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Sunflower Protein Hydrolysates Reduce Cholesterol Micellar Solubility
Authors:Cristina Megías  Justo Pedroche  María del Mar Yust  Manuel Alaiz  Julio Girón-Calle  Francisco Millán  Javier Vioque
Institution:(1) Instituto de la Grasa (C.S.I.C.), Padre García Tejero 4, 41012 Sevilla, Spain
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.
Keywords:Sunflower  Protein hydrolysate  Bioactive peptides  Cholesterol solubility
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