Effect of tyrosinase-aided crosslinking on the IgE binding potential and conformational structure of shrimp ( Metapenaeus ensis ) tropomyosin

Ahmed, Ifty; Lv, Liangtao; Lin, Hong; Ma, Jian; Chen, Guanzhi; Sun, Lirui; Xu, Lili

doi:10.1016/j.foodchem.2017.12.071

Cited by 46 publications

(50 citation statements)

References 38 publications

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“…The reduction in the allergenicity of turbot PV via Tyr and CA are consistent with the changes in the structural properties. Structural changes might cause the modification of amino acid residues and binding epitopes, which agreed with the results reported in recent studies . Fei et al did some research on crosslinked thermal polymerized arginine kinase (AK) and analyzed the potential allergenicity.…”

Section: Resultssupporting

confidence: 81%

“…Among the three treatments, PPO/CA was the most effective in reducing IgE binding capacity of peanut allergens. More recently, Ahmed et al also observed crosslinks formation and allergenicity reduction, following treatment of shrimp tropomyosin with Tyr/CA.…”

Section: Resultsmentioning

confidence: 91%

“…Intrinsic fluorescence spectra of samples were acquired on a fluorescence spectrophotometer (F‐4600, Hitachi, Tokyo, Japan) at a wavelength of 280 nm (excitation) and 300–400 nm (emission), using 2.5 nm as a constant slit. The PBS was used as a blank solution for all the samples . The experiments were conducted at room temperature.…”

Section: Methodsmentioning

confidence: 99%

“…Furthermore, Maillard reaction can significantly reduce the IgE binding capacity of fish PV . In addition, various non‐thermal processing methods have been investigated for altering the allergenic potential of food proteins, which may cause aggregation, denaturation, crosslinking, oxidation, and glycosylation, subsequently lead to masking or unmasking of allergenic epitopes …”

Section: Introductionmentioning

confidence: 99%

“…Ercili Cura et al observed crosslinking reaction after the addition of Tyr in heated milk. Recently, Ahmed et al investigated the influence of Tyr and caffeic acid (CA) on the allergenicity and structure of major allergens of shrimp. It was found that the protein structure changed greatly, and the immunoglobulin E/immunoglobulin G (IgE/IgG) binding capacity was reduced significantly.…”

Section: Introductionmentioning

confidence: 99%

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Effect of tyrosinase‐catalyzed crosslinking on the structure and allergenicity of turbot parvalbumin mediated by caffeic acid

Tian

Ahmed

et al. 2019

J Sci Food Agric

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BACKGROUND Enzymatic treatment of allergenic protein can alter their functional properties under a mild reaction condition due to specificity of enzymes. Phenolic compounds act as mediators and enhance the crosslinking reactions. The study aimed to assess the changes in the structure and immunoglobulin G (IgG) binding capacity of turbot parvalbumin (PV) upon crosslinking with tyrosinase (Tyr) in the absence and presence of caffeic acid. RESULTS Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE) analysis revealed the appearance of higher molecular weight bands (24, 36 kDa) in the crosslinked PV. The secondary structure of crosslinked PV became loosened and disordered. The results of intrinsic fluorescence and ultraviolet absorption spectral analyses, as well as surface hydrophobicity and free amino group analyses also revealed structural changes. As observed by western blot analysis, the intensity of the PV bands reduced upon Tyr treatment, indicating reduced binding of specific IgG to PV. Moreover, the indirect ELISA (enzyme‐linked immunosorbent assay) analysis confirmed that the IgG binding ability of crosslinked PV was reduced 34.94%. CONCLUSION Enzymatic treatment mitigated the allergenicity of fish PV, which was closely related to the alterations in the conformational structure. This treatment showed potential for developing hypoallergenic fish products under mild reaction conditions. © 2019 Society of Chemical Industry

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Section: Resultssupporting

confidence: 81%

Section: Resultsmentioning

confidence: 91%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Effect of tyrosinase‐catalyzed crosslinking on the structure and allergenicity of turbot parvalbumin mediated by caffeic acid

Tian

Ahmed

et al. 2019

J Sci Food Agric

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Quantification of crustacean tropomyosin in foods using high‐performance liquid chromatography–tandem mass spectrometry method

Wang

Sun

et al. 2021

J Sci Food Agric

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BACKGROUND Allergic reactions to crustacean products have been increasing owing to the rising consumption. Tropomyosin (TM) is the main crustacean allergen; it has a coiled‐coil structure, which shows stability to various food processing methods. Crustacean processed products have been used in several food products, thereby causing greater difficulties in detecting TM in these products. We aimed to develop an assay based on high‐performance liquid chromatography–tandem mass spectrometry for the accurate and reproducible quantification of crustacean TM in foods. RESULTS The three peptides IQLLEEDLER, LAEASQAADESER, and IVELEEELR were selected as peptide markers, and the peptide IVELEEELR was selected as the quantitative marker. Extraction conditions and enzymatic digestion conditions were completely optimized. The extraction solution of Tris–hydrochloric acid buffer (50 mmol L−1, pH 7.4) containing 1 mol L−1 potassium chloride and the enzymatic treatment at 1:15 ratio (enzyme/protein, m/m) for 13 h showed excellent efficiency. The method exhibited a good linear relationship, with the qualified coefficient of determination (R2 = 0.9994) in the wide range of 1 to 1000 μg L−1. The accuracy was validated based on spiked recovery at three spiking levels (12.5, 25.0, and 50.0 μg kg−1, TM/matrix) in blank matrices that included chicken sausages, beef balls, and egg–milk biscuits. The recoveries ranged from 91% to 109% with qualified relative standard deviations <15% with the limit of quantification (of 1.6 mg kg−1, TM/matrix). CONCLUSION This new approach can be used for the qualitative and quantitative detection of crustacean TM in various food matrices. © 2021 Society of Chemical Industry.

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An overview of smart packaging technologies for monitoring safety and quality of meat and meat products

et al. 2018

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The food packaging sector has experienced much development since its inception. In the past few decades, innovations in packaging sector have led to the development of smart packaging (SP) systems that carve a niche in a highly competitive food industry. SP systems have great potential for improving the shelf‐life, and safety of food products apart from their basic roles of protecting the products against unwanted biological, chemical, and physical damage and keeping them clean. Indicators and sensors, SP components, are used for real‐time monitoring of meat quality and subsequently inform the retailers and consumers about the freshness, microbiological, temperature, and shelf life status of the products. Barcodes and radio‐frequency identification tags are employed in meat packaging for real‐time information about the authenticity, and traceability of the products in the supply chain. Recently, innovations in SP technologies resulted in fast, sensitive, and effective detection, sensing, and record keeping of freshness, microbiological, and shelf life status of meat and meat products. The SP system shows promise for extensive utilization in the meat industry in response to the consumer appreciation for safe, and quality meat products, as well as their waste reduction notions. This paper gives an updated overview of ongoing scientific research, and recent technological advances that offer the perspectives of developing smart meat packaging systems that are capable of monitoring the physical, microbial, and chemical changes of the package contents from producer to the point of sale and even beyond, and remediating potential adverse reactions.

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Effect of tyrosinase-aided crosslinking on the IgE binding potential and conformational structure of shrimp ( Metapenaeus ensis ) tropomyosin

Cited by 46 publications

References 38 publications

Effect of tyrosinase‐catalyzed crosslinking on the structure and allergenicity of turbot parvalbumin mediated by caffeic acid

Effect of tyrosinase‐catalyzed crosslinking on the structure and allergenicity of turbot parvalbumin mediated by caffeic acid

Quantification of crustacean tropomyosin in foods using high‐performance liquid chromatography–tandem mass spectrometry method

An overview of smart packaging technologies for monitoring safety and quality of meat and meat products

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