Comparative study on the effects of nystose and fructofuranosyl nystose in the glycation reaction on the antigenicity and conformation of β-lactoglobulin

Zhong, Junzhen; Tu, Yue; Liu, Wei; Luo, Shuhong

doi:10.1016/j.foodchem.2015.05.015

Cited by 27 publications

(18 citation statements)

References 35 publications

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“…Even in proteins highly resistant to proteolysis, it has been reported that there is an increase in in vitro digestibility and a reduction in their immunoreactivity (Kobayashi and others ; Corzo‐Martínez and others ; Wu and others ). Glucose (Bu and others , ), chitosan (Aoki and others ), nystose, fructofuranosyl nystose, and fructooligosaccharides (Zhong and others , ), oligoisomaltose and maltose (Aalberse ; Li and others , ), and carboxymethyl dextran (Kobayashi and others ) are some sugars with a reported effect on the reduction of β‐LG and ALA antigenicity and allergenicity. Maillard reactions between lactose (disaccharide) and the accessible amino groups of lysine residue in whey proteins might also occur, leading to the formation of Amadori products (Liu and others ).…”

Section: Effect Of Processing Food Matrix and Digestibility On Milkmentioning

confidence: 99%

Bovine Milk Allergens: A Comprehensive Review

Villa

Costa

Oliveira

et al. 2017

Comp Rev Food Sci Food Safe

175

145

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Cow milk allergy is one of the most common food allergies in early childhood and often persists through adult life, forcing an individual to a complete elimination diet. Milk proteins are present in uncounted food products, such as cheese, yogurt, or bakery item, exposing allergic persons to a constant threat. Many efforts have been made to overcome this global problem and to improve the life quality of allergic individuals. First, proper and reliable food labeling is fundamental for consumers, but the verification of its compliance is also needed, which should rely on accurate and sensitive analytical methods to detect milk allergens in processed foods. At the same time, strategies to reduce milk allergenicity, such as immunotherapy or the use of food processing techniques to modify allergen structure, have to be extensively studied. Recent research findings on the applicability of food processing, such as heat treatment, fermentation, or high pressure, have revealed great potential in reducing milk allergenicity. In this review, significant research advances on cow milk allergy are explored, focusing on prevalence, diagnosis, and therapy. Molecular characterization of cow milk allergens and cross-reactivity with other nonbovine milk species are described, as well as the effects of processing, food matrix, and digestibility on milk allergenicity. Additionally, analytical methods for the detection of milk allergens in food are described, from immunoassays and mass spectrometry methods for protein analysis to real-time polymerase chain reaction for DNA analysis.

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Section: Effect Of Processing Food Matrix and Digestibility On Milkmentioning

confidence: 99%

Bovine Milk Allergens: A Comprehensive Review

Villa

Costa

Oliveira

et al. 2017

Comp Rev Food Sci Food Safe

175

145

View full text Add to dashboard Cite

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“…To eliminate the allergenicity of β-LG, several methods have been investigated. In our previous work, Zhong et al (2015) concluded that the antigenicity of β-LG sharply decreased after conjugation with nystose and 1 F -β-fructofuranosyl nystose. The antigenicity of β-LG decreased to 70% when conjugated with monomethoxy polyethylene glycol-succinimidyl carbonates at a molar ratio of 1:3, pH 7.0, and reaction time of 8 h (Zhong et al, 2016).…”

Section: Introductionmentioning

confidence: 95%

Antigenicity of β-lactoglobulin reduced by combining with oleic acid during dynamic high-pressure microfluidization: Multi-spectroscopy and molecule dynamics simulation analysis

Zhong

et al. 2019

Journal of Dairy Science

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Some food components can modulate the antigenicity of β-lactoglobulin (β-LG). This study investigated the role of oleic acid (OA) in reducing the antigenicity of β-LG. The results indicate the antigenicity of β-LG gradually decreased from 15 (sample with no OA) to 9.86, 7.51, and 6.01 µg/mL when interacting with OA during dynamic high-pressure microfluidization treatment at 0.1, 80, and 160 MPa. Although binding sites (n) of β-LG combined with OA at 0.1, 80, and 160 MPa decreased from 0.79 to 0.5 and 0.66, β-LG had a higher binding affinity (K a) to OA than that of untreated β-LG. The values of K a for β-LG/OA at 0.1, 80, and 160 MPa were 5.51 × 10 6 , 17.43 × 10 6 , and 49.75 × 10 6 M −1 , respectively. The molecule dynamic simulation showed that the OA molecules located at both β-barrel (site 1) interacted with Lys60, Glu62, and Lys69 and outer surface site 2 consisting of Tyr20, Tyr42, Ser21, Glu157, and His161. Additionally, when binding with OA during the dynamic high-pressure microfluidization treatment, the conformation of β-LG changed, reflected by the decrease of fluorescence intensity and total sulfhydryl group content, the increase of surface sulfhydryl group content, and secondary structure changes of β-LG. These results deduce that some epitopes may be masked by OA or modified by the conformational changes, resulting in the decline of antigenicity of β-LG molecules.

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“…It was found that the increase in the antigenicity of β-LG was related to the conformational changes induced by DHPM treatment (Zhong, et al, 2012). On the contrary, it was observed that when conjugated with different saccharides the conformation of β-LG changed differently, but a similar decrease in antigenicity occurred (Zhong, et al, 2015). As two different modulated processes of antigenic response of β-LG, the mechanism of its antigenicity change is not completely clear when the protein undergo a combined treatment of glycation reaction and DHPM.…”

Section: Introductionmentioning

confidence: 99%

“…However, the antigenicity of this protein limits their application in the food industry (Moro, Baez, Busti, Ballerini, & Delorenzi, 2011). Previous works have investigated the effect of various processing treatments on the antigenicity of β-LG, including dynamic high pressure microfluidization (DHPM) (Zhong, et al, 2012;Zhong, Luo, Liu, & Liu, 2014a), heat treatment (Zhong, et al, 2011), glycation (Zhong, Tu, Liu, Luo, & Liu, 2015;Zhong, et al, 2014b;Zhong, et al, 2013), and PEGylation (Zhong, et al, 2016). It was found that the increase in the antigenicity of β-LG was related to the conformational changes induced by DHPM treatment (Zhong, et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

“…However, there was no significant difference in the antigenicity decrease when β-LG was conjugated with the two main components of fructo-oligosaccharides (FOS)nystose and β-fructofuranosyl nystose (Zhong, et al, 2015). As per Kim, Lee, Go, Ahn, and Hong (2018), kestose, the smallest short-chain FOS, activates the gut immune system that induces tolerance against allergic skin inflammations in atopic dermatitis.…”

Section: Introductionmentioning

confidence: 99%

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