Publicação:
Characterization of the Catalytic Structure of Plant Phytase, Protein Tyrosine Phosphatase-Like Phytase, and Histidine Acid Phytases and Their Biotechnological Applications

dc.contributor.authorCangussu, Alex Sander Rodrigues
dc.contributor.authorAires Almeida, Deborah
dc.contributor.authorAguiar, Raimundo Wagner De Souza
dc.contributor.authorBordignon-Junior, Sidnei Emilio [UNESP]
dc.contributor.authorViana, Kelvinson Fernandes
dc.contributor.authorBarbosa, Luiz Carlos Bertucci
dc.contributor.authorCangussu, Edson Wagner Da Silva
dc.contributor.authorBrandi, Igor Viana
dc.contributor.authorPortella, Augustus Caeser Franke
dc.contributor.authorSantos, Gil Rodrigues Dos
dc.contributor.authorSobrinho, Eliane Macedo
dc.contributor.authorLima, William James Nogueira
dc.contributor.institutionUniversidade Federal Do Tocantins
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)
dc.contributor.institutionUniversidade Federal da Integração Latino-Americana
dc.contributor.institutionUniversidade Federal de Itajubá
dc.contributor.institutionUniversidade Estadual de Montes Claros
dc.contributor.institutionUniversidade Federal de Minas Gerais (UFMG)
dc.contributor.institutionInstituto Federal Do Norte Minas Gerais
dc.date.accessioned2022-04-28T19:08:50Z
dc.date.available2022-04-28T19:08:50Z
dc.date.issued2018-01-01
dc.description.abstractPhytase 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 β-sheets and α-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.en
dc.description.affiliationEngenharia de Bioprocessos e Biotecnologia e Programa de Pos-Graduação em Biotecnologia Universidade Federal Do Tocantins
dc.description.affiliationEngenharia e Ciências de Alimentos Universidade Estadual Paulista
dc.description.affiliationLaboratório de Biologia Molecular e Bioquímica-ICVN Universidade Federal da Integração Latino-Americana
dc.description.affiliationEngenharia de Bioprocessos e Biotecnologia Instituto de Recursos Naturais Universidade Federal de Itajubá
dc.description.affiliationFaculdade de Medicina Universidade Estadual de Montes Claros
dc.description.affiliationInstituto de Ciências Agrárias Universidade Federal de Minas Gerais
dc.description.affiliationInstituto Federal Do Norte Minas Gerais
dc.description.affiliationUnespEngenharia e Ciências de Alimentos Universidade Estadual Paulista
dc.identifierhttp://dx.doi.org/10.1155/2018/8240698
dc.identifier.citationEnzyme Research, v. 2018.
dc.identifier.doi10.1155/2018/8240698
dc.identifier.issn2090-0414
dc.identifier.issn2090-0406
dc.identifier.scopus2-s2.0-85045065915
dc.identifier.urihttp://hdl.handle.net/11449/221054
dc.language.isoeng
dc.relation.ispartofEnzyme Research
dc.sourceScopus
dc.titleCharacterization of the Catalytic Structure of Plant Phytase, Protein Tyrosine Phosphatase-Like Phytase, and Histidine Acid Phytases and Their Biotechnological Applicationsen
dc.typeResenha
dspace.entity.typePublication
unesp.author.orcid0000-0003-2664-8027[1]
unesp.author.orcid0000-0003-2879-0254[4]

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