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| Pesoti,Aline Regiele; Oliveira,Bruno Menezes de; Oliveira,Augusto Cesar de; Pompeu,Dávia Guimarães; Gonçalves,Daniel Bonoto; Marangoni,Sérgio; Silva,José Antonio da; Granjeiro,Paulo Afonso. |
| Abstract 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 °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... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Purification; Characterization; Inhibitor of trypsin; Chenopodium quinoa; Seeds. |
| Ano: 2015 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612015000400588 |
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