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Volume 11
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10.3390/foods11030468
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Article

Purification and Characterization of a Novel Calcium-Binding Heptapeptide from the Hydrolysate of Tilapia Bone with Its Osteogenic Activity

by
Jinlun He
,
Hao Guo
,
Mei Zhang
,
Meng Wang
,
Liping Sun
and
Yongliang Zhuang
*
Faculty of Food Science and Engineering, Kunming University of Science and Technology, No. 727 South Jingming Road, Kunming 650500, China
*
Author to whom correspondence should be addressed.
Foods 2022, 11(3), 468; https://doi.org/10.3390/foods11030468
Submission received: 18 January 2022 / Revised: 28 January 2022 / Accepted: 2 February 2022 / Published: 4 February 2022
(This article belongs to the Special Issue Food By-Products as a Source of Proteins and Peptides)
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Abstract

In this study, a calcium-binding peptide was obtained by hydrolyzing tilapia bone and its osteogenic activity was evaluated. Animal protease was selected from nine enzymes, and its hydrolysate was purified through preparative and semi-preparative reverse phase high-performance liquid chromatography. The purified peptide was identified as DGPSGPK (656.32 Da) and its calcium-binding capacity reached 111.98 µg/mg. The peptide calcium chelate (DGPSGPK-Ca) was obtained, and its structure was characterized through Fourier transform infrared spectroscopy (FTIR), X-ray diffraction (XRD), scanning electron microscopy (SEM), and mass spectrometry (MS). The results of XRD and SEM showed that DGPSGPK-Ca was formed as a new compound. The carboxyl and amino groups of Lys and Asp residues may be the chelating sites of DGPSGPK according to the FTIR and MS results. The molecular simulation showed the carbonyl groups of Asp, Pro, Ser, and Lys residues involved in the binding of calcium. The interaction of DGPSGPK and different integrins was evaluated by molecular docking simulation, and the main forces involved were electrostatic interaction forces, hydrogen bonding and hydrophobic interactions. Furthermore, DGPSGPK could inhibit the differentiation of osteoclast and promote the proliferation, differentiation and mineralization of osteoblasts.
Keywords: tilapia bone; peptide; calcium-binding capacity; structural characteristics; mass spectrometry; molecular docking; osteoblast tilapia bone; peptide; calcium-binding capacity; structural characteristics; mass spectrometry; molecular docking; osteoblast
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MDPI and ACS Style

He, J.; Guo, H.; Zhang, M.; Wang, M.; Sun, L.; Zhuang, Y. Purification and Characterization of a Novel Calcium-Binding Heptapeptide from the Hydrolysate of Tilapia Bone with Its Osteogenic Activity. Foods 2022, 11, 468. https://doi.org/10.3390/foods11030468

AMA Style

He J, Guo H, Zhang M, Wang M, Sun L, Zhuang Y. Purification and Characterization of a Novel Calcium-Binding Heptapeptide from the Hydrolysate of Tilapia Bone with Its Osteogenic Activity. Foods. 2022; 11(3):468. https://doi.org/10.3390/foods11030468

Chicago/Turabian Style

He, Jinlun, Hao Guo, Mei Zhang, Meng Wang, Liping Sun, and Yongliang Zhuang. 2022. "Purification and Characterization of a Novel Calcium-Binding Heptapeptide from the Hydrolysate of Tilapia Bone with Its Osteogenic Activity" Foods 11, no. 3: 468. https://doi.org/10.3390/foods11030468

APA Style

He, J., Guo, H., Zhang, M., Wang, M., Sun, L., & Zhuang, Y. (2022). Purification and Characterization of a Novel Calcium-Binding Heptapeptide from the Hydrolysate of Tilapia Bone with Its Osteogenic Activity. Foods, 11(3), 468. https://doi.org/10.3390/foods11030468

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