Journal
FOOD CHEMISTRY
Volume 379, Issue -, Pages -Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2022.132145
Keywords
Egg yolk; Lipovitellins; Trypsin hydrolysis; In silico; Bioactive peptides; Ultrafiltration; Polyethersulfone; Stabilised cellulose
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This study hydrolyzed lipoproteins using trypsin and evaluated the bioactivity of resulting peptides through in silico analysis. The transmission of valuable peptides through PES and SC membranes at different pHs was also assessed. The most promising antihypertensive peptide, K.VQWGIIPSWIK.K, was found in the permeates.
The lipoproteins that remain after the extraction of phosvitin from the egg yolk granular fraction possess low industrial applicability. In this study, these lipoproteins were hydrolysed using trypsin, and the bioactivity of the resulting peptides was assessed by in silico analysis. In addition, in order to isolate the most valuable previously detected peptides, their transmission through a polyethersulfone (PES) membrane and a stabilised cellulose (SC) based membrane was also evaluated at several pHs. A pH of 4.0 gave the highest observed transmission of peptides through both membranes for every peptide identified in the permeate streams. Regarding the PES membrane, six peptide sequences detected in the permeate were predicted to be antihypertensive, although only one of them showed a bioactivity score higher than 0.5 according to Peptide Ranker. When the SC membrane was assessed, five peptides with a bioactivity score higher than 0.5 were detected in the permeate streams and eight peptides were predicted as antihypertensive. The in silico analysis performed showed that K.VQWGIIPSWIK.K was the most promising antihypertensive peptide found in the permeates.
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