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A new peptide with strong calcium binding capacity was isolated from phosvitin hydrolysates. Taking calcium chelating rate as an indicator, phosvitin hydrolysates were separated gradually by anion-exchange chromatography, gel filtration chromatography and reversed-phase high performance liquid chromatography. A peptide with a molecular weight of 1106.44402 Da was identified by liquid chromatography-electrospray/mass spectrometry (LC-ESI/MS), and its amino acid sequence was DEEENDQVK, the calcium binding capacity reached 151.10 ± 3.57 mg/g. Its chelating mechanism was investigated. Results showed that, the β-sheet structure of peptide increased after adding calcium ion, and the main binding sites were carboxyl oxygen atom and amino nitrogen atom. In vitro simulated digestion experiments showed that, the solubility and dialysis rate of calcium in peptide-calcium chelate were higher than those in CaCO and D-calcium gluconate. This finding would promote the development of calcium supplements from food resources.
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http://dx.doi.org/10.1016/j.foodres.2021.110169 | DOI Listing |
J Agric Food Chem
June 2025
College of Food Science and Technology, Huazhong Agricultural University, National Research and Development Centre for Egg Processing, Key Laboratory of Egg Processing, Ministry of Agriculture and Rural Affairs, Wuhan, Hubei 430070, PR China.
This study aimed to identify a novel peptide from phosvitin hydrolysates with enhanced antioxidant and calcium absorption-promoting properties. Simultaneous enzymatic hydrolysates (trypsin + alkaline protease) exhibited better bifunctional activity than sequential enzymatic hydrolysates. Three components of phosvitin hydrolysates (PPP0, PPP1, and PPP2) were isolated by anion-exchange chromatography, and PPP2 displayed the highest activity.
View Article and Find Full Text PDFFood Chem
June 2022
Department of Chemical and Environmental Engineering, University of Oviedo, C/ Julián Clavería 8, 33006 Oviedo, Spain.
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.
View Article and Find Full Text PDFFood Res Int
March 2021
State Key Laboratory of Food Nutrition and Safety, Key Laboratory of Food Nutrition and Safety, Ministry of Education of China, College of Food Science and Engineering, Tianjin University of Science and Technology, Tianjin 300457, PR China.
A new peptide with strong calcium binding capacity was isolated from phosvitin hydrolysates. Taking calcium chelating rate as an indicator, phosvitin hydrolysates were separated gradually by anion-exchange chromatography, gel filtration chromatography and reversed-phase high performance liquid chromatography. A peptide with a molecular weight of 1106.
View Article and Find Full Text PDFPoult Sci
February 2021
National Research and Development Center for Egg Processing, College of Food Science and Technology, Huazhong Agricultural University, Wuhan, Hubei 430070, PR China. Electronic address:
Phosvitin (PV) from egg yolk is an excellent substrate for the production of phosphopeptides, which have a strong calcium chelating capacity and promoting calcium absorption and bone mineralization. This study investigated the effect of PV hydrolysates produced using a effective preparation method (high temperature (121°C) and mild pressure (0.1 MPa), HTMP) or HTMP pretreatment and trypsin hydrolysis combination (HTMP-PV18) on the physiology of an osteoblast MC3T3-E1 cells line.
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June 2020
Instituto de Investigación en Ciencias de la Alimentación (CIAL, CSIC-UAM), 28049 Madrid, Spain.
In addition to their high nutritional value, some chicken egg proteins and derivatives such as protein hydrolysates, peptides and amino acids show antioxidant properties which make them prominent candidates for the development of functional foods, drawing attention to both the food and biopharmaceutical industries. This review summarizes current knowledge on antioxidant activity of chicken egg proteins and their derived peptides. Some egg proteins such as ovalbumin, ovotransferrin and lysozyme from egg white or phosvitin from yolk have shown antioxidant properties, although derived peptides have higher bioactive potential.
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