Preparation of Calcium-Binding Peptides Derived from Mackerel (

Pengbo Cui, Jianqin Liang, Tianyu Cheng, Jianyou Zhang

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Article in Foods (Basel, Switzerland), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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4 authors.

Pengbo CuiZhejiang Key Laboratory of Green, Low-Carbon and Efficient Development of Marine Fishery Resources, College of Food Science and Technology, Zhejiang University of Technology, Hangzhou 310014, China.

Jianqin LiangZhejiang Key Laboratory of Green, Low-Carbon and Efficient Development of Marine Fishery Resources, College of Food Science and Technology, Zhejiang University of Technology, Hangzhou 310014, China.

Tianyu ChengZhejiang Key Laboratory of Green, Low-Carbon and Efficient Development of Marine Fishery Resources, College of Food Science and Technology, Zhejiang University of Technology, Hangzhou 310014, China.

Jianyou ZhangZhejiang Key Laboratory of Green, Low-Carbon and Efficient Development of Marine Fishery Resources, College of Food Science and Technology, Zhejiang University of Technology, Hangzhou 310014, China.ORCID 0000-0003-0917-2290

Funding

Zhejiang Provincial Natural Science Foundation LQ22C200015

6 · The paper itself

Abstract

The purpose of this study was to prepare mackerel peptides (MPs) with calcium-binding capacity through an enzyme method and to investigate the potential role they play in improving the bioavailability of calcium in vitro. The calcium-binding capacity, degree of hydrolysis (DH), molecular weight (MW), and charge distribution changes with the enzymolysis time of MPs were measured. The structural characterization of mackerel peptide-calcium (MP-calcium) complexes was performed using spectroscopy and morphology analysis. The results showed that the maximum calcium-binding capacity of the obtained MPs was 120.95 mg/g when alcalase was used for 3 h, with a DH of 15.45%. Moreover, with an increase in hydrolysis time, the MW of the MPs decreased, and the negative charge increased. The carboxyl and amino groups in aspartic (Asp) and glutamate (Glu) of the MPs may act as calcium-binding sites, which are further assembled into compact nanoscale spherical complexes with calcium ions through intermolecular interactions. Furthermore, even under the influence of oxalic acid, MP-calcium complexes maintained a certain solubility. This study provides a basis for developing new calcium supplements and efficiently utilizing the mackerel protein resource.

Indexed as

calcium-binding peptidecharacterizationmackerelstability analysis

Identifiers

PMID38890881

DOI10.3390/foods13111652

PMCPMC11171527

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