Angiotensin I-Converting Enzyme Inhibitory Peptides of Chia (Salvia hispanica) Produced by Enzymatic Hydrolysis
Synthetic angiotensin I-converting enzyme (ACE-I) inhibitors can have undesirable side effects, while natural inhibitors have no side effects and are potential nutraceuticals. A protein-rich fraction from chia (Salvia hispanica L.) seed was hydrolyzed with an Alcalase-Flavourzyme sequential system a...
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doaj-4d8b2bdda0cf4b30bc452ba59d4123552020-11-24T23:22:39ZengHindawi LimitedInternational Journal of Food Science2314-57652013-01-01201310.1155/2013/158482158482Angiotensin I-Converting Enzyme Inhibitory Peptides of Chia (Salvia hispanica) Produced by Enzymatic HydrolysisMaira Rubi Segura Campos0Fanny Peralta González1Luis Chel Guerrero2David Betancur Ancona3Facultad de Ingeniería Química, Universidad Autónoma de Yucatán, Periférico Norte. Km 33.5, Tablaje Catastral 13615, Colonia Chuburná de Hidalgo Inn, 97203 Mérida, YUC, MexicoFacultad de Ingeniería Química, Universidad Autónoma de Yucatán, Periférico Norte. Km 33.5, Tablaje Catastral 13615, Colonia Chuburná de Hidalgo Inn, 97203 Mérida, YUC, MexicoFacultad de Ingeniería Química, Universidad Autónoma de Yucatán, Periférico Norte. Km 33.5, Tablaje Catastral 13615, Colonia Chuburná de Hidalgo Inn, 97203 Mérida, YUC, MexicoFacultad de Ingeniería Química, Universidad Autónoma de Yucatán, Periférico Norte. Km 33.5, Tablaje Catastral 13615, Colonia Chuburná de Hidalgo Inn, 97203 Mérida, YUC, MexicoSynthetic angiotensin I-converting enzyme (ACE-I) inhibitors can have undesirable side effects, while natural inhibitors have no side effects and are potential nutraceuticals. A protein-rich fraction from chia (Salvia hispanica L.) seed was hydrolyzed with an Alcalase-Flavourzyme sequential system and the hydrolysate ultrafiltered through four molecular weight cut-off membranes (1 kDa, 3 kDa, 5 kDa, and 10 kDa). ACE-I inhibitory activity was quantified in the hydrolysate and ultrafiltered fractions. The hydrolysate was extensive (DH = 51.64%) and had 58.46% ACE-inhibitory activity. Inhibition ranged from 53.84% to 69.31% in the five ultrafiltered fractions and was highest in the <1 kDa fraction (69.31%). This fraction’s amino acid composition was identified and then it was purified by gel filtration chromatography and ACE-I inhibition measured in the purified fractions. Amino acid composition suggested that hydrophobic residues contributed substantially to chia peptide ACE-I inhibitory strength, probably by blocking angiotensin II production. Inhibitory activity ranged from 48.41% to 62.58% in the purified fractions, but fraction F1 (1.5–2.5 kDa) exhibited the highest inhibition (IC50 = 3.97 μg/mL; 427–455 mL elution volume). The results point out the possibility of obtaining bioactive peptides from chia proteins by means of a controlled protein hydrolysis using Alcalase-Flavourzyme sequentional system.http://dx.doi.org/10.1155/2013/158482 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Maira Rubi Segura Campos Fanny Peralta González Luis Chel Guerrero David Betancur Ancona |
spellingShingle |
Maira Rubi Segura Campos Fanny Peralta González Luis Chel Guerrero David Betancur Ancona Angiotensin I-Converting Enzyme Inhibitory Peptides of Chia (Salvia hispanica) Produced by Enzymatic Hydrolysis International Journal of Food Science |
author_facet |
Maira Rubi Segura Campos Fanny Peralta González Luis Chel Guerrero David Betancur Ancona |
author_sort |
Maira Rubi Segura Campos |
title |
Angiotensin I-Converting Enzyme Inhibitory Peptides of Chia (Salvia hispanica) Produced by Enzymatic Hydrolysis |
title_short |
Angiotensin I-Converting Enzyme Inhibitory Peptides of Chia (Salvia hispanica) Produced by Enzymatic Hydrolysis |
title_full |
Angiotensin I-Converting Enzyme Inhibitory Peptides of Chia (Salvia hispanica) Produced by Enzymatic Hydrolysis |
title_fullStr |
Angiotensin I-Converting Enzyme Inhibitory Peptides of Chia (Salvia hispanica) Produced by Enzymatic Hydrolysis |
title_full_unstemmed |
Angiotensin I-Converting Enzyme Inhibitory Peptides of Chia (Salvia hispanica) Produced by Enzymatic Hydrolysis |
title_sort |
angiotensin i-converting enzyme inhibitory peptides of chia (salvia hispanica) produced by enzymatic hydrolysis |
publisher |
Hindawi Limited |
series |
International Journal of Food Science |
issn |
2314-5765 |
publishDate |
2013-01-01 |
description |
Synthetic angiotensin I-converting enzyme (ACE-I) inhibitors can have undesirable side effects, while natural inhibitors have no side effects and are potential nutraceuticals. A protein-rich fraction from chia (Salvia hispanica L.) seed was hydrolyzed with an Alcalase-Flavourzyme sequential system and the hydrolysate ultrafiltered through four molecular weight cut-off membranes (1 kDa, 3 kDa, 5 kDa, and 10 kDa). ACE-I inhibitory activity was quantified in the hydrolysate and ultrafiltered fractions. The hydrolysate was extensive (DH = 51.64%) and had 58.46% ACE-inhibitory activity. Inhibition ranged from 53.84% to 69.31% in the five ultrafiltered fractions and was highest in the <1 kDa fraction (69.31%). This fraction’s amino acid composition was identified and then it was purified by gel filtration chromatography and ACE-I inhibition measured in the purified fractions. Amino acid composition suggested that hydrophobic residues contributed substantially to chia peptide ACE-I inhibitory strength, probably by blocking angiotensin II production. Inhibitory activity ranged from 48.41% to 62.58% in the purified fractions, but fraction F1 (1.5–2.5 kDa) exhibited the highest inhibition (IC50 = 3.97 μg/mL; 427–455 mL elution volume). The results point out the possibility of obtaining bioactive peptides from chia proteins by means of a controlled protein hydrolysis using Alcalase-Flavourzyme sequentional system. |
url |
http://dx.doi.org/10.1155/2013/158482 |
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