Journal
FOOD & FUNCTION
Volume 10, Issue 12, Pages 7724-7732Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c9fo01383k
Keywords
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Funding
- National Natural Science Foundation of China [31601474]
- Open Fund of Beijing Advanced Innovation Center for Food Nutrition and Human Health [20181001]
- Science and Technology Project of Guangzhou, China [201707010415]
- Natural Science Foundation of Guangdong Province [2016A030310442]
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In this study, a novel calcium-binding peptide from casein hydrolysate was purified using reversed-phase high performance liquid chromatography and sequenced by high-performance liquid chromatography-mass spectrometry (MS)/MS. The amino acid sequence of the calcium-binding peptide was identified as VLPVPQK (N- to C-terminal, MW = 779.4960 Da). The calcium binding characteristics of VLPVPQK were further investigated using UV absorption spectroscopy, zeta potential and isothermal titration calorimetry (ITC). The results showed that VLPVPQK has a strong calcium binding activity (129.46 mg g(-1)), 312% higher than that of 3-hour enzymatic hydrolysates. VLPVPQK could chelate calcium with a 1:3 stoichiometry, causing a decrease in the positive charge of the peptide-Ca2+ complex. Furthermore, VLPVPQK could effectively enhance calcium transport and absorption in a concentration-dependent manner in Caco-2 cell monolayers, suggesting that VLPVPQK has the potential to be developed as a nutraceutical additive.
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