期刊
FOOD SCIENCE AND TECHNOLOGY
卷 35, 期 4, 页码 588-597出版社
SOC BRASILEIRA CIENCIA TECNOLOGIA ALIMENTOS
DOI: 10.1590/1678-457X.6655
关键词
purification; characterization; inhibitor of trypsin; Chenopodium quinoa; seeds
资金
- Fundacao de Amparo a Pesquisa do Estado de Minas Gerais (FAPEMIG)
- Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (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.
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