ANTI-TRYPTIC ACTIVITY IN SEED AND FOOD PRODUCT OF CHIA (SALVIA HISPANICA L.)

Authors

  • Ana Paula Araújo de Souza Curso de Nutrição, Centro de Ciências da Saúde, Universidade Federal do Rio Grande do Norte, Natal - RN, Brasil.
  • Lorena Maria Araújo Marinheiro Nascimento Curso de Nutrição, Centro de Ciências da Saúde, Universidade Federal do Rio Grande do Norte, Natal - RN, Brasil.
  • Vanessa Cristina Oliveira de Lima Programa de Pós graduação em Bioquímica, Centro de Biociências, Universidade Federal do Rio Grande do Norte, Natal, RN, Brasil.
  • Fabiana Maria Coimbra de Carvalho Programa de Pós graduação em Bioquímica, Centro de Biociências, Universidade Federal do Rio Grande do Norte, Natal, RN, Brasil.
  • Elizeu Antunes dos Santos Departamento de Bioquímica, Centro de Biociências, Universidade Federal do Rio Grande do Norte, Natal - RN, Brasil Programa de Pós graduação em Bioquímica, Centro de Biociências, Universidade Federal do Rio Grande do Norte, Natal, RN, Brasil.
  • Ana Heloneida de Araújo Morais Departamento de Nutrição, Centro de Ciências da Saúde, Universidade Federal do Rio Grande do Norte, Natal - RN, Brasil. Programa de Pós Graduação em Nutrição, Centro de Biociências, Universidade Federal do Rio Grande do Norte, Natal - RN, Brasil.

DOI:

https://doi.org/10.12957/demetra.2017.25636

Keywords:

Flour. Protein. Enzyme Inhibitors. Trypsin.

Abstract

Objective: This study has aimed to detect anti-tryptic activity in commercial chia seeds and flour and to isolate a trypsin inhibitor present in the seeds. Methodology: Protein extraction, ammonium sulfate fractionation, affinity chromatography, trypsin inhibition assay, protein quantification and sodium dodecyl sulfate polyacrylamide gel electrophoresis were performed. Results and discussion: From the retained protein peak in the affinity column, 51% and 64% of anti-tryptic activity for chia flour and seeds were respectively found. Large amounts of soluble proteins were not observed in the retained protein peaks of both chia seeds and flour when compared to the crude extract and protein fractions. The trypsin inhibitor in the seeds was isolated, with an estimated molecular mass of approximately 14.4 kDa. Conclusions: In view of the unprecedented results regarding the detection of anti-tryptic activity in commercial chia seeds and flour and isolation of the inhibitor in the seeds, further research is needed on this new molecule, regarding its bioactive properties and safe consumption.

DOI: 10.12957/demetra.2017.25636

 

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Published

2017-03-03

How to Cite

1.
Souza APA de, Nascimento LMAM, Lima VCO de, Carvalho FMC de, Santos EA dos, Morais AH de A. ANTI-TRYPTIC ACTIVITY IN SEED AND FOOD PRODUCT OF CHIA (SALVIA HISPANICA L.). DEMETRA [Internet]. 2017 Mar. 3 [cited 2025 Jul. 27];12(1):319-31. Available from: https://www.e-publicacoes.uerj.br/demetra/article/view/25636

Issue

Vol. 12 No. 1 (2017)

Section

FREE THEMED ARTICLES

License

 

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