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Please use this identifier to cite or link to this item: http://hdl.handle.net/1843/45351
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dc.creatorMariana Sousa Vieirapt_BR
dc.creatorVinícius Valim Pereirapt_BR
dc.creatorAlice da Cunha Morales Álvarespt_BR
dc.creatorLais Moreira Nogueirapt_BR
dc.creatorWilliam James Nogueira Limapt_BR
dc.creatorPaulo Afonso Granjeiropt_BR
dc.creatorDaniel Bonoto Gonçalvespt_BR
dc.creatorMariana Campos da Paz Lopespt_BR
dc.creatorSonia Maria de Freitaspt_BR
dc.creatorAlexsandro Sobreira Galdinopt_BR
dc.date.accessioned2022-09-21T15:19:15Z-
dc.date.available2022-09-21T15:19:15Z-
dc.date.issued2019-
dc.citation.volume10pt_BR
dc.citation.issue2pt_BR
dc.citation.spage131pt_BR
dc.citation.epage139pt_BR
dc.identifier.doi10.2174/2212798410666181205114153pt_BR
dc.identifier.issn1876-1429pt_BR
dc.identifier.urihttp://hdl.handle.net/1843/45351-
dc.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.pt_BR
dc.description.sponsorshipFAPEMIG - Fundação de Amparo à Pesquisa do Estado de Minas Geraispt_BR
dc.description.sponsorshipOutra Agênciapt_BR
dc.languageengpt_BR
dc.publisherUniversidade Federal de Minas Geraispt_BR
dc.publisher.countryBrasilpt_BR
dc.publisher.departmentICA - INSTITUTO DE CIÊNCIAS AGRÁRIASpt_BR
dc.publisher.initialsUFMGpt_BR
dc.relation.ispartofRecent Patents on Food, Nutrition and Agriculturept_BR
dc.rightsAcesso Restritopt_BR
dc.subject.otherYersíniapt_BR
dc.subject.otherCinética enzimáticapt_BR
dc.subject.otherÁcido fítico - Efeito fisiológicopt_BR
dc.subject.otherEscherichia colipt_BR
dc.titleExpression and biochemical characterization of a Yersinia intermedia phytase expressed in Escherichia colipt_BR
dc.typeArtigo de Periódicopt_BR
dc.url.externahttps://www.eurekaselect.com/article/95031pt_BR
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