Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/242889
Type: Artigo
Title: Extraction, purification and characterization of inhibitor of trypsin from Chenopodium quinoa seeds
Author: Pesoti, Aline Regiele
Oliveira, Bruno Menezes de
Oliveira, Augusto César 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 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.
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
Subject: Eletroforese em gel de poliacrilamida
Quinoa
Inibidores da tripsina
Sequência de aminoácidos
Sementes
Country: Brasil
Editor: Sociedade Brasileira de Ciencia e Tecnologia de Alimentos
Citation: 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.
Rights: aberto
Identifier DOI: 10.1590/1678-457X.6655
Address: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612015000400588
Date Issue: 2015
Appears in Collections:IB - Artigos e Outros Documentos

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