Changes in the structure, digestibility and immunoreactivities of glycinin induced by the cross‐linking of microbial transglutaminase following heat denaturation

Yang, Anshu; Xia, Jiaheng; Gong, Yuqing; Deng, Han; Wu, Zhihua; Li, Xin; Tong, Ping

doi:10.1111/ijfs.13507

Cited by 25 publications

(14 citation statements)

References 29 publications

(42 reference statements)

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“…The IgG‐ and IgE‐binding capacity of SM and FSM proteins were assessed through competitive inhibition ELISA, as previously reported, with few modifications . In brief, the native SM protein was coated (2 and 10 μg/mL for IgG and IgE tests, respectively, 100 μL per well) in carbonate buffer overnight at 4 °C.…”

Section: Methodssupporting

confidence: 72%

“…The IgG-and IgE-binding capacity of SM and FSM proteins were assessed through competitive inhibition ELISA, as previously reported, with few modifications. 19 In brief, the native SM protein was coated (2 and 10 μg/mL for IgG and IgE tests, respectively, 100 μL per well) in carbonate buffer overnight at 4 ∘ C. For the competitive proteins, 60 μL/well of samples (1, 2, 5, 10, and 20 μg/mL for IgG-binding; 20, 40, 80, 160, and 320 μg/mL for IgE-binding) was mixed with 60 μL/well of rabbit anti-soybean sera (diluted 1:5000, for IgG binding test) or soybean-allergic patients' serum pool (diluted 1:10, for IgE binding test). For the IgE binding test, HRP-conjugated streptavidin (diluted 1:60) was also added.…”

Section: Elisamentioning

confidence: 99%

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Allergenicity reduction and rheology property of Lactobacillus‐fermented soymilk

Xia

Yang

et al. 2019

J Sci Food Agric

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BACKGROUND This study aimed to investigate the reduction in the potential allergenicity of soymilk, and its rheological properties, after fermentation with Lactobacillus. Soymilk (SM) was fermented with Lactobacillus brevis and Lactobacillus sp. The molecular weight of fermented soymilk (FSM) was characterized using sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS‐PAGE), and the potential allergenicity of FSM was analyzed using enzyme‐linked immunosorbent assay in vitro and the BALB/c mouse model to detect changes in histamine, mouse mast cell protease‐1 (mMCP‐1), allergen‐specific IgG/IgE, and cytokine levels and histomorphology of jejunum in vivo. RESULTS The SDS‐PAGE and enzyme linked immunosorbent assay (ELISA) showed that allergens of soybean (β‐conglycinin and acidic subunit of glycinin) were almost degraded, and their immunoreactivity was decreased. In the BALB/c mouse model, the FSM group did not show anaphylactic shock symptoms compared with the SM group. Moreover, a tendency toward decreased serum allergen‐specific IgG/IgE levels, plasma histamine levels, and mMCP‐1 concentrations was observed in the FSM group. Furthermore, Th2‐related cytokines were decreased, while IFN‐γ production increased in spleen cell cultures. The intestinal villus was slightly damaged after the challenge. All these findings indicated that the Th1/Th2 balance in the FSM group shifted toward a Th1 response, ultimately reducing the potential allergenicity of FSM. Rheological assessment suggested that FSM has good viscous and pseudoplastic properties. CONCLUSION Fermentation might be a promising method for producing tasty, hypoallergenic soybean products. © 2019 Society of Chemical Industry

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Section: Methodssupporting

confidence: 72%

Section: Elisamentioning

confidence: 99%

Allergenicity reduction and rheology property of Lactobacillus‐fermented soymilk

Xia

Yang

et al. 2019

J Sci Food Agric

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“…Glycinin extraction was conducted following a previous protocol [ 12 ]. All centrifugation was performed at 10,000× g , 4 °C for 15 min in a centrifuge (TGL-16R, Shan Dong BaiO Medical Technology CO., LTD., Shandong, China).…”

Section: Methodsmentioning

confidence: 99%

“…Several technologies have been developed to reduce the antigenicity of soy proteins, including thermal and non-thermal processing (e.g., high hydrostatic pressure treatment, enzymatic hydrolysis, genetic modification and microbial fermentation) [ 3 , 11 , 12 , 13 , 14 ]. Fermentation, an ancient processing approach, demonstrated improvements in the functional and nutritional properties of soy products [ 15 ].…”

Section: Introductionmentioning

confidence: 99%

The Conformational Structural Change of Soy Glycinin via Lactic Acid Bacteria Fermentation Reduced Immunoglobulin E Reactivity

Liu

Wang

Liu

et al. 2021

Foods

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This study investigated the fermentation of isolated soy glycinin by using the Lactiplantibacillus plantarum B1-6 strain, its reduction effect on immunoglobulin E (IgE) reactivity, the relationship with protein aggregation/gelation state and conformational changes. Fermentation was performed under different glycinin concentrations (0.1%, 0.5%, 1% and 2%, w/v) and varied fermentation terminal pH levels (FT-pH) (pH 6.0, 4.5, 4.0 and 3.5). L. plantarum B1-6 showed potency in reducing immunoreactivity to 0.10–69.85%, as determined by a sandwich enzyme-linked immunosorbent assay. At a FT-pH of 6.0 and 4.5, extremely low IgE reactivity (0.1–22.32%) was observed. Fermentation resulted in a great increase (2.31–6.8-fold) in particle size and a loss of intensity in A3 and basic subunits. The conformation of glycinin was altered, as demonstrated by improved surface hydrophobicity (1.33–7.39-fold), decreased intrinsic fluorescence intensity and the α-helix structure. Among the four selected concentrations, glycinin at 1% (w/v, G-1) evolved the greatest particles during fermentation and demonstrated the lowest immunoreactivity. Principal component analysis confirmed that particle size, intrinsic fluorescence intensity, α-helix and ionic bond were closely related to immunoreactivity reduction.

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“…The results inferred that alkaline pH shifting in conjunction with TG crosslinking can be an effective way to diminish the IgE-binding of glycinin. Yang et al (2017) observed that sequential heat treatment and enzymatic crosslinking unfolded the structure of glycinin and reduced the digestion stability. Bai et al (2020) evaluated the sensitization effect of crosslinked tofu with microbial TG in a BALB/c mouse model.…”

Section: Soybean Allergymentioning

confidence: 99%

Enzymatic crosslinking and food allergenicity: A comprehensive review

Ahmed

Chen

et al. 2021

Comp Rev Food Sci Food Safe

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Food allergy has become a major global public health concern. In the past decades, enzymatic crosslinking technique has been employed to mitigate the immunoreactivity of food allergens. It is an emerging non-thermal technique that can serve as a great alternative to conventional food processing approaches in developing hypoallergenic food products, owing to their benefits of high specificity and selectivity. Enzymatic crosslinking via tyrosinase (TYR), laccase (LAC), peroxidase (PO), and transglutaminase (TG) modifies the structural and biochemical properties of food allergens that subsequently cause denaturation and masking of the antigenic epitopes. LAC, TYR, and PO catalyze the oxidation of tyrosine side chains to initiate protein crosslinking, while TG initiates isopeptide bonding between lysine and glutamine residues. Enzymatic treatment produces a high molecular weight crosslinked polymer with reduced immunoreactivity and IgE-binding potential. Crosslinked allergens further inhibit mast cell degranulation due to the lower immunostimulatory potential that assists in the equilibration of T-helper (Th)1/Th2 immunobalance. This review provides an updated overview of the studies carried out in the last decade on the potential application of enzymatic crosslinking for mitigating food allergenicity that can be of importance in the context of developing hypoallergenic/non-allergenic food products.

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Changes in the structure, digestibility and immunoreactivities of glycinin induced by the cross‐linking of microbial transglutaminase following heat denaturation

Cited by 25 publications

References 29 publications

Allergenicity reduction and rheology property of Lactobacillus‐fermented soymilk

Allergenicity reduction and rheology property of Lactobacillus‐fermented soymilk

The Conformational Structural Change of Soy Glycinin via Lactic Acid Bacteria Fermentation Reduced Immunoglobulin E Reactivity

Enzymatic crosslinking and food allergenicity: A comprehensive review

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