Sunflower Protein Hydrolysates Reduce Cholesterol Micellar Solubility |
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Authors: | Cristina Megías Justo Pedroche María del Mar Yust Manuel Alaiz Julio Girón-Calle Francisco Millán Javier Vioque |
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Institution: | (1) Instituto de la Grasa (C.S.I.C.), Padre García Tejero 4, 41012 Sevilla, Spain |
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Abstract: | Plant protein hydrolysates are a source of bioactive peptides. There are peptides that decrease the micellar cholesterol solubility
from bile acids and therefore may reduce in vivo cholesterol absorption. The presence of these peptides in sunflower protein hydrolysates has been studied. Sunflower protein
hydrolysates produced with alcalase plus flavourzyme or with pepsin plus pancreatin inhibited in some degree the cholesterol
incorporation to micelles. Protein hydrolysates generated after 30 min of hydrolysis with alcalase, and after 30 min of hydrolysis
with pepsin, were the inhibitoriest of the cholesterol incorporation to micelles. The average amino acid hydrophobicity of
inhibitory peptides in cholesterol micelles was higher than the observed in the corresponding protein hydrolysates. This high
hydrophobicity probably favours their inclusion in the lipid micelles. In vivo, this inhibition may translate in a decrease of cholesterol absorption. Reported results show that a combination of different
characteristics such as peptide size or hydrophobicity may be responsible of the inhibitory activity of generated peptides. |
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Keywords: | Sunflower Protein hydrolysate Bioactive peptides Cholesterol solubility |
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