Phytase: Source, Structure and Application

Lei, Xin Gen; Porres, Jesús M.; Mullaney, Edward J.; Brinch-Pedersen, Henrik

doi:10.1007/1-4020-5377-0_29

Cited by 81 publications

(103 citation statements)

References 121 publications

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“…A number of enzymes with phytase activity are known from plants, animals, and microorganisms (Dvoráková, 1998). They are classified according to their catalytic mechanism as belonging to the histidine acid phosphatases (HAPs), purple acid phosphatases (PAPs), Cys phosphatases, or b-propeller phosphatases (Lei et al, 2007). Each group consists of several phosphatases, but only a few of them have phytase activity.…”

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Cloning and Characterization of Purple Acid Phosphatase Phytases from Wheat, Barley, Maize, and Rice

et al. 2011

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Barley (Hordeum vulgare) and wheat (Triticum aestivum) possess significant phytase activity in the mature grains. Maize (Zea mays) and rice (Oryza sativa) possess little or virtually no preformed phytase activity in the mature grain and depend fully on de novo synthesis during germination. Here, it is demonstrated that wheat, barley, maize, and rice all possess purple acid phosphatase (PAP) genes that, expressed in Pichia pastoris, give fully functional phytases (PAPhys) with very similar enzyme kinetics. Preformed wheat PAPhy was localized to the protein crystalloid of the aleurone vacuole. Phylogenetic analyses indicated that PAPhys possess four conserved domains unique to the PAPhys. In barley and wheat, the PAPhy genes can be grouped as PAPhy_a or PAPhy_b isogenes (barley, HvPAPhy_a, HvPAPhy_b1, and HvPAPhy_b2; wheat, TaPAPhy_a1, TaPAPhy_a2, TaPAPhy_b1, and TaPAPhy_b2). In rice and maize, only the b type (OsPAPhy_b and ZmPAPhy_b, respectively) were identified. HvPAPhy_a and HvPAPhy_b1/b2 share 86% and TaPAPhya1/a2 and TaPAPhyb1/b2 share up to 90% (TaPAPhy_a2 and TaPAPhy_b2) identical amino acid sequences. despite of this, PAPhy_a and PAPhy_b isogenes are differentially expressed during grain development and germination. In wheat, it was demonstrated that a and b isogene expression is driven by different promoters (approximately 31% identity). TaPAPhy_a/b promoter reporter gene expression in transgenic grains and peptide mapping of TaPAPhy purified from wheat bran and germinating grains confirmed that the PAPhy_a isogene set present in wheat/barley but not in rice/maize is the origin of high phytase activity in mature grains.

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“…The HAPs constitute a large group of enzymes that share the catalytic mechanism as an N-terminal RHGXRXP motif and a C-terminal HD motif position together and form the active site (Lei et al, 2007). The PAPs are metallohydrolases that bind two metal ions in the active center.…”

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Cloning and Characterization of Purple Acid Phosphatase Phytases from Wheat, Barley, Maize, and Rice

et al. 2011

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“…1.3.8,EC 3.1.3.26,and EC 3.1.3.72) catalyze the release of phosphate from phytates present in plant protein sources making P and other minerals available (Lei, Porres, Mullaney, & Brinch-Pedersen, 2007). At present, phytases are grouped into four major classes: histidine acid, β-propeller, cysteine, and purple acid phytases.…”

Section: Introductionmentioning

confidence: 99%

“…Several β-propeller phytases, one from B. subtilis (Guerrero-Olazarán, Rodríguez-Blanco, Carreon-Treviño, Gallegos-López, Viader-Salvadó, 2010), and others designed by a structure-guided consensus approach, have been produced by the methylotrophic yeast P. pastoris (Viader-Salvadó, Gallegos-López, Carreón-Treviño, Castillo-Galván, Rojo-Domínguez, & Guerrero-Olazarán, 2010). Therefore, during the last two decades, optimizing plant-based diets using phytase as a feed additive has been a way to reduce phytates' antinutritional effect (Fox, Lawrence, Saccardi, Davis, Ricque-Marie, Cruz-Suarez, & Samocha 2006;Lei et al, 2007;Lim & Lee, 2009), thereby improving the absorption and retention of minerals and amino acids (Rebollar and Mateos, 1999;Gómez-Villalva, 2005), and enhancing the activity of proteolytic enzymes, survival rate, and weight gain (Ricque-Marie, Cruz-Suarez, Zavala-Chavez, Nieto-Lopez, Guajardo, Tapia-Salazar, McCallum, & Newkirk, 2004;Cao, Ye, Wang, & Guo, 2010;Wang, Yang, Han, Dong, Yang, & Zou, 2009;Gamboa, Aguilera, Gaxiola, Cuzon, Guerrero, & López, 2011). The digestive tract of shrimp has a pH range of 6-8, hence FTEII is a good alternative for either pretreatment with fresh water added to meals or direct inclusion in shrimp feed.…”

Section: Introductionmentioning

confidence: 99%

Effect of Beta-propeller Phytase from Pichia pastoris on Energy Partition in Juvenile Litopenaeus vannamei Fed a Plant Protein-Based Diet

Gamboa¹,

Cuzon²,

Guerrero-Olazarán³

et al. 2016

IJB

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The main objective of this study was to evaluate the effect of a new isolated exogenous β-propeller phytase (FTEII) obtained from Pichia pastoris, on growth, survival and energy partition of juveniles of Litopenaeus vannamei fed a plant protein diet. Two treatments were designed for the experiment: a plant protein-based diet without phytase (T1), and a diet comprising pretreated plant protein with β-propeller phytase (T2). The gowth rate monitored over 30 days significantly improved when phytase was added to the diet (T2) compared to control T1 (p<0.05), and survival rates were similar between treatments (p>0.05). Energy partitioning was affected by basal metabolism (HeE) which was similar in both dietary treatments (p> 0.05) but the heat increment of feeding (HiE) was higher with T1 than T2 (p<0.05), whereas retained energy (RE) increased in T2 compared to T 1 (p<0.05). In summary, exogenous phytase added to a plant protein-based diet decreased the negative effect of phytic acid, released phosphorus, and therefore improved weight gain.

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“…Based on amino-acid sequence comparison, phytases can be classified into four classes: histidine acid phosphatase (HAP), purple acid phosphatase (PAP), -propeller phytase (BPP) and cysteine phosphatase (CP) (Lei et al, 2007). A typical BPP has a six-bladed propeller fold with two phosphate-binding sites (a cleavage site and an affinity site) and six calcium-binding sites, three of which are highaffinity binding sites responsible for enzyme stability and the other three of which are low-affinity sites regulating the catalytic activity of the enzyme (Fu et al, 2008;Kim et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

Preparation, purification, crystallization and preliminary crystallographic analysis of dual-domain β-propeller phytase fromBacillussp. HJB17

Liu

Guo

et al. 2014

Acta Cryst Sect F

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-Propeller phytases (BPPs) are abundant in nature. Recently, dual-domain BPPs have been found in which the typical BPP domain is responsible for phytate hydrolysis. The dual-domain BPP (PhyH) from Bacillus sp. HJB17 was obtained with an incomplete N-terminal BPP domain (PhyH-DI; residues 41-318) and a typical BPP domain (PhyH-DII; residues 319-644) at the C-terminus. PhyH-DI was found to act synergistically (with a 1.2-2.5-fold increase in phosphate release) with PhyH-DII, other BPPs (PhyP and 168PhyA) and a histidine acid phosphatase. The structure of PhyH was therefore studied with the aim of explaining these functions. PhyH with the secreted signal peptide of the first 40 amino acids deleted (PhyHT) was cloned and expressed in Escherichia coli. Purified and active PhyHT protein was obtained by refolding from the precipitant. PhyHT was crystallized using the vapour-diffusion method. The crystal grew in a condition consisting of 0.2 M sodium acetate trihydrate, 0.1 M Tris-HCl pH 9.5, 25%(w/v) polyethylene glycol 4000 using 1 mg ml À1 protein solution at 289 K. A complete data set was collected from a crystal to 2.85 Å resolution using synchrotron radiation at 100 K. The crystal belonged to space group P12 1 1, with unit-cell parameters a = 46.82, b = 140.19, c = 81.94 Å , = 90.00, = 92.00, = 90.00 . The asymmetric unit was estimated to contain one molecule of PhyHT.

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Phytase: Source, Structure and Application

Cited by 81 publications

References 121 publications

Cloning and Characterization of Purple Acid Phosphatase Phytases from Wheat, Barley, Maize, and Rice

Cloning and Characterization of Purple Acid Phosphatase Phytases from Wheat, Barley, Maize, and Rice

Effect of Beta-propeller Phytase from Pichia pastoris on Energy Partition in Juvenile Litopenaeus vannamei Fed a Plant Protein-Based Diet

Preparation, purification, crystallization and preliminary crystallographic analysis of dual-domain β-propeller phytase fromBacillussp. HJB17

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