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Open AccessArticle

Oyster-Derived Zinc-Binding Peptide Modified by Plastein Reaction via Zinc Chelation Promotes the Intestinal Absorption of Zinc

1
College of Food Science and Engineering, Ocean University of China, Qingdao 266003, China
2
School of Food and Bioengineering, Jiangsu University, Zhenjiang 212013, China
3
School of Food Sciences and Engineering, South China University of Technology, Guangzhou 510641, China
4
Hisense (Shandong) Refrigerator Co., Ltd., Qingdao 266100, China
5
Jiangsu Baoyuan Biotechnology Co., Ltd., Lianyungang 222100, China
6
College of Food and Bioengineering, Henan University of Science and Technology, Luoyang 471023, China
*
Author to whom correspondence should be addressed.
These authors contributed equally to this study.
Mar. Drugs 2019, 17(6), 341; https://doi.org/10.3390/md17060341
Received: 13 May 2019 / Revised: 3 June 2019 / Accepted: 5 June 2019 / Published: 8 June 2019
Zinc-binding peptides from oyster (Crassostrea gigas) have potential effects on zinc supplementation. The aim of this study was to prepare efficient zinc-binding peptides from oyster-modified hydrolysates by adding exogenous glutamate according to the plastein reaction and to further explore the zinc absorption mechanism of the peptide-zinc complex (MZ). The optimum conditions for the plastein reaction were as follows: pH 5.0, 40 °C, substrate concentration of 40%, pepsin dosage of 500 U/g, reaction time of 3 h and l-[1-13C]glutamate concentration of 10 mg/mL. The results of 13C isotope labelling suggested that the addition of l-[1-13C]glutamate contributed to the increase in the zinc-binding capacity of the peptide. The hydrophobic interaction was the main mechanism of action of the plastein reaction. Ultraviolet spectra and scanning electronic microscopy (SEM) revealed that the zinc-binding peptide could bind with zinc and form MZ. Furthermore, MZ could significantly enhance zinc bioavailability in the presence of phytic acid, compared to the commonly used ZnSO4. Additionally, MZ significantly promoted the intestinal absorption of zinc mainly through two pathways, the zinc ion channel and the small peptide transport pathway. Our work attempted to increase the understanding of the zinc absorption mechanism of MZ and to support the potential application of MZ as a supplementary medicine. View Full-Text
Keywords: oyster zinc-binding peptide; peptide-zinc complex; caco-2 cells; intestinal absorption; zinc bioavailability oyster zinc-binding peptide; peptide-zinc complex; caco-2 cells; intestinal absorption; zinc bioavailability
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MDPI and ACS Style

Li, J.; Gong, C.; Wang, Z.; Gao, R.; Ren, J.; Zhou, X.; Wang, H.; Xu, H.; Xiao, F.; Cao, Y.; Zhao, Y. Oyster-Derived Zinc-Binding Peptide Modified by Plastein Reaction via Zinc Chelation Promotes the Intestinal Absorption of Zinc. Mar. Drugs 2019, 17, 341.

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