Investigation into allergenicity reduction and glycation sites of glycated β-lactoglobulin with ultrasound pretreatment by high-resolution mass spectrometry

Liu, Guangxian; Tu, Zong–cai; Yang, Wenhua; Wang, Hui; Zhang, Lu; Ma, Da; Li, Jun; Li, Xue

doi:10.1016/j.foodchem.2018.01.086

Cited by 73 publications

(48 citation statements)

References 28 publications

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“…The changes in the tertiary structure of PV may lead to the destruction of the conformational epitopes, and the IgE/IgG binding capacity is related to the integrity of antigenic, which depends on the structure of protein. Our previous study also indicated that glycation could significantly decrease the IgE‐binding capacity of β‐lg‐ribose conjugate (Liu, Tu, Yang, et al, 2018). However, it is worth mentioning that the decrease of IgE/IgG binding capacity in PV‐Lac is not caused by glycation, but lactose is involved in the immune response after being transformed into lactulose.…”

Section: Resultsmentioning

confidence: 77%

“…At the same time, it was further explained that the binding site of PV-Glu is closer to Trp, and the hydrophobicity of PV-Glu was decreased (Wang et al, 2007). Our previous study also indicated that glycation could significantly decrease the IgE-binding capacity of β-lg-ribose conjugate (Liu, Tu, Yang, et al, 2018). However, it is worth mentioning that the decrease of IgE/IgG binding capacity in PV-Lac is not caused by glycation, but lactose is involved in the immune response after being transformed into lactulose.…”

Section: Synchronous Fluorescence Spectramentioning

confidence: 88%

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The IgE/IgG binding capacity and structural changes of Alaska Pollock parvalbumin glycated with different reducing sugars

Zhang

Liu

et al. 2020

J. Food Biochem.

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Parvalbumin (PV) is one of the major allergens in fish. The aim of our present work was to research the influence mechanism of glycation with different reducing sugars (glucose, fructose, ribose, lactose, and galactose) on the immunoglobulin E (IgE) and immunoglobulin G (IgG) binding capacity and structure changes of PV in Alaska Pollock. PV glycated with glucose or fructose (PV-Glu/ PV-Fru) exhibited the higher IgE/IgG binding capacities than that of ribose, galactose, or lactose. During glycation, the lysine (Lyr), tyrosine (Tyr), and phenylalanine (Phe) of PV were gradually embed into core area of three-dimensional structure of protein, which reflected in the ultraviolet (UV) spectrum and fluorescence spectra. Moreover, the increase of surface hydrophobicity had confirmed the conformation alteration of glycated PV. These results suggest that there is a specific association among the change of PV in glycation and in potential allergenicity. The types and conformation of reducing sugar greatly influenced the IgE/IgG binding capacity of PV, and glycation with ribose and galactose was a promising approach for reducing the IgE/IgG binding capacity of PV from Alaska Pollock. Practical applications Parvalbumin (PV), the major allergen of fish, it can not only maintain the physiological activity of cells, but also cross react with human amyloid protein to alleviate Alzheimer's disease and Parkinson's syndrome. This study revealed that the IgE/IgG binding capacity and structural changes of PV from Alaska Pollock modified by glycation with different reducing sugars. This will help us to understand the sensitization and structural change of the glycated products after the reaction of PV with different reducing sugars. It provides an effective carbonyl source for the preparation of low antigenicity PV based on glycation and lays a foundation for glycation modification of other food allergens.

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Section: Resultsmentioning

confidence: 77%

Section: Synchronous Fluorescence Spectramentioning

confidence: 88%

The IgE/IgG binding capacity and structural changes of Alaska Pollock parvalbumin glycated with different reducing sugars

Zhang

Liu

et al. 2020

J. Food Biochem.

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“…A review on this topic was recently published by Doost et al [94]. Some of the novel approaches that have been demonstrated to have a positive impact on the glycation process in a wet state are the application of ultrasonication [103,104], pulsed-electric fields [105], or irradiation [106] to the protein-carbohydrate dispersion to induce elevated temperatures, and in some cases, promote protein unfolding. Another approach is high-pressure pre-treatment of the protein dispersion to induce unfolding and structural changes that facilitate glycation in a subsequent heating step [107].…”

Section: Novel Approachesmentioning

confidence: 99%

Glycation of Plant Proteins Via Maillard Reaction: Reaction Chemistry, Technofunctional Properties, and Potential Food Application

Kutzli

Weiß

Gibis

2021

Foods

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Plant proteins are being considered to become the most important protein source of the future, and to do so, they must be able to replace the animal-derived proteins currently in use as techno-functional food ingredients. This poses challenges because plant proteins are oftentimes storage proteins with a high molecular weight and low water solubility. One promising approach to overcome these limitations is the glycation of plant proteins. The covalent bonding between the proteins and different carbohydrates created via the initial stage of the Maillard reaction can improve the techno-functional characteristics of these proteins without the involvement of potentially toxic chemicals. However, compared to studies with animal-derived proteins, glycation studies on plant proteins are currently still underrepresented in literature. This review provides an overview of the existing studies on the glycation of the major groups of plant proteins with different carbohydrates using different preparation methods. Emphasis is put on the reaction conditions used for glycation as well as the modifications to physicochemical properties and techno-functionality. Different applications of these glycated plant proteins in emulsions, foams, films, and encapsulation systems are introduced. Another focus lies on the reaction chemistry of the Maillard reaction and ways to harness it for controlled glycation and to limit the formation of undesired advanced glycation products. Finally, challenges related to the controlled glycation of plant proteins to improve their properties are discussed.

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“…A review on this topic was recently published by Doost et al [93]. Some of the novel approaches that have been demonstrated to have a positive impact on the glycation process in wet state are the application of ultrasonication [102,103], pulsed-electric fields [104] or irradiation [105] to the protein-carbohydrate-dispersion to induce elevated temperatures and in some cases promote protein unfolding. Another approach are high-pressure pre-treatments of the protein dispersion to induce unfolding and structural changes which facilitate glycation in a subsequent heating step [106].…”

Section: Novel Approachesmentioning

confidence: 99%

Glycation of Plant Proteins via Maillard Reaction: Reaction Chemistry, Technofunctional Properties, and Potential Food Application

Kutzli¹,

Weiß²,

Gibis³

2020

Preprint

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Plant proteins being considered to become the most important protein source of the future, they must be able to replace the animal-derived proteins currently in use as technofunctional food ingredients. This poses challenges because plant proteins are oftentimes storage proteins with a high molecular weight and low water solubility. One promising approach to overcome these limitations is the glycation of plant proteins. The covalent bonding between the proteins and different carbohydrates created via the initial stage of the Maillard reaction can improve the technofunctional characteristics of these proteins without the involvement of potentially toxic chemicals. However, compared to studies with animal-derived proteins, glycation studies on plant proteins are currently still underrepresented in literature. This review provides an overview of the existing studies on the glycation of the major groups of plant proteins with different carbohydrates using different preparation methods. Emphasis is put on the reaction conditions used for glycation as well as the modifications to physicochemical properties and technofunctionality. Different applications of these glycated plant proteins in emulsions, foams, films, and encapsulation systems are introduced. Another focus lies on the reaction chemistry of the Maillard reaction and ways to harness it for controlled glycation and to limit the formation of undesired advanced glycation products. Finally, challenges related to the controlled glycation of plant proteins to improve their properties are discussed.

show abstract

Investigation into allergenicity reduction and glycation sites of glycated β-lactoglobulin with ultrasound pretreatment by high-resolution mass spectrometry

Cited by 73 publications

References 28 publications

The IgE/IgG binding capacity and structural changes of Alaska Pollock parvalbumin glycated with different reducing sugars

The IgE/IgG binding capacity and structural changes of Alaska Pollock parvalbumin glycated with different reducing sugars

Glycation of Plant Proteins Via Maillard Reaction: Reaction Chemistry, Technofunctional Properties, and Potential Food Application

Glycation of Plant Proteins via Maillard Reaction: Reaction Chemistry, Technofunctional Properties, and Potential Food Application

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