Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/102950
Title: Commercial processed soy-based food product contains glycated and glycoxidated lunasin proteoforms
Authors: Serra, Aida
Gallart-Palau, Xavier
See-Toh, Rachel Su-En
Hemu, Xinya
Sze, Siu Kwan
Tam, James Pingkwan
Keywords: Food Analysis
Soybean Protein
DRNTU::Science::Biological sciences
Issue Date: 2016
Source: Serra, A., Gallart-Palau, X., See-Toh, R. S.-E., Hemu, X., Tam, J. P., & Sze, S. K. (2016). Commercial processed soy-based food product contains glycated and glycoxidated lunasin proteoforms. Scientific Reports, 6, 26106-. doi:10.1038/srep26106
Series/Report no.: Scientific Reports
Abstract: Nutraceuticals have been proposed to exert positive effects on human health and confer protection against many chronic diseases. A major bioactive component of soy-based foods is lunasin peptide, which has potential to exert a major impact on the health of human consumers worldwide, but the biochemical features of dietary lunasin still remain poorly characterized. In this study, lunasin was purified from a soy-based food product via strong anion exchange solid phase extraction and then subjected to top-down mass spectrometry analysis that revealed in detail the molecular diversity of lunasin in processed soybean foods. We detected multiple glycated proteoforms together with potentially toxic advanced glycation end products (AGEs) derived from lunasin. In both cases, modification sites were Lys24 and Lys29 located at the helical region that shows structural homology with a conserved region of chromatin-binding proteins. The identified post-translational modifications may have an important repercussion on lunasin epigenetic regulatory capacity. Taking together, our results demonstrate the importance of proper chemical characterization of commercial processed food products to assess their impact on consumer’s health and risk of chronic diseases.
URI: https://hdl.handle.net/10356/102950
http://hdl.handle.net/10220/46522
DOI: 10.1038/srep26106
Rights: © 2016 The Authors (Nature Publishing Group). This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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