Expression and biochemical characterization of a Yersinia intermedia phytase expressed in Escherichia coli

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dc.creatorMariana Sousa Vieira
dc.creatorVinícius Valim Pereira
dc.creatorAlice da Cunha Morales Álvares
dc.creatorLais Moreira Nogueira
dc.creatorWilliam James Nogueira Lima
dc.creatorPaulo Afonso Granjeiro
dc.creatorDaniel Bonoto Gonçalves
dc.creatorMariana Campos da Paz Lopes
dc.creatorSonia Maria de Freitas
dc.creatorAlexsandro Sobreira Galdino
dc.date.accessioned2022-09-21T15:19:15Z
dc.date.accessioned2025-09-09T01:26:05Z
dc.date.available2022-09-21T15:19:15Z
dc.date.issued2019
dc.description.sponsorshipFAPEMIG - Fundação de Amparo à Pesquisa do Estado de Minas Gerais
dc.description.sponsorshipOutra Agência
dc.identifier.doi10.2174/2212798410666181205114153
dc.identifier.issn1876-1429
dc.identifier.urihttps://hdl.handle.net/1843/45351
dc.languageeng
dc.publisherUniversidade Federal de Minas Gerais
dc.relation.ispartofRecent Patents on Food, Nutrition and Agriculture
dc.rightsAcesso Restrito
dc.subjectYersínia
dc.subjectCinética enzimática
dc.subjectÁcido fítico - Efeito fisiológico
dc.subjectEscherichia coli
dc.titleExpression and biochemical characterization of a Yersinia intermedia phytase expressed in Escherichia coli
dc.typeArtigo de periódico
local.citation.epage139
local.citation.issue2
local.citation.spage131
local.citation.volume10
local.description.resumoBackground: phytases are enzymes capable of degrading phytic acid and used in animal feed supplementation in order to improve digestibility through the release of minerals such as phosphorus. Objective: the main goal of this study was to express and characterize a Yersinia intermedia phytase expressed in Escherichia coli cells. Methods: the Y. intermedia phytase gene was synthesized and overexpressed in Escherichia coli cells. The phytase recombinante (rPHY) was purified to homogeneity using a Ni-NTA column. The biochemical and biophysical properties of the rPHY were measured in order to fully characterize the recombinant enzyme. The following patents database were consulted: Espacenet, USPTO, LATIPAT, Patent Scope, WIPO and Google Patents. Results: the results showed that the rPHY is active at 37-40ºC and presented an optimal pH and temperature of 8.0 and 40°C, respectively. The phytase rPHY was activated by Cu2+ ion and showed resistance to trypsin and pepsin, retaining 55% of the activity at the ratio of 0.02. Furthermore, the dissociation constant (Kd = 1.1150 ± 0.0087 mM), as estimated by a fluorescence binding assay, suggests a medium affinity of the enzyme with the substrate. Conclusion: the results of this article can be considered as innovative and for this reason, they were protected by Intellectual Property Law in Brazil. Take together, the biochemical properties of the rPHY could be useful in future for its industrial application of this enzyme as an additive in the monogastric feed.
local.publisher.countryBrasil
local.publisher.departmentICA - INSTITUTO DE CIÊNCIAS AGRÁRIAS
local.publisher.initialsUFMG
local.url.externahttps://www.eurekaselect.com/article/95031

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