Extraction, purification and characterization of inhibitor of trypsin from Chenopodium quinoa seeds

dc.creatorAline Regiele Pesoti
dc.creatorBruno Menezes de Oliveira
dc.creatorAugusto Cesar de Oliveira
dc.creatorDávia Guimarães Pompeu
dc.creatorDaniel Bonoto Gonçalves
dc.creatorSérgio Marangoni
dc.creatorJosé Antonio da Silva
dc.creatorPaulo Afonso Granjeiro
dc.date2015
dc.date.accessioned2026-07-07T04:19:00Z
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 °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.
dc.formatapplication/pdf
dc.identifier0101-2061
dc.identifierhttps://www.redalyc.org/articulo.oa?id=395943288002
dc.identifier.urihttp://hdl.handle.net/123456789/457592
dc.languageen
dc.publisherSociedade Brasileira de Ciência e Tecnologia de Alimentos
dc.relationhttp://www.redalyc.org/revista.oa?id=3959
dc.rightsCiência e Tecnologia de Alimentos
dc.sourceCiência e Tecnologia de Alimentos (Brasil) Num.4 Vol.35
dc.subjectAgrociencias
dc.titleExtraction, purification and characterization of inhibitor of trypsin from Chenopodium quinoa seeds
dc.typeartículo científico

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