Literature DB >> 17364542

In vitro and in vivo characteristics of bacterial phytases and their efficacy in broiler chickens.

E A I Elkhalil1, K Männer, R Borriss, O Simon.   

Abstract

1. Three bacterial phytases derived from Bacillus, Escherichia coli or Klebsiella were compared with a phytase derived from Aspergillus niger in vitro and in vivo. 2. The in vitro results indicated that Aspergillus, E. coli and Klebsiella phytase displayed their activity optima in an acid pH range while Bacillus phytase did so in neutral pH. 3. The trials also revealed that only Bacillus phytase is more resistant to heat treatments, while E. coli and Klebsiella phytases are more stable against proteolytic inactivation. 4. In vivo phytases derived from Aspergillus, Bacillus, E. coli, Klebsiella or a combination of Bacillus and E. coli improved the utilisation of phosphorus (P balance) significantly to 0.54, 0.54, 0.55, 0.55 or 0.58, respectively, compared to 0.42 in the negative control. 5. The phytases used in this study seemed to be equally effective in improving P utilisation regardless of proposed intestinal site of activity. Combination of phytases acting in the gizzard with phytases acting in the intestine seems to be a promising way to further improving in vivo efficacy of phytases in poultry.

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Year:  2007        PMID: 17364542     DOI: 10.1080/00071660601148195

Source DB:  PubMed          Journal:  Br Poult Sci        ISSN: 0007-1668            Impact factor:   2.095


  7 in total

1.  Gene cloning and characterization of a thermostable phytase from Bacillus subtilis US417 and assessment of its potential as a feed additive in comparison with a commercial enzyme.

Authors:  Ameny Farhat; Hichem Chouayekh; Mounira Ben Farhat; Kameleddine Bouchaala; Samir Bejar
Journal:  Mol Biotechnol       Date:  2008-06-10       Impact factor: 2.695

2.  Rational design-based engineering of a thermostable phytase by site-directed mutagenesis.

Authors:  Azita Fakhravar; Ardeshir Hesampour
Journal:  Mol Biol Rep       Date:  2018-09-08       Impact factor: 2.316

3.  Computational-based structural, functional and phylogenetic analysis of Enterobacter phytases.

Authors:  Krishnendu Pramanik; Shreyasi Kundu; Sandipan Banerjee; Pallab Kumar Ghosh; Tushar Kanti Maiti
Journal:  3 Biotech       Date:  2018-05-19       Impact factor: 2.406

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

Authors:  Aliya D Suleimanova; Astrid Beinhauer; Liia R Valeeva; Inna B Chastukhina; Nelly P Balaban; Eugene V Shakirov; Ralf Greiner; Margarita R Sharipova
Journal:  Appl Environ Microbiol       Date:  2015-07-24       Impact factor: 4.792

5.  Heterologous expression and optimization using experimental designs allowed highly efficient production of the PHY US417 phytase in Bacillus subtilis 168.

Authors:  Ameny Farhat-Khemakhem; Mounira Ben Farhat; Ines Boukhris; Wacim Bejar; Kameleddine Bouchaala; Radhouane Kammoun; Emmanuelle Maguin; Samir Bejar; Hichem Chouayekh
Journal:  AMB Express       Date:  2012-01-26       Impact factor: 3.298

6.  Hydrolysis of phytate and formation of inositol phosphate isomers without or with supplemented phytases in different segments of the digestive tract of broilers.

Authors:  Ellen Zeller; Margit Schollenberger; Imke Kühn; Markus Rodehutscord
Journal:  J Nutr Sci       Date:  2015-01-26

7.  Heterologous Expression of Secreted Bacterial BPP and HAP Phytases in Plants Stimulates Arabidopsis thaliana Growth on Phytate.

Authors:  Lia R Valeeva; Chuluuntsetseg Nyamsuren; Margarita R Sharipova; Eugene V Shakirov
Journal:  Front Plant Sci       Date:  2018-02-20       Impact factor: 5.753

  7 in total

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