Issue 12, 2019

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

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

Article information

Article type
Paper
Submitted
27 Jun 2019
Accepted
21 Oct 2019
First published
21 Oct 2019

Food Funct., 2019,10, 7724-7732

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

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements