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Tytuł:
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Insight into the mechanism of urea inhibit ovalbumin-glucose glycation by conventional spectrometry and liquid chromatography-high resolution mass spectrometry.
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Autorzy:
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Hu YM; State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, Jiangxi 330047, China.
Guo HZ; State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, Jiangxi 330047, China.
Wang H; State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, Jiangxi 330047, China. Electronic address: .
Yang YF; State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, Jiangxi 330047, China.
Tu ZC; State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, Jiangxi 330047, China; National R&D Center of Freshwater Fish Processing, Jiangxi Normal University, Nanchang 330022, China; Engineering Research Center of Freshwater Fish High-value Utilization of Jiangxi Province, Jiangxi Normal University, Nanchang 330022, China. Electronic address: tuzc_.
Huang T; College of Food and Pharmaceutical Sciences, Ningbo University, Ningbo, Zhejiang 315800, China.
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Źródło:
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Food chemistry [Food Chem] 2021 Apr 16; Vol. 342, pp. 128340. Date of Electronic Publication: 2020 Oct 09.
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Typ publikacji:
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Journal Article
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Język:
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English
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Imprint Name(s):
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Publication: Barking : Elsevier Applied Science Publishers
Original Publication: Barking, Eng., Applied Science Publishers.
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MeSH Terms:
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Chromatography, Liquid*
Mass Spectrometry*
Glucose/*metabolism
Ovalbumin/*metabolism
Urea/*pharmacology
Circular Dichroism ; Glycosylation/drug effects ; Spectrometry, Fluorescence
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Contributed Indexing:
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Keywords: Conventional spectroscopy; Inhibition; LC-HRMS; Ovalbumin-glucose glycation; Urea
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Substance Nomenclature:
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8W8T17847W (Urea)
9006-59-1 (Ovalbumin)
IY9XDZ35W2 (Glucose)
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Entry Date(s):
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Date Created: 20201018 Date Completed: 20210204 Latest Revision: 20210204
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Update Code:
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20240105
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DOI:
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10.1016/j.foodchem.2020.128340
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PMID:
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33069536
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The inhibition effect of urea on ovalbumin (OVA) glycation was investigated, and the mechanism was evaluated through the changes in protein structure as well as glycation sites and average degree of substitution per peptide molecule (DSP) by conventional spectrometry and liquid chromatography-high resolution mass spectrometry (LC-HRMS). A urea concentration of 3 M was chosen as the optimum condition. Ultraviolet and fluorescence spectra suggested that both glycation and urea treatment could unfold the OVA, but urea inhibited the glycation-induced protein unfolding. Circular dichroism spectra showed that urea treatment could increase the β-sheet content and reduce the α-helix content of OVA. LC-HRMS indicated that the number of glycation sites was reduced from 15 to 3, and DSP values decreased with urea treatment. In conclusion, urea could significantly inhibit the OVA-glucose glycation, and the sites competition as well as structure unfolding inhibition resulted from urea could be the main factors.
(Copyright © 2020 Elsevier Ltd. All rights reserved.)
