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Isolation and identification of zinc‐chelating peptides from sea cucumber ( Stichopus japonicus ) protein hydrolysate
Author(s) -
Liu Xiaoyang,
Wang Zixu,
Zhang Jing,
Song Liang,
Li Deyang,
Wu Zixuan,
Zhu Beiwei,
Nakamura Yoshimasa,
Shahidi Fereidoon,
Yu Chenxu,
Zhou Dayong
Publication year - 2019
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.9919
Subject(s) - chemistry , zinc , isothermal titration calorimetry , chromatography , sea cucumber , hydrolysate , chelation , ultrafiltration (renal) , gel permeation chromatography , nuclear chemistry , hydrolysis , biochemistry , organic chemistry , biology , ecology , polymer
BACKGROUND Zinc is known to play an essential role in the biological activities in the human body. In this study, a zinc‐chelating peptide (ZCP) produced by Alcalase‐assisted hydrolysis of the body wall of sea cucumber was isolated and identified. The ZCP was purified stepwise by ultrafiltration, anion‐exchange chromatography, and gel filtration chromatography, in conjunction with ultraviolet–visual (UV–visual) spectrophotometry, which was used to analyze each purified fraction. RESULTS Analysis of the purified ZCP revealed that its zinc‐chelating ability was 33.31%. Analysis of isothermal titration calorimetry suggested that the binding of ZCP and zinc (N ≈ 2) was endothermic, with weak binding affinity. Fourier transform infrared spectroscopy spectra (FTIR) indicated that carboxylic and amide groups in ZCP were the primary binding sites of Zn. Sequencing the result by ultra‐performance liquid chromatography‐quadrupole/time of flight mass spectrometry (UPLC‐Q‐TOF‐MS/MS) showed that a representative ZCP had the sequence WLTPTYPE with a molecular weight of 1005.5 Da. CONCLUSION These results provide a promising foundation for the production of zinc supplements from sea‐cucumber‐derived ZCPs. © 2019 Society of Chemical Industry