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- Title
Characterization of the Catalytic Structure of Plant Phytase, Protein Tyrosine Phosphatase-Like Phytase, and Histidine Acid Phytases and Their Biotechnological Applications.
- Authors
Cangussu, Alex Sander Rodrigues; Aires Almeida, Deborah; Aguiar, Raimundo Wagner de Souza; Bordignon-Junior, Sidnei Emilio; Viana, Kelvinson Fernandes; Barbosa, Luiz Carlos Bertucci; Cangussu, Edson Wagner da Silva; Brandi, Igor Viana; Portella, Augustus Caeser Franke; Santos, Gil Rodrigues dos; Sobrinho, Eliane Macedo; Lima, William James Nogueira
- Abstract
Phytase plays a prominent role in monogastric animal nutrition due to its ability to improve phytic acid digestion in the gastrointestinal tract, releasing phosphorus and other micronutrients that are important for animal development. Moreover, phytase decreases the amounts of phytic acid and phosphate excreted in feces. Bioinformatics approaches can contribute to the understanding of the catalytic structure of phytase. Analysis of the catalytic structure can reveal enzymatic stability and the polarization and hydrophobicity of amino acids. One important aspect of this type of analysis is the estimation of the number of <italic>β</italic>-sheets and <italic>α</italic>-helices in the enzymatic structure. Fermentative processes or genetic engineering methods are employed for phytase production in transgenic plants or microorganisms. To this end, phytase genes are inserted in transgenic crops to improve the bioavailability of phosphorus. This promising technology aims to improve agricultural efficiency and productivity. Thus, the aim of this review is to present the characterization of the catalytic structure of plant and microbial phytases, phytase genes used in transgenic plants and microorganisms, and their biotechnological applications in animal nutrition, which do not impact negatively on environmental degradation.
- Subjects
PLANT enzymes; PHYTASES; PROTEIN-tyrosine kinases; CATALYTIC activity; TRACE elements in animal nutrition; GASTROINTESTINAL system physiology
- Publication
Enzyme Research, 2018, p1
- ISSN
2090-0406
- Publication type
Article
- DOI
10.1155/2018/8240698