal kingdom while phytase 6 is originated from the plants. The catalysis results into dephosphorylation and therefore, releases inorganic phosphate and lower inositol phosphate esters (myo-inositol hexakisinositolphosphate to myo-inositol) (Figure 1).
Animal feed, with the addition of phytase, decreases the phosphorus load upto 50% in the environment and increases the availability of phosphorus for animal digestion (Simons et al., 1990; Lei et al., 1993; Qian et al., 1996; Vohra et al., 2006). The release of inorganic phosphate however depends on the enzyme activity (Buchholz et al., 2012). The current review elucidates the phytase production from different sources by using natural and recombinant means along with its removal from the environment.
The natural sources of phytases are quite diverse. Plants, animals, fungi as well as bacteria are the natural sources of phytases (Konietzny and Greiner, 2004).
Occurrence of phytase producing bacteria
The bacterial phytases possess several characteristics that make them important in enzyme industry. These include broad spectrum of temperature tolerance, wide range of pH functioning (even closer to the stomach pH of chicken and pigs), high catalytic efficiency, and greater resistance to pepsin. A good example is the phytase-associated class of Escherichia coli, that enhances the overall availability of phosphate from phytate (Santos, 2011). The strain BL21 (DE3) of Escherichia coli can produce phytase up to 20% of total soluble protein under T7 promoter (Kim et al., 1998). Similarly, wide range of Bacillus species are also identified with promising phytase production. Two strains of Bacillus licheniformis LH1 and LF1 can produce inorganic phytase quicker than average strains (Roy et al., 2009). Interestingly, the role of Bacillus species in phytase enzyme industry is not limited but has also been observed in the immobilization of enzymes on edible matrix. This helps in creating stabilized feed with the enzyme responsible for release of phosphate from phytate. The method displays an efficient food-grade safety (Cho et al., 2011).
Recombinant DNA technology is used to improve the working efficiency of the enzyme machinery especially on wide pH range and temperature (Miao et al., 2013). This technology has further enhanced the production rate in certain species. For example, cloning of the E. coli originated benzyl penicillin acylase gene increased phytase production up to 45-fold as compared to wild-type (Adrio and Demain, 2010). Likewise, lactic acid producing bacteria (LAB) such as Lactobacillus reuteri, Lactobacillus panis, Pediococcus pentosaceus and Lactobacillus panis were also tested for both intra and extra cellular activity; among which Lactobacillus panis appeared to have highest phytase activity (Nuobariene et al., 2015).
Despite the renowned importance in biotechnology, information regarding phytase-producing bacteria is not clearly defined and limited. Some major research insights are however required to improve the information about bacterial phytases and their utilization. Some bacteria that show quicker and high rate of phytase production are listed in (Table 1).
Occurrence of phytase producing Yeast
Yeast is a better source of phytases as compared to the bacteria due to the heterologous protein production (Macauley‐Patrick et al., 2005). All yeast phytases have a broad temperature (55-75ºC) range and optimal pH (2-5). The molecular weight (MW) of yeast protein range is (40-490 kDa) while bacteria have (10-45 kDa) (Vohra and Satyanarayana, 2004). To analyze phytase production, specific phytase assays were performed on different yeast strains. Two strains namely Arxula adeninivorans and Pichia anomalareached have been shown to possess highest phytase activity (Olstorpe et al., 2009). Some phytase producing species of yeast are listed in Table 2.
Occurrence of phytase producing fungi
The fungal sources of phytase production are recognized as most promising source due to three main reasons, i.e., (1) fungi is itself resistant to the harsh environment, (2) its growth rate is higher as compared to other sources, and (3) its products (enzymes) possess diverse functioning potential. An example is thermophilic fungi T. lanuginosus that secretes phytases, which are tolerant against high temperatures, wide pH range, possesses longer shelf life, and is protease resistant (Singh and Satyanarayana, 2006; Wang et al., 2007). This is the reason that thermophilic fungi have been widely exploited for commercial purposes, e.g., feed and food industries to tolerate acidic environment of intestine during digestion (Greiner and Konietzny, 2006; Maheshwari et al., 2000; Reilly, 1999; Suhairin et al., 2010, Kelly et al., 1986). Thermophilic fungi have an advantage to grow in solid-state fermentation, which is not possible for yeast and bacteria (Vohra and Satyanarayana, 2003), (Vats and Banerjee, 2004). As described earlier, many of the fungi originated phytases are stable in organic solvents and therefore, their functioning is not inhibited in majority of the cases (Gulati et al., 2007; Singh and Satyanarayana, 2009; Vats and Banerjee, 2005).
Extracellular phytases are secreted by a cell and functions outside it. These have simple nutritional environment than bacteria and yeast (Wodzinski and Ullah, 1995), (Vohra and Satyanarayana, 2003), (Maheshwari et al., 2000). Extracellular secreted phytase can be purified easily by down streaming process, which is cost effective as compared to the purification of the intracellular enzymes. Different strains of Aspergillus niger have been employed to produce a bulk amount of extracellular phytase with subsequent cultivation on solid-state substrates economically (Ramachandran et al., 2007).Some fungal sources of phytase are given in Table 3.
Genetically modified sources of phytases
The natural sources of phytases are quite diverse but the rate of production is quite low to meet up demand of food industry (Singh and Satyanarayana, 2008a). Bacterial genera Xinnthomonas, Psettdomonas, Xanthomonas campestri, Pseudomonas syringae, Xanthomonas oryzae, produces various types of phytases (Jorquera et al., 2008). But the rate of prodution is quite low, moreover downstreaming processing is costly due to intracellular prodution. To overcome this problem, different approaches of genetic and protein engineering are carried out for phytase production (Lei and Stahl, 2001). Facultative methylotrophic yeasts such as Hansenula polymorpha and Pichia pastoris are considered as high yield expression systems (genetic constructs, designed to produce an RNA or protein either inside or outside a cell (Macauley‐Patrick et al., 2005) in another host system) for phytase production (Gellissen, 2000). Methanol utilization pathway associated with expression system (methanol is used as an inducer for gene expression) in Pichia pastoris is used for phytase production (Mayer et al., 1999).
Genetically modified plant phytase expressed in canola and tobacco is better source of phytase than microbial sources. The phytase gene can easily be transferred and expressed in plants without the danger of contamination by animal pathogen. Phytaseed is genetically produced from canola seed having phytase activity (Zhang et al., 2000). Table 4 show sources strain and production strain for phytase while comparison of phytase sources at optimum conditions along with their efficacy are shown in Table 5.
Commercially available phytases
As far as its commercialization, some of bacterial and fungal phytase are available in market. Phyzyme (Danisco Animal Nutrition, Carol Stream, IL) a bacterial phytase from Esherichia coli and produced by Schizosacchromyces pombe is also commercialized phytase used as feed supplement (Wu et al., 2006). Natuphos (BASF Corp., Mt. Olive, NJ) is an aspergillus niger phytase used as animal feed along with soyabeen meal (Augspurger et al., 2003). Ronozyme (Roche Vitamins, Parsippany, NJ) is a fungal phytase naturally derived from Peniophora lyci and expressed in Apergillus oryzae through gene technology and used as phytase source in poultry industry (Nielsen and Wenzel, 2007). Similarly, two phytases from the fungal source, one from basidiomycete, Peniophora lycii, and the other from a deuteromycete, Aspergillus ficuum, have been commercialized (Lei and Porres, 2003). Some commercially available genetically modified phytases are shown in Table 6.
Classical examples on application of phytases
In recent years, addition of feed enzymes in diets of pigs and poultry enhances the nutrient utilization. Exogenous enzymes are capable of degrading non-starch polysaccharides (NSP) in broiler feed based on grains; including barley and wheat initiated this study practice (Yin et al., 2001). However, phytate-bound phosphorus and its partial availability are found in all chick diets (Nelson, 1967). A general application of phytase enzymes is its presence in poultry and pig feed that economically enhances bioavailability of P and reduces the P load on the environment (Cao et al., 2007).
In human foodstuffs, the negative influence of phytate on the bioavailability of Calcium and trace elements zinc has been comprehensively investigated. In certain aspects, however, human diets containing phytate contents have potential paybacks, e.g. anti-carcinogenic properties (Selle and Ravindran, 2007). The application of phytases is in the manufacture of food supplements and functional foods in human consumption (Greiner and Konietzny, 2006). Phytases are used in long shelf life products, liquid and dry enzyme preparations. Enzymes worked well by retaining their activity at high temperatures (Haefner et al., 2005).
Phytases not only have application in diets for mono-gastric animals as feed additive, but also have great potential in enzymes processing and manufacturing for human food consumption. Complete removal of phytate from food digestion in upper small intestine and human stomach results in the bioavailability of essential minerals like (Fe and Zn). Animal feed, with the addition of phytase, decreases the phosphorus load upto 50% in the environment and increases the availability of phosphorus for animal digestion.
Moreover, phytate removal could be cost effective for production, purity and yield of the final products like bread making; corn wet milling, production of plant protein isolates and fractionation of cereal bran. Further research is required to identify metabolically active myo-inositol phosphate or a mixture of phosphatases and phytases. Still one ideal phytase does not exist for complete food degradation. Intrinsic phytases, their catalytic properties should be used for phytate dephosphorylation and to optimize phytate degradation in food product.
We acknowledge National Institute for Biotechnology and Genetic Engineering (NIBGE) for providing excellent research facilities. We further extend our acknowledgments to Dr. Farooq Latif, Dr. Asma Imran, and Mr. Muhammad Arslan, for support and guidance in improving the manuscript.
Compliance with ethical standards
Conflict of Interest
The authors declare that they have no conflict of interests..
Abram, M.E., Ferris, A.L., Das, K., Quinoñes, O., Shao, W., Tuske, S., Alvord, W.G., Arnold, E., Hughes, S.H., 2014. Mutations in HIV-1 Reverse Transcriptase Affect the Errors Made in a Single Cycle of Viral Replication. Journal of Virology 88, 7589-7601.
Adrio, J.-L., Demain, A.L., 2010. Recombinant organisms for production of industrial products. Bioengineered bugs 1, 116-131.
Affrifah, N.S., Chinnan, M.S., Fang, C., 2006. Modeling the thermal inactivation of phytase in steamed cowpea seeds. LWT - Food Science and Technology 39, 598-604.
Andlid, T.A., Veide, J., Sandberg, A.-S., 2004. Metabolism of extracellular inositol hexaphosphate (phytate) by Saccharomyces cerevisiae. International journal of food microbiology 97, 157-169.
Anis Shobirin, M., Farouk, A., Greiner, R., 2009. Potential phytate-degrading enzyme producing bacteria isolated from Malaysian maize plantation. African Journal of Biotechnology 8, 3540-3546.
Aseri, G., Jain, N., Tarafdar, J., 2009. Hydrolysis of organic phosphate forms by phosphatases and phytase producing fungi of arid and semi-arid soils of India. Am Eurasian J Agric Environ Sci 5, 564-570.
Augspurger, N., Webel, D., Lei, X., Baker, D., 2003. Efficacy of an phytase expressed in yeast for releasing phytate-bound phosphorus in young chicks and pigs. Journal of Animal Science 81, 474-483.
Awad, G.E., Helal, M.M., Danial, E.N., Esawy, M.A., 2014. Optimization of phytase production by Penicillium purpurogenum GE1 under solid state fermentation by using Box–Behnken design. Saudi journal of biological sciences 21, 81-88.
Bala, A., Sapna, Jain, J., Kumari, A., Singh, B., 2014. Production of an extracellular phytase from a thermophilic mould Humicola nigrescens in solid state fermentation and its application in dephytinization. Biocatalysis and Agricultural Biotechnology 3, 259-264.
Baldi, B.G., Scott, J.J., Everard, J.D., Loewus, F.A., 1988. Localization of constitutive phytases in lily pollen and properties of the pH 8 form. Plant Science 56, 137-147.
Beilen, J.B.v., Li, Z., 2002. Enzyme technology: an overview. Current Opinion in Biotechnology 13, 338-344.
Berka, R.M., Rey, M.W., Brown, K.M., Byun, T., Klotz, A.V., 1998. Molecular characterization and expression of a phytase gene from the thermophilic fungus Thermomyces lanuginosus. Applied and environmental microbiology 64, 4423-4427.
Bindu, S., Somashekar, D., Joseph, R., 1998. A comparative study on permeabilization treatments for in situ determination of phytase of Rhodotorula gracilis. Letters in applied microbiology 27, 336-340.
Bingol, N.T., Karsli, M.A., Bolat, D., Akca, I., Levendoglu, T., 2009. Effects of microbial phytase on animal performance, amount of phosphorus excreted and blood parameters in broiler fed low non-phytate phosphorus diets. Asian Journal of Animal and Veterinary Advances 4, 160-166.
Böer, E., Piontek, M., Kunze, G., 2009. Xplor® 2—an optimized transformation/expression system for recombinant protein production in the yeast Arxula adeninivorans. Applied microbiology and biotechnology 84, 583-594.
Bogar, B., Szakacs, G., Pandey, A., Abdulhameed, S., Linden, J.C., Tengerdy, R.P., 2003. Production of Phytase by Mucorracemosus in Solid‐State Fermentation. Biotechnology progress 19, 312-319.
Bohn, L., Meyer, A.S., Rasmussen, S.K., 2008. Phytate: impact on environment and human nutrition. A challenge for molecular breeding. Journal of Zhejiang University Science B 9, 165-191.
Brask-Pedersen, D.N., Glitsø, L.V., Skov, L.K., Lund, P., Sehested, J., 2013. Effect of exogenous phytase on degradation of inositol phosphate in dairy cows. Journal of Dairy Science 96, 1691-1700.
Brinch-Pedersen, H., 2000. Phytate and phytase in plants.(Review.). DIAS Report, Plant Production.
Brink, E.J., Beynen, A., 1991. Nutrition and magnesium absorption: a review. Progress in food & nutrition science 16, 125-162.
Buchholz, K., Kasche, V., Bornscheuer, U.T., 2012. Biocatalysts and enzyme technology. John Wiley & Sons.
Çalık, P., Ata, Ö., Güneş, H., Massahi, A., Boy, E., Keskin, A., Öztürk, S., Zerze, G.H., Özdamar, T.H., 2015. Recombinant protein production in Pichia pastoris under glyceraldehyde-3-phosphate dehydrogenase promoter: From carbon source metabolism to bioreactor operation parameters. Biochemical Engineering Journal 95, 20-36.
Cao, L., Wang, W., Yang, C., Yang, Y., Diana, J., Yakupitiyage, A., Luo, Z., Li, D., 2007. Application of microbial phytase in fish feed. Enzyme and Microbial Technology 40, 497-507.
Cao, S.-s., Hu, Z.-q., 2009. A new method for gene synthesis and its high-level expression. Journal of Microbiological Methods 79, 106-110.
Casey, A., Walsh, G., 2004. Identification and characterization of a phytase of potential commercial interest. Journal of Biotechnology 110, 313-322.
Chadha, B., Harmeet, G., Mandeep, M., Saini, H., Singh, N., 2004. Phytase production by the thermophilic fungus Rhizomucor pusillus. World Journal of Microbiology and Biotechnology 20, 105-109.
Chen, C.-C., Wu, P.-H., Huang, C.-T., Cheng, K.-J., 2004. A Pichia pastoris fermentation strategy for enhancing the heterologous expression of an Escherichia coli phytase. Enzyme and Microbial Technology 35, 315-320.
Chen, R., Zhang, C., Yao, B., Xue, G., Yang, W., Zhou, X., Zhang, J., Sun, C., Chen, P., Fan, Y., 2013. Corn seeds as bioreactors for the production of phytase in the feed industry. Journal of Biotechnology 165, 120-126.
Cheng, K., Selinger, L., Yanke, L., Bae, H., Zhou, L., Forsberg, C., 1999. Phytases of rumen micro-organisms, particularly of Selenomonas ruminantium, and uses thereof in feed additives and in transgenic plants. US patent 5, 605.
Chi-Wei Lan, J., Chang, C.-K., Wu, H.-S., 2014. Efficient production of mutant phytase (phyA-7) derived from Selenomonas ruminantium using recombinant Escherichia coli in pilot scale. Journal of Bioscience and Bioengineering 118, 305-310.
Cho, J., Lee, C., Kang, S., Lee, J., Lee, H., Bok, J., Woo, J., Moon, Y., Choi, Y., 2005. Molecular cloning of a phytase gene (phy M) from Pseudomonas syringae MOK1. Current microbiology 51, 11-15.
Cho, E.-A., Kim, E.-J., Pan, J.-G., 2011. Adsorption immobilization of Escherichia coli phytase on probiotic Bacillus polyfermenticus spores. Enzyme and Microbial Technology 49, 66-71.
Choct, M., 2006. Enzymes for the feed industry: past, present and future. World Poultry Science Journal 62, 5-16.
Choi, Y.M., Suh, H.J., , J.M., 2001. Purification and properties of extracellular phytase from Bacillus sp. KHU-10. Journal of Protein Chemistry 20, 287-292.
Chu, H.-M., Guo, R.-T., Lin, T.-W., Chou, C.-C., Shr, H.-L., Lai, H.-L., Tang, T.-Y., Cheng, K.-J., Selinger, B.L., Wang, A.H.-J., 2004. Structures of Selenomonas ruminantium phytase in complex with persulfated phytate: DSP phytase fold and mechanism for sequential substrate hydrolysis. Structure 12, 2015-2024.
Clare, J.J., Romanes, M.A., Rayment, F.B., Rowedder, J.E., Smith, M.A., Payne, M.M., Sreekrishna, K., Henwood, C.A., 1991. Production of mouse epidermal growth factor in yeast: high-level secretion using Pichia pastoris strains containing multiple gene copies. Gene 105, 205-212.
Coffey, R., Cromwell, G., 1995. The impact of environment and antimicrobial agents on the growth response of early-weaned pigs to spray-dried porcine plasma. Journal of Animal Science 73, 2532-2539.
Cowieson, A., Wilcock, P., Bedford, M., 2011. Super-dosing effects of phytase in poultry and other monogastrics. World Poultry Science Journal 67, 225.
Cregg, J.M., Madden, K.R., 1988. Development of the methylotrophic yeast, Pichia pastoris, as a host system for the production of foreign proteins. Developments in industrial Microbiology 29, 33-41.
Dali, N.S.M., Nuge, T., Maifiah, M.H.M., Yusof, F., Hussin, A.S.M., Farouk, A.-E., Salleh, H.M., 2011. Molecular Cloning and Production of Recombinant Phytase from Bacillus subtilis ASUIA243 in Pichia pastoris. IIUM Engineering Journal 12.
Dave, G., Modi, H., 2013. Phytase producing microbial species associated with rhizosphere of mangroves in an Arid Coastal Region of Dholara. Academia Journal of Biotechnology 1, 027-035.
Dechavez, R.B., Serrano Jr, A.E., Nuñal, S., Caipang, C.M., 2011. Production and characterization of phytase from Bacillus spp. as feed additive in aquaculture. AACL Bioflux 4, 394-403.
Delic, M., Mattanovich, D., Gasser, B., 2013. Repressible promoters—a novel tool to generate conditional mutants in Pichia pastoris. Microbial cell factories 12, 1-6.
Dvořáková, J., 1998. Phytase: sources, preparation and exploitation. Folia microbiologica 43, 323-338.
Ehrlich, K.C., Montalbano, B., Mullaney, E.J., Dischinger, H., Ullah, A.H., 1993. Identification and cloning of a second phytase gene (phyB) from Aspergillus niger (ficuum). Biochemical and biophysical research communications 195, 53-57.
Farhat, M.B., Farhat, A., Bejar, W., Kammoun, R., Bouchaala, K., Fourati, A., Antoun, H., Bejar, S., Chouayekh, H., 2009. Characterization of the mineral phosphate solubilizing activity of Serratia marcescens CTM 50650 isolated from the phosphate mine of Gafsa. Archives of microbiology 191, 815-824.
Fonseca-Maldonado, R., Maller, A., Bonneil, E., Thibault, P., Botelho-Machado, C., Ward, R.J., Polizeli, M.d.L.T.d.M., 2014. Biochemical properties of glycosylation and characterization of a histidine acid phosphatase (phytase) expressed in Pichia pastoris. Protein Expression and Purification 99, 43-49.
Fugthong, A., Boonyapakron, K., Sornlek, W., Tanapongpipat, S., Eurwilaichitr, L., Pootanakit, K., 2010. Biochemical characterization and in vitro digestibility assay of Eupenicillium parvum (BCC17694) phytase expressed in Pichia pastoris. Protein Expression and Purification 70, 60-67.
Fredrikson, M., Andlid, T., Haikara, A., Sandberg, A.S., 2002. Phytate degradation by micro‐organisms in synthetic media and pea flour. Journal of applied microbiology 93, 197-204.
Fukuda, Y., Hayakawa, T., Ichihara, E., Inoue, K., Ishihara, K., Ishino, H., Itow, Y., Kajita, T., Kameda, J., Kasuga, S., 1999. Measurement of the flux and zenith-angle distribution of upward throughgoing muons by Super-Kamiokande. Physical Review Letters 82, 2644.
Gellissen, G., 2000. Heterologous protein production in methylotrophic yeasts. Appl Microbiol Biotechnol 54, 741-750.
Gontia-Mishra, I., Deshmukh, D., Tripathi, N., Bardiya-Bhurat, K., Tantwai, K., Tiwari, S., 2013. Isolation, morphological and molecular characterization of phytate-hydrolysing fungi by 18S rDNA sequence analysis. Brazilian Journal of Microbiology 44, 317-323.
Golovan, S., Wang, G., Zhang, J., Forsberg, C.W., 1999. Characterization and overproduction of the Escherichia coli appA encoded bifunctional enzyme that exhibits both phytase and acid phosphatase activities. Canadian journal of microbiology 46, 59-71.
Greiner, R., Jany, K., 1991. Characterization of a phytase from Escherichia-coli, Biological Chemistry Hoppe-Seyler. WALTER DE GRUYTER & CO GENTHINER STRASSE 13, D-10785 BERLIN, GERMANY, pp. 664-665.
Greiner, R., Konietzny, U., Jany, K.-D., 1993. Purification and characterization of two phytases from Escherichia coli. Archives of biochemistry and biophysics 303, 107-113.
Greiner, R., 2004a. Degradation of myo-inositol hexakisphosphate by a phytate-degrading enzyme from Pantoea agglomerans. The protein journal 23, 577-585.
Greiner, R., 2004b. Purification and properties of a phytate-degrading enzyme from Pantoea agglomerans. The protein journal 23, 567-576.
Greiner, R., Konietzny, U., 2006. Phytase for food application. Food Technology and Biotechnology 44, 123-140.
Greiner, R., Konietzny, U., Blackburn, D.M., Jorquera, M.A., 2013. Production of partially phosphorylated myo-inositol phosphates using phytases immobilised on magnetic nanoparticles. Bioresource Technology 142, 375-383.
Guerfal, M., Ryckaert, S., Jacobs, P.P., Ameloot, P., Van Craenenbroeck, K., Derycke, R., Callewaert, N., 2010. Research The HAC1 gene from Pichia pastoris: characterization and effect of its overexpression on the production of secreted, surface displayed and membrane proteins. Microb Cell Fact 9, 49-60.
Guimarães, L.H.S., Peixoto-Nogueira, S.C., Michelin, M., Rizzatti, A.C.S., Sandrim, V.C., Zanoelo, F.F., Aquino, A.C.M., Junior, A.B., Polizeli, M.d.L., 2006. Screening of filamentous fungi for production of enzymes of biotechnological interest. Brazilian Journal of Microbiology 37, 474-480.
Gulati, H., Chadha, B., Saini, H., 2007. Production, purification and characterization of thermostable phytase from thermophilic fungus Thermomyces lanuginosus TL-7. Acta microbiologica et immunologica hungarica 54, 121-138.
Guo, M., Hang, H., Zhu, T., Zhuang, Y., Chu, J., Zhang, S., 2008. Effect of glycosylation on biochemical characterization of recombinant phytase expressed in Pichia pastoris. Enzyme and Microbial Technology 42, 340-345.
Ha, N.-C., Kim, Y.-O., Oh, T.-K., Oh, B.-H., 1999. Preliminary X-ray crystallographic analysis of a novel phytase from a Bacillus amyloliquefaciens strain. Acta Crystallographica Section D: Biological Crystallography 55, 691-693.
Ha, N.-C., Oh, B.-C., Shin, S., Kim, H.-J., Oh, T.-K., Kim, Y.-O., Choi, K.Y., Oh, B.-H., 2000. Crystal structures of a novel, thermostable phytase in partially and fully calcium-loaded states. Nature Structural & Molecular Biology 7, 147-153.
Haefner, S., Knietsch, A., Scholten, E., Braun, J., Lohscheidt, M., Zelder, O., 2005. Biotechnological production and applications of phytases. Appl Microbiol Biotechnol 68, 588-597.
Han, Y., Wilson, D.B., gen Lei, X., 1999. Expression of an Aspergillus nigerPhytase Gene (phyA) in Saccharomyces cerevisiae. Applied and Environmental Microbiology 65, 1915-1918.
Hang, H., Ye, X., Guo, M., Chu, J., Zhuang, Y., Zhang, M., Zhang, S., 2009. A simple fermentation strategy for high-level production of recombinant phytase by Pichia pastoris using glucose as the growth substrate. Enzyme and Microbial Technology 44, 185-188.
Haros, M., Bielecka, M., Sanz, Y., 2005. Phytase activity as a novel metabolic feature in Bifidobacterium. FEMS Microbiology Letters 247, 231-239.
Huang, H., Luo, H., Yang, P., Meng, K., Wang, Y., Yuan, T., Bai, Y., Yao, B., 2006. A novel phytase with preferable characteristics from Yersinia intermedia. Biochemical and biophysical research communications 350, 884-889.
Huang, X., Chen, L., Xu, J., Ji, H.-F., Zhu, S., Chen, H., 2014. Rapid visual detection of phytase gene in genetically modified maize using loop-mediated isothermal amplification method. Food Chemistry 156, 184-189.
Idriss, E.E., Makarewicz, O., Farouk, A., Rosner, K., Greiner, R., Bochow, H., Richter, T., Borriss, R., 2002. Extracellular phytase activity of Bacillus amyloliquefaciens FZB45 contributes to its plant-growth-promoting effecta. Microbiology 148, 2097-2109.
Irving, G., Cosgrove, D., 1971. Inositol phosphate phosphatases of microbiological origin. Some properties of a partially purified bacterial (Pseudomonas sp.) phytase. Australian journal of biological sciences 24, 547-558.
Jang, E.-S., KIM, Y.-J., OH, N.-S., 2004. Purification and properties of an extracellular acid phytase from Pseudomonas fragi Y9451. Journal of microbiology and biotechnology 14, 1004-1008.
Jareonkitmongkol, S., Ohya, M., Watanabe, R., Takagi, H., Nakamori, S., 1997. Partial purification of phytase from a soil isolate bacterium, Klebsiella oxytoca MO-3. Journal of fermentation and bioengineering 83, 393-394.
Johnson, S.C., Yang, M., Murthy, P.P.N., 2010. Heterologous expression and functional characterization of a plant alkaline phytase in Pichia pastoris. Protein Expression and Purification 74, 196-203.
Jorquera, M., MARTíNEZ, O., Maruyama, F., Marschner, P., de la Luz Mora, M., 2008. Current and future biotechnological applications of bacterial phytases and phytase-producing bacteria. Microbes and environments 23, 182-191.
Kelly, C.T., Giblin, M., Fogarty, W.M., 1986. Resolution, purification, and characterization of two extracellular glucohydrolases, α-glucosidase and maltase, of Bacillus licheniformis. Canadian journal of microbiology 32, 342-347.
Kerovuo, J., Lauraeus, M., Nurminen, P., Kalkkinen, N., Apajalahti, J., 1998. Isolation, characterization, molecular gene cloning, and sequencing of a novel phytase from Bacillus subtilis. Applied and Environmental Microbiology 64, 2079-2085.
Kerovuo, J., Lappalainen, I., Reinikainen, T., 2000. The metal dependence of Bacillus subtilis phytase. Biochemical and biophysical research communications 268, 365-369.
Kim, Y.-O., Kim, H.-K., Bae, K.-S., Yu, J.-H., Oh, T.-K., 1998. Purification and properties of a thermostable phytase from Bacillus sp. DS11. Enzyme and Microbial Technology 22, 2-7.
Kim, Y.-O., Lee, J.-K., Kim, H.-K., Yu, J.-H., Oh, T.-K., 1998. Cloning of the thermostable phytase gene (phy) from Bacillus sp. DS11 and its overexpression in Escherichia coli. FEMS Microbiology Letters 162, 185-191.
Kim, H.-W., Kim, Y.-O., Lee, J.-H., Kim, K.-K., Kim, Y.-J., 2003. Isolation and characterization of a phytase with improved properties from Citrobacter braakii. Biotechnology letters 25, 1231-1234.
Koganesawa, N., Aizawa, T., Shimojo, H., Miura, K., Ohnishi, A., Demura, M., Hayakawa, Y., Nitta, K., Kawano, K., 2002. Expression and purification of a small cytokine growth-blocking peptide from armyworm Pseudaletia separata by an optimized fermentation method using the methylotrophic yeast Pichia pastoris. Protein expression and purification 25, 416-425.
Konietzny, U., Greiner, R., 2004. Bacterial phytase: potential application, in vivo function and regulation of its synthesis. Brazilian Journal of Microbiology 35, 12-18
Krygier, S., Solbak, A., Shanahan, D., Ciofalo, V., 2014. Safety evaluation of phytase 50104 enzyme preparation (also known as VR003), expressed in Pseudomonas fluorescens, intended for increasing digestibility of phytate in monogastrics. Regulatory Toxicology and Pharmacology 70, 545-554.
Kuhn, M.R., Stahl, S.A., 2003. Fluency: A review of developmental and remedial practices. Journal of educational psychology 95, 3.
Kumar, V., Sinha, A.K., Makkar, H.P., Becker, K., 2010. Dietary roles of phytate and phytase in human nutrition: A review. Food Chemistry 120, 945-959.
Lambrechts, C., Boze, H., Segueilha, L., Moulin, G., Galzy, P., 1993. Influence of culture conditions on the biosynthesis of Schwanniomyces castellii phytase. Biotechnology Letters 15, 399-404.
Lan, G., Abdullah, N., Jalaludin, S., Ho, Y., 2002. Culture conditions influencing phytase production of Mitsuokella jalaludinii, a new bacterial species from the rumen of cattle. Journal of applied microbiology 93, 668-674.
Lazali, M., Drevon, J.J., 2014. The nodule conductance to O2 diffusion increases with phytase activity in N2-fixing Phaseolus vulgaris L. Plant Physiology and Biochemistry 80, 53-59.
Lee, S., Kim, T., Stahl, C.H., Lei, X.G., 2005. Expression of Escherichia coli AppA2 phytase in four yeast systems. Biotechnology Letters 27, 327-334.
Lei, X., Ku, P., Miller, E., Yokoyama, M., 1993. Supplementing corn-soybean meal diets with microbial phytase linearly improves phytate phosphorus utilization by weanling pigs. Journal of Animal Science 71, 3359-3367.
Lei, X., Stahl, C., 2001. Biotechnological development of effective phytases for mineral nutrition and environmental protection. Appl Microbiol Biotechnol 57, 474-481.
Lei, X.G., Porres, J.M., 2003. Phytase enzymology, applications, and biotechnology. Biotechnology Letters 25, 1787-1794.
Li, X., Liu, Z., Chi, Z., 2008. Production of phytase by a marine yeast Kodamaea ohmeri BG3 in an oats medium: optimization by response surface methodology. Bioresource technology 99, 6386-6390.
Lim, H., Namkung, H., Paik, I., 2003. Effects of phytase supplementation on the performance, egg quality, and phosphorous excretion of laying hens fed different levels of dietary calcium and nonphytate phosphorous. Poultry Science 82, 92-99.
Liu, B.-L., Rafiq, A., Tzeng, Y.-M., Rob, A., 1998. The induction and characterization of phytase and beyond. Enzyme and Microbial Technology 22, 415-424.
Loponen, J., Sibakov, J., 2013. Sourdough and Cereal Beverages, Handbook on Sourdough Biotechnology. Springer, pp. 265-278.
Luo, H.-Y., Huang, H.-Q., Bai, Y.-G., Wang, Y.-R., Yang, P.-L., Meng, K., Yuan, T.-Z., Yao, B., 2006. Improving Phytase Expression by Increasing the Gene Copy Number of appA-m in Pichia pastoris. Chinese Journal of Biotechnology 22, 528-533.
Lynd, L.R., Wyman, C.E., Gerngross, T.U., 1999. Biocommodity engineering. Biotechnology progress 15, 777-793.
Macauley‐Patrick, S., Fazenda, M.L., McNeil, B., Harvey, L.M., 2005. Heterologous protein production using the Pichia pastoris expression system. Yeast 22, 249-270.
Maheshwari, R., Bharadwaj, G., Bhat, M.K., 2000. Thermophilic fungi: their physiology and enzymes. Microbiology and molecular biology reviews 64, 461-488.
Mayer, A., Hellmuth, K., Schlieker, H., Lopez‐Ulibarri, R., Oertel, S., Dahlems, U., Strasser, A., Van Loon, A., 1999. An expression system matures: A highly efficient and cost‐effective process for phytase production by recombinant strains of Hansenula polymorpha. Biotechnology and bioengineering 63, 373-381.
Miao, Y., Xu, H., Fei, B., Qiao, D., Cao, Y., 2013. Expression of food-grade phytase in Lactococcus lactis from optimized conditions in milk broth. Journal of Bioscience and Bioengineering 116, 34-38.
Mitchell, D.B., Vogel, K., Weimann, B.J., Pasamontes, L., van Loon, A.P., 1997. The phytase subfamily of histidine acid phosphatases: isolation of genes for two novel phytases from the fungi Aspergillus terreus and Myceliophthora thermophila. Microbiology 143, 245-252.
Mittal, A., Singh, G., Goyal, V., Yadav, A., Aggarwal, N.K., 2012. Production of phytase by acido-thermophilic strain of Klebsiella sp. DB-3FJ711774. 1 using orange peel flour under submerged fermentation. Innovative Romanian Food Biotechnology 10.
Moraes, M.L., Oliveira Jr, O.N., Filho, U.P.R., Ferreira, M., 2008. Phytase immobilization on modified electrodes for amperometric biosensing. Sensors and Actuators B: Chemical 131, 210-215.
Moubasher, A.-A.H., Ismail, M.A., Hussein, N.A., Gouda, H.A., 2016. Enzyme producing capabilities of some extremophilic fungal strains isolated from different habitats of Wadi El-Natrun, Egypt. Part 1: Protease, lipase and phosphatase. European Journal of Biological Research 6, 92-102.
Mullaney, E.J., Daly, C.B., Ullah, A.H., 2000. Advances in phytase research. Advances in applied microbiology 47, 157-199.
Murphy, A.M., Otto, B., Brearley, C.A., Carr, J.P., Hanke, D.E., 2008. A role for inositol hexakisphosphate in the maintenance of basal resistance to plant pathogens. The Plant Journal 56, 638-652.
Nelson, T., 1967. The utilization of phytate phosphorus by poultry—A review. Poultry Science 46, 862-871.
Nevalainen, H.K., Paloheimo, M.T., Miettinen-Oinonen, A.S., Torkkeli, T.K., Cantrell, M., Piddington, C.S., Rambosek, J.A., Turunen, M.K., Fagerstrom, R.B., 1998. Production of phytate degrading enzymes in Trichoderma. Google Patents.
Nielsen, P.H., Wenzel, H., 2007. Environmental assessment of Ronozyme® P5000 CT phytase as an alternative to inorganic phosphate supplementation to pig feed used in intensive pig production. The International Journal of Life Cycle Assessment 12, 514
Nielsen, M.M., Damstrup, M.L., Hansen, Å., 2008. An optimised micro-titer plate method for characterisation of endogenous rye phytase under industrial rye bread making conditions. European Food Research and Technology 227, 1009-1015.
Noseda, D.G., Recúpero, M.N., Blasco, M., Ortiz, G.E., Galvagno, M.A., 2013. Cloning, expression and optimized production in a bioreactor of bovine chymosin B in Pichia (Komagataella) pastoris under AOX1 promoter. Protein expression and purification 92, 235-244.
Nuobariene, L., Cizeikiene, D., Gradzeviciute, E., Hansen, Å.S., Rasmussen, S.K., Juodeikiene, G., Vogensen, F.K., 2015. Phytase-active lactic acid bacteria from sourdoughs: Isolation and identification. LWT - Food Science and Technology 63, 766-772.
Olstorpe, M., Schnürer, J., Passoth, V., 2009. Screening of yeast strains for phytase activity. FEMS yeast research 9, 478-488.
Pandey, A., Szakacs, G., Soccol, C.R., Rodriguez-Leon, J.A., Soccol, V.T., 2001. Production, purification and properties of microbial phytases. Bioresource Technology 77, 203-214.
Papagianni, M., Nokes, S.E., Filer, K., 1999. Production of phytase by Aspergillus niger in submerged and solid-state fermentation. Process Biochemistry 35, 397-402.
Pasamontes, L., Haiker, M., Henriquez-Huecas, M., Mitchell, D.B., van Loon, A.P., 1997. Cloning of the phytases from Emericella nidulans and the thermophilic fungus Talaromyces thermophilus. Biochimica et Biophysica Acta (BBA)-Gene Structure and Expression 1353, 217-223.
Pasamontes, L., Haiker, M., Wyss, M., Tessier, M., Van Loon, A., 1997. Gene cloning, purification, and characterization of a heat-stable phytase from the fungus Aspergillus fumigatus. Applied and Environmental microbiology 63, 1696-1700.
Piddington, C., Houston, C., Paloheimo, M., Cantrell, M., Miettinen-Oinonen, A., Nevalainen, H., Rambosek, J., 1993. The cloning and sequencing of the genes encoding phytase (phy) and pH 2.5-optimum acid phosphatase (aph) from Aspergillus niger var. awamori. Gene 133, 55-62.
Poutanen, K., Flander, L., Katina, K., 2009. Sourdough and cereal fermentation in a nutritional perspective. Food microbiology 26, 693-699.
Prielhofer, R., Maurer, M., Klein, J., Wenger, J., Kiziak, C., Gasser, B., Mattanovich, D., 2013. Induction without methanol: novel regulated promoters enable high-level expression in Pichia pastoris. Microb Cell Fact 12, 5.
Promdonkoy, P., Tang, K., Sornlake, W., Harnpicharnchai, P., Kobayashi, R.S., Ruanglek, V., Upathanpreecha, T., Vesaratchavest, M., Eurwilaichitr, L., Tanapongpipat, S., 2009. Expression and characterization of Aspergillus thermostable phytases in Pichia pastoris. FEMS microbiology letters 290, 18-24.
Qian, H., Kornegay, E., Conner, D., 1996. Adverse effects of wide calcium: phosphorus ratios on supplemental phytase efficacy for weanling pigs fed two dietary phosphorus levels. Journal of Animal Science 74, 1288-1297.
Quan, C.-S., Tian, W.-J., Fan, S.-D., Kikuchi, J.-I., 2004. Purification and properties of a low-molecular-weight phytase from Cladosporium sp. FP-1. Journal of Bioscience and Bioengineering 97, 260-266.
Ramachandran, S., Singh, S.K., Larroche, C., Soccol, C.R., Pandey, A., 2007. Oil cakes and their biotechnological applications–A review. Bioresource technology 98, 2000-2009.
Reese, B.N., Payne, G.A., Nielsen, D.M., Woloshuk, C.P., 2011. Gene expression profile and response to maize kernels by Aspergillus flavus. Phytopathology 101, 797-804.
Reilly, P.J., 1999. Protein engineering of glucoamylase to improve industrial performance—a review. Starch‐Stärke 51, 269-274.
Richardson, A., Hadobas, P., 1997. Soil isolates of Pseudomonas spp. that utilize inositol phosphates. Canadian Journal of Microbiology 43, 509-516.
Rocky-Salimi, K., Hashemi, M., Safari, M., Mousivand, M., 2016. A novel phytase characterized by thermostability and high pH tolerance from rice phyllosphere isolated Bacillus subtilis B.S.46. Journal of Advanced Research 7, 381-390.
Rodriguez, M.S., Desterro, J.M., Lain, S., Midgley, C.A., Lane, D.P., Hay, R.T., 1999. SUMO‐1 modification activates the transcriptional response of p53. The EMBO journal 18, 6455-6461.
Rodriguez, E., Wood, Z.A., Karplus, P.A., Lei, X.G., 2000. Site-directed mutagenesis improves catalytic efficiency and thermostability of Escherichia coli pH 2.5 acid phosphatase/phytase expressed in Pichia pastoris. Archives of Biochemistry and Biophysics 382, 105-112.
Rosen, G., Garnsworthy, P., Wiseman, J., 2002. Microbial phytase in broiler nutrition. Recent advances in animal nutrition 2002, 105-117.
Rousseau, X., Même, N., Magnin, M., Nys, Y., Narcy, A., 2011. Meta-analysis of phosphorus utilisation taking into account dietary calcium and microbial phytase supply in growing-finishing broilers. 9ème Journées de la Recherche Avicole, Tours, France, 29-30 Mars, 2011.
Roy, T., Mondal, S., Ray, A.K., 2009. Phytase‐producing bacteria in the digestive tracts of some freshwater fish. Aquaculture research 40, 344-353.
Sajidan, A., Farouk, A., Greiner, R., Jungblut, P., Müller, E.-C., Borriss, R., 2004. Molecular and physiological characterisation of a 3-phytase from soil bacterium Klebsiella sp. ASR1. Applied microbiology and biotechnology 65, 110-118.
Samson, R.A., 1994. Current systematics of the genus Aspergillus, The genus Aspergillus. Springer, pp. 261-276.
Sano, K., Fukuhara, H., Nakamura, Y., 1999. Phytase of the yeast Arxula adeninivorans. Biotechnology Letters 21, 33-38.
Santos, T., 2011. Optimisation of phytase production by Aspergillus niger using solid state fermentation. National University of Ireland.
Sarangi, S., Tye, S.-H.H., 2002. Cosmic string production towards the end of brane inflation. Physics Letters B 536, 185-192.
Schallmey, M., Singh, A., Ward, O.P., 2004. Developments in the use of Bacillus species for industrial production. Canadian journal of microbiology 50, 1-17.
Shah, V., Parekh, L., 1990. Phytase from Klebsiella Sp. No. PG-2: purification and properties. Indian journal of biochemistry & biophysics 27, 98-102.
Simons, P., Versteegh, H.A., Jongbloed, A.W., Kemme, P., Slump, P., Bos, K., Wolters, M., Beudeker, R., Verschoor, G., 1990. Improvement of phosphorus availability by microbial phytase in broilers and pigs. British Journal of Nutrition 64, 525-540.
Singh, B., Satyanarayana, T., 2008. Phytase production by a thermophilic mould Sporotrichum thermophile in solid state fermentation and its potential applications. Bioresource technology 99, 2824-2830.
Singh, B., Satyanarayana, T., 2011. Microbial phytases in phosphorus acquisition and plant growth promotion. Physiology and Molecular Biology of Plants 17, 93-103.
Sreeramulu, G., Srinivasa, D., Nand, K., Joseph, R., 1996. Lactobacillus amylovorus as a phytase producer in submerged culture. Letters in Applied Microbiology 23, 385-388.
Schoevaart, R., Wolbers, M., Golubovic, M., Ottens, M., Kieboom, A., Van Rantwijk, F., Van der Wielen, L., Sheldon, R., 2004. Preparation, optimization, and structures of cross‐linked enzyme aggregates (CLEAs). Biotechnology and Bioengineering 87, 754-762.
Scott, J.J., 1991. Alkaline phytase activity in nonionic detergent extracts of legume seeds. Plant Physiology 95, 1298-1301.
Selle, P.H., Ravindran, V., 2007. Microbial phytase in poultry nutrition. Animal Feed Science and Technology 135, 1-41.
Shetty, J.K., Paulson, B., Pepsin, M., Chotani, G., Dean, B., Hruby, M., 2008. Phytase in fuel ethanol production offers economical and environmental benefits. International Sugar Journal 110, 160, 162, 164, 166, 168-174.
Simons, P., Versteegh, H.A., Jongbloed, A.W., Kemme, P., Slump, P., Bos, K., Wolters, M., Beudeker, R., Verschoor, G., 1990. Improvement of phosphorus availability by microbial phytase in broilers and pigs. British Journal of Nutrition 64, 525-540.
Singh, B., Satyanarayana, T., 2006. A marked enhancement in phytase production by a thermophilic mould Sporotrichum thermophile using statistical designs in a cost‐effective cane molasses medium. Journal of applied microbiology 101, 344-352.
Singh, B., Satyanarayana, T., 2008a. Phytase production by a thermophilic mould Sporotrichum thermophile in solid state fermentation and its potential applications. Bioresource technology 99, 2824-2830.
Singh, B., Satyanarayana, T., 2008b. Phytase production by Sporotrichum thermophile in a cost‐effective cane molasses medium in submerged fermentation and its application in bread. Journal of applied microbiology 105, 1858-1865.
Singh, B., Satyanarayana, T., 2009. Characterization of a HAP–phytase from a thermophilic mould Sporotrichum thermophile. Bioresource technology 100, 2046-2051.
Slominski, B.A., Davie, T., Nyachoti, M.C., Jones, O., 2007. Heat stability of endogenous and microbial phytase during feed pelleting. Livestock Science 109, 244-246.
Soetan, K., Oyewole, O., 2009. The need for adequate processing to reduce the anti-nutritional factors in plants used as human foods and animal feeds: A review. African Journal of Food Science 3, 223-232.
Stadlmayr, G., Mecklenbräuker, A., Rothmüller, M., Maurer, M., Sauer, M., Mattanovich, D., Gasser, B., 2010. Identification and characterisation of novel Pichia pastoris promoters for heterologous protein production. Journal of biotechnology 150, 519-529.
Suhairin, A., Manap, A., Yazid, M., Hussin, M., Shobirin, A., Mustafa, S., 2010. Phytase: application in food industry. International Food Research Journal 17, 13-21.
Summerbell, R.C., 2005. From Lamarckian fertilizers to fungal castles: recapturing the pre-1985 literature on endophytic and saprotrophic fungi associated with ectomycorrhizal root systems. Studies in Mycology 53, 191-256.
Tambe, S.M., Kaklij, G.S., Kelkar, S.M., Parekh, L.J., 1994. Two distinct molecular forms of phytase from Klebsiella aerogenes: Evidence for unusually small active enzyme peptide. Journal of fermentation and bioengineering 77, 23-27.
Teixeira Filho, F.L., Baracat, E.C., Lee, T.H., Suh, C.S., Matsui, M., Chang, R.J., Shimasaki, S., Erickson, G.F., 2013. Aberrant expression of growth differentiation factor-9 in oocytes of women with polycystic ovary syndrome. The Journal of Clinical Endocrinology & Metabolism.
Thornton, C.G., Passen, S., 2004. Inhibition of PCR amplification by phytic acid, and treatment of bovine fecal specimens with phytase to reduce inhibition. Journal of Microbiological Methods 59, 43-52.
Turner, B., Baxter, R., Ellwood, N., Whitton, B., 2001. Characterization of the phosphatase activities of mosses in relation to their environment. Plant, Cell & Environment 24, 1165-1176.
Ullah, A.H., Sethumadhavan, K., Mullaney, E.J., Ziegelhoffer, T., Austin-Phillips, S., 1999. Characterization of recombinant fungal phytase (phyA) expressed in tobacco leaves. Biochemical and biophysical research communications 264, 201-206.
Ushasree, M.V., Vidya, J., Pandey, A., 2014. Extracellular expression of a thermostable phytase (phyA) in Kluyveromyces lactis. Process Biochemistry 49, 1440-1447.
Van Hartingsveldt, W., van Zeijl, C.M., Harteveld, G.M., Gouka, R.J., Suykerbuyk, M.E., Luiten, R.G., van Paridon, P.A., Selten, G.C., Veenstra, A.E., van Gorcom, R.F., 1993. Cloning, characterization and overexpression of the phytase-encoding gene (phyA) of Aspergillus niger. Gene 127, 87-94.
Vassilev, N., Vassileva, M., Bravo, V., Fernández-Serrano, M., Nikolaeva, I., 2007. Simultaneous phytase production and rock phosphate solubilization by Aspergillus niger grown on dry olive wastes. Industrial Crops and Products 26, 332-336.
Vats, P., Banerjee, U., 2005. Biochemical characterisation of extracellular phytase (myo-inositol hexakisphosphate phosphohydrolase) from a hyper-producing strain of Aspergillus niger van Teighem. Journal of Industrial Microbiology and Biotechnology 32, 141-147.
Vats, P., Banerjee, U.C., 2004. Production studies and catalytic properties of phytases (myo-inositolhexakisphosphate phosphohydrolases): an overview. Enzyme and Microbial Technology 35, 3-14.
Vogl, T., Glieder, A., 2013. Regulation of Pichia pastoris promoters and its consequences for protein production. New biotechnology 30, 385-404.
Vohra, A., Satyanarayana, T., 2001. Phytase production by the yeast, Pichia anomala. Biotechnology Letters 23, 551-554.
Vohra, A., Satyanarayana, T., 2002. Statistical optimization of the medium components by response surface methodology to enhance phytase production by Pichia anomala. Process Biochemistry 37, 999-1004.
Vohra, A., Satyanarayana, T., 2003. Phytases: microbial sources, production, purification, and potential biotechnological applications. Critical reviews in biotechnology 23, 29-60.
Vohra, A., Satyanarayana, T., 2004. A cost‐effective cane molasses medium for enhanced cell‐bound phytase production by Pichia anomala. Journal of applied microbiology 97, 471-476.
Vohra, A., Rastogi, S., Satyanarayana, T., 2006. Amelioration in growth and phosphorus assimilation of poultry birds using cell-bound phytase of Pichia anomala. World Journal of Microbiology and Biotechnology 22, 553-558.
Wang, X., Upatham, S., Panbangred, W., Isarangkul, D., Summpunn, P., Wiyakrutta, S., Meevootisom, V., 2004. Purification, characterization, gene cloning and sequence analysis of a phytase from Klebsiella pneumoniae subsp. pneumoniae XY-5. Science Asia 30, 383-390.
Wang, Y., Gao, X., Su, Q., Wu, W., An, L., 2007. Cloning, expression, and enzyme characterization of an acid heat-stable phytase from Aspergillus fumigatus WY-2. Current microbiology 55, 65-70.
Wang, Z.-h., Dong, X.-f., Tong, J.-m., Xu, S.-z., 2014. Effects of Fermentation Product Containing Phytase on Productive Performance, Egg Quality, and Phosphorous Apparent Metabolism of Laying Hens Fed Different Levels of Phosphorus. Journal of Integrative Agriculture 13, 2253-2259.
Watanabe, T., Ikeda, H., Masaki, K., Fujii, T., Iefuji, H., 2009. Cloning and characterization of a novel phytase from wastewater treatment yeast Hansenula fabianii J640 and expression in Pichia pastoris. Journal of Bioscience and Bioengineering 108, 225-230.
Whisstock, J.C., 2011. Serpin structure and evolution. Academic Press.
Wodzinski, R.J., Ullah, A., 1995. Phytase. Advances in applied microbiology 42, 263-302.
Wu, G., Liu, Z., Bryant, M., Roland, D., 2006. Comparison of Natuphos and Phyzyme as phytase sources for commercial layers fed corn-soy diet. Poultry Science 85, 64-69.
Wyss, M., Brugger, R., Kronenberger, A., Rémy, R., Fimbel, R., Oesterhelt, G., Lehmann, M., van Loon, A.P., 1999. Biochemical characterization of fungal phytases (myo-inositol hexakisphosphate phosphohydrolases): catalytic properties. Applied and environmental microbiology 65, 367-373.
Xiong, A.S., Yao, Q.-H., Peng, R.-H., Li, X., Fan, H.-Q., Guo, M.-J., Zhang, S.-L., 2004. Isolation, characterization, and molecular cloning of the cDNA encoding a novel phytase from Aspergillus niger 113 and high expression in Pichia pastoris. BMB Reports 37, 282-291.
Xiong, A.S., Yao, Q.H., Peng, R.H., Han, P.L., Cheng, Z.M., Li, Y., 2005. High level expression of a recombinant acid phytase gene in Pichia pastoris. Journal of applied Microbiology 98, 418-428.
Xiong, A.-S., Yao, Q.-H., Peng, R.-H., Zhang, Z., Xu, F., Liu, J.-G., Han, P.-L., Chen, J.-M., 2006. High level expression of a synthetic gene encoding Peniophora lycii phytase in methylotrophic yeast Pichia pastoris. Applied microbiology and biotechnology 72, 1039-1047.
Yip, W., Wang, L., Cheng, C., Wu, W., Lung, S., Lim, B.-L., 2003. The introduction of a phytase gene from Bacillus subtilis improved the growth performance of transgenic tobacco. Biochemical and biophysical research communications 310, 1148-1154.
Yadav, B., Verma, A., 2012. Phosphate solubilization and mobilization in soil through microorganisms under arid ecosystems. INTECH Open Access Publisher, Crotaia, 93-108.
Yadav, R., Tarafdar, J., 2003. Phytase and phosphatase producing fungi in arid and semi-arid soils and their efficiency in hydrolyzing different organic P compounds. Soil Biology and Biochemistry 35, 745-751.
Yanke, L., Bae, H., Selinger, L., Cheng, K., 1998. Phytase activity of anaerobic ruminal bacteria. Microbiology 144, 1565-1573.
Yanke, L., Selinger, L., Cheng, K.J., 1999. Phytase activity of Selenomonas ruminantium: a preliminary characterization. Letters in applied microbiology 29, 20-25.
Yin, Y.-L., Baidoo, S., Jin, L., Liu, Y., Schulze, H., Simmins, P., 2001. The effect of different carbohydrase and protease supplementation on apparent (ileal and overall) digestibility of nutrients of five hulless barley varieties in young pigs. Livestock Production Science 71, 109-120.
Yin, Q.Q., Zheng, Q.H., Kang, X.T., 2007. Biochemical characteristics of phytases from fungi and the transformed microorganism. Animal Feed Science and Technology 132, 341-350.
Yoon, S.J., Choi, Y.J., Min, H.K., Cho, K.K., Kim, J.W., Lee, S.C., Jung, Y.H., 1996. Isolation and identification of phytase-producing bacterium, Enterobacter sp. 4, and enzymatic properties of phytase enzyme. Enzyme and Microbial Technology 18, 449-454.
Zinin, N.V., Serkina, A.V., Gelfand, M.S., Shevelev, A.B., Sineoky, S.P., 2004. Gene cloning, expression and characterization of novel phytase from Obesumbacterium proteus. FEMS Microbiology Letters 236, 283-290.
Zhang, L., An, L., Gao, X., Wang, Y., 2005. Properties of A. ficuum AS3.324 phytase expressed in tobacco. Process Biochemistry 40, 213-216.
Zhang, L., Wang, Y., Zhang, C., Wang, Y., Zhu, D., Wang, C., Nagata, S., 2006. Supplementation effect of ectoine on thermostability of phytase. Journal of Bioscience and Bioengineering 102, 560-563.
Zhao, D.M., Wang, M., Mu, X.J., Sun, M.L., Wang, X.Y., 2007. Screening, cloning and overexpression of Aspergillus niger phytase (phyA) in Pichia pastoris with favourable characteristics. Letters in applied microbiology 45, 522-528.
Zhao, Q., Liu, H., Zhang, Y., Zhang, Y., 2010. Engineering of protease-resistant phytase from Penicillium sp.: High thermal stability, low optimal temperature and pH. Journal of Bioscience and Bioengineering 110, 638-645.