Extraction, Purification And Characterization Of Inhibitor Of Trypsin From Chenopodium Quinoa Seeds

dc.creatorPesoti
dc.creatorAline Regiele; de Oliveira
dc.creatorBruno Menezes; de Oliveira
dc.creatorAugusto Cesar; Pompeu
dc.creatorDavia Guimaraes; Goncalves
dc.creatorDaniel Bonoto; Marangoni
dc.creatorSergio; da Silva
dc.creatorJose Antonio; Granjeiro
dc.creatorPaulo Afonso
dc.date2015-OCT-DEC
dc.date2016-06-07T13:20:27Z
dc.date2016-06-07T13:20:27Z
dc.date.accessioned2018-03-29T01:40:28Z
dc.date.available2018-03-29T01:40:28Z
dc.identifier
dc.identifierExtraction, Purification And Characterization Of Inhibitor Of Trypsin From Chenopodium Quinoa Seeds. Soc Brasileira Ciencia Tecnologia Alimentos, v. 35, p. 588-597 OCT-DEC-2015.
dc.identifier0101-2061
dc.identifierWOS:000367390300002
dc.identifier10.1590/1678-457X.6655
dc.identifierhttp://www.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612015000400588&lng=en&nrm=iso&tlng=en
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/242889
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1306587
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionA novel trypsin inhibitor of protease (CqTI) was purified from Chenopodium quinoa seeds. The optimal extracting solvent was 0.1M NaCl pH 6.8 (p < 0.05). The extraction time of 5h and 90 degrees C was optimum for the recovery of the trypsin inhibitor from C. quinoa seeds. The purification occurred in gel-filtration and reverse phase chromatography. CqTI presented active against commercial bovine trypsin and chymotrypsin and had a specific activity of 5,033.00 (TIU/mg), which was purified to 333.5-fold. The extent of purification was determined by SDS-PAGE. CqTI had an apparent molecular weight of approximately 12KDa and two bands in reduced conditions as determined by Tricine-SDS-PAGE. MALDI-TOF showed two peaks in 4,246.5 and 7,908.18m/z. CqTI presented high levels of essential amino acids. N-terminal amino acid sequence of this protein did not show similarity to any known protease inhibitor. Its activity was stable over a pH range (2-12), temperatures range (20-100 degrees C) and reducing agents.
dc.description35
dc.description4
dc.description
dc.description588
dc.description597
dc.descriptionFundação de Amparo à Pesquisa do Estado de Minas Gerais (FAPEMIG)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description
dc.description
dc.description
dc.languageen
dc.publisherSOC BRASILEIRA CIENCIA TECNOLOGIA ALIMENTOS
dc.publisher
dc.publisherCAMPINAS
dc.relationFOOD SCIENCE AND TECHNOLOGY
dc.rightsfechado
dc.sourceWOS
dc.subjectBowman-birk Inhibitor
dc.subjectProtease Inhibitor
dc.subjectGut Proteinases
dc.subjectCell Lines
dc.subjectSystems
dc.subjectWilld.
dc.titleExtraction, Purification And Characterization Of Inhibitor Of Trypsin From Chenopodium Quinoa Seeds
dc.typeArtículos de revistas


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