Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction

Peruško, Marija; Al-Hanish, Ayah; Veličković, Tanja Ćirković; Stanić-Vučinić, Dragana

doi:10.1016/j.foodchem.2015.01.042

Cited by 73 publications

(35 citation statements)

References 41 publications

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“…Heated BLG showed a significantly higher loss of β‐sheets (Figure S2A,B, Supporting Information). The protective effect of sugar on the heat‐induced denaturation and aggregation of BLG has been shown extensively before . Therefore structural changes induced by Maillard reaction are not simply the sum of thermally induced structural changes and covalent attachment of sugar moieties.…”

Section: Resultsmentioning

confidence: 86%

“…Thermally treated BLG under the same conditions but without glucose was also prepared. To determine the degree of glycation, free amino groups were estimated by the ortho‐phthalaldehyde (OPA) method as described previously . To further characterize glycated BLG, SDS‐PAGE was performed on 14% gel (5 μg of protein per lane, under reducing and nonreducing conditions.…”

Section: Methodsmentioning

confidence: 99%

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Glycation of the Major Milk Allergen β‐Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation

Peruško¹,

Roest

Stanić-Vučinić

et al. 2018

Molecular Nutrition Food Res

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ScopeDuring food processing, the Maillard reaction (МR) may occur, resulting in the formation of glycated proteins. Glycated proteins are of particular importance in food allergies because glycation may influence interactions with the immune system. This study compared native and extensively glycated milk allergen β‐lactoglobulin (BLG), in their interactions with cells crucially involved in allergy.Methods and resultsBLG was glycated in MR and characterized. Native and glycated BLG were tested in experiments of epithelial transport, uptake and degradation by DCs, T‐cell cytokine responses, and basophil cell degranulation using ELISA and flow cytometry. Glycation of BLG induced partial unfolding and reduced its intestinal epithelial transfer over a Caco‐2 monolayer. Uptake of glycated BLG by bone marrow–derived dendritic cells (BMDC) was increased, although both BLG forms entered BMDC via the same mechanism, receptor‐mediated endocytosis. Once inside the BMDC, glycated BLG was degraded faster, which might have led to observed lower cytokine production in BMDC/CD4+ T‐cells coculture. Finally, glycated BLG was less efficient in induction of degranulation of BLG‐specific IgE sensitized basophil cells.ConclusionsThis study suggests that glycation of BLG by MR significantly alters its fate in processes involved in immunogenicity and allergenicity, pointing out the importance of food processing in food allergy.

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Section: Resultsmentioning

confidence: 86%

Section: Methodsmentioning

confidence: 99%

Glycation of the Major Milk Allergen β‐Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation

Peruško¹,

Roest

Stanić-Vučinić

et al. 2018

Molecular Nutrition Food Res

Self Cite

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“…Macromolecular crowding has also been reported to be used in the fabrication of liquid crystalline imprinter polymers. 51 In food chemistry, Perusko et al 52 applied macromolecular crowding, using PEG, to enhance oxidation and glycation of whey proteins which resulted in the shortening of processing time, milder conditions, while preserving the structure of proteins as well as reducing the formation of protein aggregates.…”

Section: Applications Of Macromolecular Crowdingmentioning

confidence: 99%

Making microenvironments: A look into incorporating macromolecular crowding into in vitro experiments, to generate biomimetic microenvironments which are capable of directing cell function for tissue engineering applications

Benny

Raghunath

2017

J Tissue Eng

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Biomimetic microenvironments are key components to successful cell culture and tissue engineering in vitro. One of the most accurate biomimetic microenvironments is that made by the cells themselves. Cell-made microenvironments are most similar to the in vivo state as they are cell-specific and produced by the actual cells which reside in that specific microenvironment. However, cell-made microenvironments have been challenging to re-create in vitro due to the lack of extracellular matrix composition, volume and complexity which are required. By applying macromolecular crowding to current cell culture protocols, cell-made microenvironments, or cell-derived matrices, can be generated at significant rates in vitro. In this review, we will examine the causes and effects of macromolecular crowding and how it has been applied in several in vitro systems including tissue engineering.

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“…These 266 results are consistent with previous studies. 12,35 There was no significant difference 267 in diameter sizes between WD and WDC regardless of heat treatment. In our previous 268 publication, we reported that HWDC dispersion was stable against pH and salt, but…”

mentioning

confidence: 91%

“…This work 29 will be beneficial to understand protein conformational changes and molecular forces 30 in biopolymer nanoparticles, and to prepare the stable biopolymer nanoparticles from 31 heating electrostatic complexes of native or glycosylated protein and polysaccharide. 32 35 Biopolymer nanoparticles, as a delivery vehicle for hydrophobic bioactive 36 compounds, have attracted great attention due to their remarkable nonantigenicity, 37 biocompatibility, biodegradability, and abundant renewable properties. [1][2][3][4][5] The 38 stability of biopolymer nanoparticles, especially under different physiological 39 conditions, is essential to prevent microstructural destruction before reaching certain 40 target sites after uptake.…”

mentioning

confidence: 99%

Mechanism of Formation and Stabilization of Nanoparticles Produced by Heating Electrostatic Complexes of WPI–Dextran Conjugate and Chondroitin Sulfate

Dai

Zhu

et al. 2016

J. Agric. Food Chem.

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Protein conformational changes were demonstrated in biopolymer nanoparticles, and molecular forces were studied to elucidate the formation and stabilization mechanism of biopolymer nanoparticles. The biopolymer nanoparticles were prepared by heating electrostatic complexes of whey protein isolate (WPI)-dextran conjugate (WD) and chondroitin sulfate (ChS) above the denaturation temperature and near the isoelectric point of WPI. The internal characteristics of biopolymer nanoparticles were analyzed by several spectroscopic techniques. Results showed that grafted dextran significantly (p < 0.05) prevented the formation of large aggregates of WD dispersion during heat treatment. However, heat treatment slightly induced the hydrophobicity changes of the microenvironment around fluorophores of WD. ChS electrostatic interaction with WD changed the fluorescence intensity of WD regardless of heat treatment. Far-UV circular dichroism (CD) and attenuated total reflectance Fourier transform infrared (ATR-FTIR) spectroscopies confirmed that glycosylation and ionic polysaccharide did not significantly cause protein conformational changes in WD and ChS (WDC) during heat treatment. In addition, hydrophobic bonds were the major molecular force for the formation and stabilization of biopolymer nanoparticles. However, hydrogen bonds slightly influenced their formation and stabilization. Ionic bonds only promoted the formation of biopolymer nanoparticles, while disulfide bonds partly contributed to their stability. This work will be beneficial to understand protein conformational changes and molecular forces in biopolymer nanoparticles, and to prepare the stable biopolymer nanoparticles from heating electrostatic complexes of native or glycosylated protein and polysaccharide.

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Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction

Cited by 73 publications

References 41 publications

Glycation of the Major Milk Allergen β‐Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation

Glycation of the Major Milk Allergen β‐Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation

Making microenvironments: A look into incorporating macromolecular crowding into in vitro experiments, to generate biomimetic microenvironments which are capable of directing cell function for tissue engineering applications

Mechanism of Formation and Stabilization of Nanoparticles Produced by Heating Electrostatic Complexes of WPI–Dextran Conjugate and Chondroitin Sulfate

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