LC-Orbitrap MS analysis of the glycation modification effects of ovalbumin during freeze-drying with three reducing sugar additives

Chen, Yang; Tu, Zong–cai; Wang, Hui; Liu, Guangxian; Liao, Zi-wei; Zhang, Lu

doi:10.1016/j.foodchem.2018.06.092

Cited by 24 publications

(26 citation statements)

References 36 publications

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“…Lysine and arginine were the major susceptible sites during glycation under mild dry heating. This finding was different from our previous studies, which indicated that the sugars were predominantly located at lysine rather than arginine. , The first step of MR involves the preferential linkage of reducing sugar to ε-NH 2 of lysine. In the advanced steps of the reaction, the free guanidino groups are modified with carbonyl compounds .…”

Section: Resultscontrasting

confidence: 99%

“…A milder condition might reduce the disturbance of thermal effects, consequently emphasizing the structural influences of the days of incubation with monoses. Chen et al 30 also found similar changes in secondary structures between OVA and glycated OVA during freeze drying. Peptide Mapping and Glycation Identification.…”

Section: ■ Materials and Methodsmentioning

confidence: 68%

“…With respect to Arg105, Lys182, Lys227, Lys229, R285, Lys287, Lys291, Lys323, Arg340, Arg360, Lys370, and Arg382 (Figure S2 of the Supporting Information), they were located at the strands of the β-sheet inside the spherical structure of OVA and did not come into contact with monoses. Subsequently, the main strands of the β-sheet constituted a firm neighborhood that hindered OVA from interacting with monoses; on the contrary, protein unfolding could expose these sites to monoses. , Interestingly, 6, 6, 6, 4, and 4 glycated sites located at the strands of the β-sheet (Table ) were determined in OVA-Rib, OVA-Xyl, OVA-Gal, OVA-Glu, and OVA-Fru, respectively, suggesting the dramatic structural changes in the glycated OVA. The higher extent of glycation at the main strands of the β-sheet in OVA-Gal, OVA-Rib, and OVA-Xyl might indicate the increased level of unfolding in conformation compared to the other OVA–monose conjugates.…”

Section: Resultsmentioning

confidence: 99%

See 2 more Smart Citations

Investigation of the Mechanism of Conformational Alteration in Ovalbumin as Induced by Glycation with Different Monoses through Conventional Spectrometry and Liquid Chromatography High-Resolution Mass Spectrometry

Yang

Liu

Wang

2019

J. Agric. Food Chem.

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Glycation between ovalbumin (OVA) and different monoses under mild dry heating at 37 °C was studied. The content of free amino groups decreased dramatically, and the conformational changes based on fluorescence and circular dichroism spectra were evident in glycated OVA. The glycated sites and the average degree of substitution per peptide molecule per site were determined using liquid chromatography high-resolution mass spectrometry. Lysine and arginine were the predominant glyaction sites, in which Lys207 was a relatively reactive site for glycation in all of the conjugates. In general, the extent of glycation of aldose was higher, and its alterations on the steric layouts of protein were more drastic than those of ketose. The configuration of hydroxyl groups at C-4 in sugar epimers might be important for the glycation reactivity and conformational modification in the glycated proteins. These insights would have important implications for the creation of sweetened food products with desirable structures and excellent quality control.

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Section: Resultscontrasting

confidence: 99%

Section: ■ Materials and Methodsmentioning

confidence: 68%

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Investigation of the Mechanism of Conformational Alteration in Ovalbumin as Induced by Glycation with Different Monoses through Conventional Spectrometry and Liquid Chromatography High-Resolution Mass Spectrometry

Yang

Liu

Wang

2019

J. Agric. Food Chem.

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“…Specifically, water serves as a reaction medium, but an excessive amount of water could dilute the concentration of reactants leading to a depressive effect on glycation. It was noteworthy that recently the glycation during freeze-drying was reported, in which the temperature was −80 °C and the water existed in the form of crystals with very low water activity. , …”

Section: Introductionmentioning

confidence: 99%

“…It was noteworthy that recently the glycation during freeze-drying was reported, in which the temperature was −80 °C and the water existed in the form of crystals with very low water activity. 44,45 Glycation has been widely studied and proved to be a significant path to modify proteins. 11 The Amadori product formed between aldose and protein is called glycated protein.…”

Section: ■ Introductionmentioning

confidence: 99%

Glucose Glycation of α-Lactalbumin and β-Lactoglobulin in Glycerol Solutions

Chen

Zhang

Bhandari

et al. 2018

J. Agric. Food Chem.

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The glucose glycation of α-lactalbumin and β-lactoglobulin at 50 °C in a glycerol-based liquid system was investigated to evaluate the effect of water activity on glycation and site-specificity in a glycerol matrix. Glycation extent during the reaction was determined using the o-phthalaldehyde (OPA) method as well as ultraperformance liquid chromatography combined with electro-spray ionization mass spectrum (UPLC-ESI-MS) analysis. Glycation sites were identified by data-independent acquisition LC–MS (LC-MSE). The surface potential achieved by PyMOL and the tertiary structure determined by circular dichroism (CD) were used to assist the analysis of the glycation site-specificity in the glycerol matrix. The water activity of glycerol solutions was negatively correlated to the glycerol concentration. Results showed that the initial glycation rate in glycerol matrix was fitted to a linear equation in the first 48 h. Glycation accelerated with the increase of glycerol concentration, namely, the decrease of water activity, regardless of the native structure of the protein. The glycation sites were identical at a similar DSP although achieved at different water activities, with 4 and 7 sites detected in α-lactalbumin and β-lactoglobulin, respectively. However, compared with the glycation sites in a water-based matrix, the site-specificity of glycation was affected by the glycerol matrix, depending on the native structure of the proteins. Glycation was prone to occur at the reactive sites distributed on the surface of the proteins, particularly in the region with positive potential.

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Mechanisms of isoquercitrin attenuates ovalbumin glycation: Investigation by spectroscopy, spectrometry and molecular docking

Zhang

et al. 2020

Food Chemistry

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LC-Orbitrap MS analysis of the glycation modification effects of ovalbumin during freeze-drying with three reducing sugar additives

Cited by 24 publications

References 36 publications

Investigation of the Mechanism of Conformational Alteration in Ovalbumin as Induced by Glycation with Different Monoses through Conventional Spectrometry and Liquid Chromatography High-Resolution Mass Spectrometry

Investigation of the Mechanism of Conformational Alteration in Ovalbumin as Induced by Glycation with Different Monoses through Conventional Spectrometry and Liquid Chromatography High-Resolution Mass Spectrometry

Glucose Glycation of α-Lactalbumin and β-Lactoglobulin in Glycerol Solutions

Mechanisms of isoquercitrin attenuates ovalbumin glycation: Investigation by spectroscopy, spectrometry and molecular docking

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