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Issue 12, 2019
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The purification, identification and bioactivity study of a novel calcium-binding peptide from casein hydrolysate

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Abstract

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.

Graphical abstract: The purification, identification and bioactivity study of a novel calcium-binding peptide from casein hydrolysate

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Article information


Submitted
27 Jun 2019
Accepted
21 Oct 2019
First published
21 Oct 2019

Food Funct., 2019,10, 7724-7732
Article type
Paper

The purification, identification and bioactivity study of a novel calcium-binding peptide from casein hydrolysate

W. Liao, S. Liu, X. Liu, S. Duan, S. Xiao, Z. Yang, Y. Cao and J. Miao, Food Funct., 2019, 10, 7724
DOI: 10.1039/C9FO01383K

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