Artículos de revistas
Extraction, Purification And Characterization Of Inhibitor Of Trypsin From Chenopodium Quinoa Seeds
Registro en:
Extraction, Purification And Characterization Of Inhibitor Of Trypsin From Chenopodium Quinoa Seeds. Soc Brasileira Ciencia Tecnologia Alimentos, v. 35, p. 588-597 OCT-DEC-2015.
0101-2061
WOS:000367390300002
10.1590/1678-457X.6655
Autor
Pesoti
Aline Regiele; de Oliveira
Bruno Menezes; de Oliveira
Augusto Cesar; Pompeu
Davia Guimaraes; Goncalves
Daniel Bonoto; Marangoni
Sergio; da Silva
Jose Antonio; Granjeiro
Paulo Afonso
Institución
Resumen
Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) A 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. 35 4
588 597 Fundação de Amparo à Pesquisa do Estado de Minas Gerais (FAPEMIG) Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)