Allergenicity of roasted peanuts treated with a non-human digestive protease

Yu, Jianglong; Hernández, Michelle; Li, Hao; Goktepe, Ipek; Robinette, Carole; Auerbach, Amy; Peden, David B.; Ahmedna, Mohamed

doi:10.1016/j.foodres.2015.01.007

Cited by 22 publications

(8 citation statements)

References 31 publications

(38 reference statements)

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“…Oxidative stability and allergenicity are two major concerns of peanuts. While protease hydrolysis of peanuts has shown to be effective and practical in reducing allergen content and allergenicity of roasted and raw peanuts [ 29 , 30 , 31 , 32 ], the effect of hydrolysis on the oxidative stability has not been investigated. Oxidation deterioration limits the shelf life, reduces the nutritional value, and renders peanuts unacceptable by consumers because of the rancid flavor.…”

Section: Discussionmentioning

confidence: 99%

“…Agricultural and food scientists have made significant effort to reduce the allergenic potential of peanuts. Some previous studies demonstrated that protease hydrolysis of peanuts or peanut flour is an effective post-harvest approach to mitigate the allergenicity of peanuts [ 28 , 29 , 30 , 31 , 32 ]. However, the breaking down of protein molecules by proteolytic enzyme modifies the surface and internal structure of peanut kernels, which may result in leaching of antioxidant vitamin E originally present in peanut, thus changing in oxidative stability.…”

Section: Introductionmentioning

confidence: 99%

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Oxidative Stability of Protease Treated Peanut with Reduced Allergenicity

Smith

Idris

et al. 2020

Foods

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Oxidative stability and allergenicity are two major concerns of peanuts. This study evaluated the impact of protease treatment of peanuts on its oxidative stability during storage. The raw and dry-roasted peanut kernels were hydrolyzed with Alcalase solution at pH 7.5 for 3 h. The contents of Ara h 1, Ara h 2, and Ara h 6 in peanuts were determined before and after enzyme treatment by a sandwich ELISA. After drying, the samples were packed in eight amber glass jars and stored at 37 °C for 1–8 weeks. Controls are untreated raw and dry-roasted peanuts packed and stored in the same way as their treated counterparts. Samples were taken biweekly to determine peroxide value (PV) and thiobarbituric acid reactive substances (TBARS) as indicators of oxidation (n = 3), and to determine antioxidant activity. Alcalase treatment reduced intact major allergens Ara h 1, Ara h 2, and Ara h 6 by 100%, 99.8%, and 85%, respectively. The PVs of Alcalase-treated raw and roasted peanuts was lower than those of untreated (p < 0.05) over the 8-week storage. The TBARS of Alcalase-treated raw peanuts were slightly higher than that of untreated (p < 0.05), but the TBARS of Alcalase-treated dry-roasted peanuts were slightly but significantly lower than that of untreated (p < 0.05). The protease treatment increased the antioxidant activities including reducing power, DPPH free radical scavenging capacity, and metal chelating capacity of peanuts.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Oxidative Stability of Protease Treated Peanut with Reduced Allergenicity

Smith

Idris

et al. 2020

Foods

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“…These treatments are effective because they induce exposure to enzyme cleavage sites. To loosen the peanut kernel structure, roasted peanut kernels were pretreated with ultrasound for 1 h at 50 Hz before hydrolysis with Alcalase using different concentrations (Yu et al, 2015). The authors reported decreased Ara h 1 and Ara h 2 concentrations in both insoluble and soluble peanut portions compared to the control (untreated peanuts).…”

Section: Alleviating Allergenicitymentioning

confidence: 99%

Enzymatic Modification of Plant Proteins for Improved Functional and Bioactive Properties

Olatunde

Owolabi²,

Fadairo³

et al. 2022

Food Bioprocess Technol

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Plant-based proteins have shown great potential as an alternative substitute for animal proteins to meet the increasing global demand. Nevertheless, several limitations mitigate plant-based protein application and utilization. As a panacea to meeting the market demand, it is imperative to modify plant-based proteins to produce improved quality and technofunctionalities compared to conventional animal protein ingredients. Enzymatic, chemical, and physical modi cations have been used for plant-based proteins, which has shown exciting results in improving their techno-functional properties, digestibility, and inherent allergenicity. Among these modi cation methods, the low cost, limited time, high sensitivity, and high reproducibility give enzymatic modi cation leverage over chemical and physical methods. This review gave a concise summary of the advantages and disadvantages of enzymatic modi cations. The e cacy of enzymatic modi cation in producing protein ingredients from plant sources with improved techno-functional properties, digestibility, and alleviated allergenicity was discussed. Furthermore, the application of enzymatic modi cation in the production of bioactive compounds with health-bene cial properties adds in no small measure to the novelty of this review.

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“…), and lamination (combination of ultrasound with enzymatic treatment, heat-induced glycosylation, etc.) have been adopted to study their actions of attenuating the risk of protein anaphylaxis. − Among modern physical processing methods, researchers have focused extensive attention on irradiation, which can not only change the immunogenicity of food allergens resulting from high-energy rays but can also improve the quality of food items by prolonging shelf life without weakening the nutrient and flavor. , In addition, as a typical nonthermal technology, irradiation treatment can bypass the disadvantages of low efficiency, environmentally unfriendly nature, and complex operation of other processing methods to be suitable for industrial application …”

Section: Introductionmentioning

confidence: 99%

Investigation of the Mechanism of ⁶⁰Co Gamma-Ray Irradiation-Stimulated Oxidation Enhancing the Antigenicity of Ovalbumin by High-Resolution Mass Spectrometry

Bian

Wang

et al. 2022

J. Agric. Food Chem.

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60Co gamma-ray irradiation-induced antigenicity changes in ovalbumin (OVA) were investigated, and the molecular mechanism was analyzed. Irradiation treatment at 0–100 kGy could significantly enhance the IgG/IgE binding ability of OVA in a dose-dependent paradigm by concomitant oxidative modification, which exhibited color browning and an increase in carbonyl content caused by high-penetrable rays. More allergenic epitopes of OVA were exposed after irradiation treatment reflected by structural changes including the unfolding of tertiary structure, the conversion of α-helix structures to β-sheet and random coil structures, and the cleavage of several peptide bonds. Meanwhile, three oxidation sites of K46, T49, and N260 located in key linear epitopes were observed, which might increase the allergenic ability of OVA via the disaggregation of noncovalent bonds and the unwinding of α-helix structures. Conclusively, irradiation may enhance the potential allergenicity of OVA by oxidative modification, which provides theoretical guidance for effectively controlling the oxidation of proteins in the irradiation process.

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Allergenicity of roasted peanuts treated with a non-human digestive protease

Cited by 22 publications

References 31 publications

Oxidative Stability of Protease Treated Peanut with Reduced Allergenicity

Oxidative Stability of Protease Treated Peanut with Reduced Allergenicity

Enzymatic Modification of Plant Proteins for Improved Functional and Bioactive Properties

Investigation of the Mechanism of ⁶⁰Co Gamma-Ray Irradiation-Stimulated Oxidation Enhancing the Antigenicity of Ovalbumin by High-Resolution Mass Spectrometry

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Allergenicity of roasted peanuts treated with a non-human digestive protease

Cited by 22 publications

References 31 publications

Oxidative Stability of Protease Treated Peanut with Reduced Allergenicity

Oxidative Stability of Protease Treated Peanut with Reduced Allergenicity

Enzymatic Modification of Plant Proteins for Improved Functional and Bioactive Properties

Investigation of the Mechanism of 60Co Gamma-Ray Irradiation-Stimulated Oxidation Enhancing the Antigenicity of Ovalbumin by High-Resolution Mass Spectrometry

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Product

Resources

About

Investigation of the Mechanism of ⁶⁰Co Gamma-Ray Irradiation-Stimulated Oxidation Enhancing the Antigenicity of Ovalbumin by High-Resolution Mass Spectrometry