Extraction, purification and characterization of inhibitor of trypsin from Chenopodium quinoa seeds
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 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 °C) and reducing agents.
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Sociedade Brasileira de Ciência e Tecnologia de Alimentos
2015
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oai:scielo:S0101-206120150004005882015-12-21Extraction, purification and characterization of inhibitor of trypsin from Chenopodium quinoa seedsPesoti,Aline RegieleOliveira,Bruno Menezes deOliveira,Augusto Cesar dePompeu,Dávia GuimarãesGonçalves,Daniel BonotoMarangoni,SérgioSilva,José Antonio daGranjeiro,Paulo Afonso purification characterization inhibitor of trypsin Chenopodium quinoa seeds 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 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 °C) and reducing agents.info:eu-repo/semantics/openAccessSociedade Brasileira de Ciência e Tecnologia de AlimentosFood Science and Technology v.35 n.4 20152015-12-01info:eu-repo/semantics/articletext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612015000400588en10.1590/1678-457X.6655 |
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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 |
| spellingShingle |
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 Extraction, purification and characterization of inhibitor of trypsin from Chenopodium quinoa seeds |
| author_facet |
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 |
| author_sort |
Pesoti,Aline Regiele |
| title |
Extraction, purification and characterization of inhibitor of trypsin from Chenopodium quinoa seeds |
| title_short |
Extraction, purification and characterization of inhibitor of trypsin from Chenopodium quinoa seeds |
| title_full |
Extraction, purification and characterization of inhibitor of trypsin from Chenopodium quinoa seeds |
| title_fullStr |
Extraction, purification and characterization of inhibitor of trypsin from Chenopodium quinoa seeds |
| title_full_unstemmed |
Extraction, purification and characterization of inhibitor of trypsin from Chenopodium quinoa seeds |
| title_sort |
extraction, purification and characterization of inhibitor of trypsin from chenopodium quinoa seeds |
| description |
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 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 °C) and reducing agents. |
| publisher |
Sociedade Brasileira de Ciência e Tecnologia de Alimentos |
| publishDate |
2015 |
| url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612015000400588 |
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