Key factors affecting the immunoreactivity of roasted and boiled peanuts: Temperature and water

Rao, Huan; Tian, Yang; Tao, Shiquan; Tang, Jie; Xi, Li; Xue, Wei

doi:10.1016/j.lwt.2016.05.014

Cited by 25 publications

(35 citation statements)

References 36 publications

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“…On the contrary, the bands 5 and 8 of raw and processed peanuts, respectively, resulted in similar composition (mainly Ara h 3 and Ara h 2), suggesting that these proteins were scarcely affected by the roasting process. Such results were in accordance with what was reported in previous studies [37,38].…”

Section: Varietal Diversity Andsupporting

confidence: 94%

Effects of the Varietal Diversity and the Thermal Treatment on the Protein Profile of Peanuts and Hazelnuts

Angelis

Bavaro

Monaci

et al. 2018

Journal of Food Quality

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Several bu er compositions were compared for their e ciency in protein extraction from both raw and roasted peanut and hazelnut samples, the nal goal being to understand the modi cation of protein solubility upon roasting and maximize the extraction yield. Denaturant conditions provided by urea-TBS bu er resulted in satisfactory extraction yields for both peanut and hazelnut samples, before and after the thermal treatment. In addition, di erent varieties of peanuts and hazelnuts were characterized to highlight the extent of variability in the protein pro le accounted by the varietal factor and eventual di erential resistance among cultivars to protein modi cation induced by the thermal processing. e protein pro le was characterized by gel electrophoresis, and speci c bands were analyzed by micro-HPLC-MS/MS coupled to software-based protein identi cation. No signi cant di erence was observed for the investigated hazelnut cultivars, namely, Campana, Romana, and Georgia, whereas interesting features were presented for the peanut varieties Virginia, Zambia, and China. In particular, Zambia variety lacked two bands of approximately 36 and 24 kDa that were visible in Virginia and China varieties, which could suggest a lower allergenic potential of this particular variety which deserves to be further investigated before drawing nal conclusions.

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Section: Varietal Diversity Andsupporting

confidence: 94%

Effects of the Varietal Diversity and the Thermal Treatment on the Protein Profile of Peanuts and Hazelnuts

Angelis

Bavaro

Monaci

et al. 2018

Journal of Food Quality

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“…Among all of these strategies, thermal processing has been verified to be a promising tool that can lead to the destruction of the secondary and tertiary structures of proteins, along with disulfide bond cleavage and new disulfide bond formation, thereby masking protein epitomes and reducing the allergenicity of the allergen (Rao et al, 2016). Therefore, many studies have investigated the thermal effects on common allergens, primarily the allergens in peanut (Rao et al, 2016), soybean protein (Li, Zhu, Zhou, Peng, & Guo, 2016), milk (Sampson, 2004;Xu, Shi, Yao, Jiang, & Luo, 2015), wheat, and almond (Taheri-Kafrani et al, 2009), as well as egg OVT (Fu et al, 2010;Tong, Gao, Chen, & Li, 2012), at different temperatures. Due to their complex conformational structure, different allergens exhibit different changes in their characteristics.…”

Section: Introductionmentioning

confidence: 99%

Effects of heating, autoclaving and ultra-high pressure on the solubility, immunoreactivity and structure of major allergens in egg

Zhang

Wang

Zhou

et al. 2017

Food and Agricultural Immunology

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Ovotransferrin (OVT) and ovomucoid (OVM) were treated, respectively by different food processing conditions. The protein recovery and immunoreactivity of OVT significantly decreased during heat treatment (P < .05), and aggregates appeared after dry heating at 150°C or 200°C or boiling at 100°C. OVM appeared more stable than OVT under the same treatment. Greatly reduced solubility occurred only after dry heating at 200°C. The immunoreactivity increased after dry heating at 100°C or 150°C or moist heating (60°C, boiling). Autoclave sterilization had a strong effect on the characteristics of both OVT and OVM. Ultra-high pressure had very little effect on OVT and OVM, except at 600 MPa in the moist treatment. Results showed that temperature synergistic processing with water and high pressure had the greatest impact on the characteristics, which could be a potential strategy for mitigating the negative effects of allergens in egg.

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“…Methods from Rao et al (2016) were modified as follows: protein samples were identified by using sodium dodecyl sulphonate polyacrylamide gel electrophoresis (SDS-PAGE) on a mini-protean II gel apparatus (Bio-Rad, USA). Samples in SDS-loading buffer were boiled and loaded (10 μg/lane) on a 12% polyacrylamide gel and afterwards dyed using Coomassie brilliant blue R250 for 40 min, bleached in destaining solution (1.31 M HAc, 1.23 M methanol) for 12 h. BIO-RAD GelDoc 2000 gel imaging system was used to photograph and analyse the pictures of electrophoresis results.…”

Section: Sds-pagementioning

confidence: 99%

Section: Introductionmentioning

confidence: 97%

“…It has been reported that peanut roasted over 130°C for 20 min can significantly reduce the solubility and sensitivity of Ara h 1 (Rao et al, 2016). However, more extreme thermal processing such as roasting at 140°C appeared to enhance IgE-binding capacity of Ara h 1 (Rao et al, 2016). According to Blanc et al (2011), Ara h 1 boiled in the absence or presence of glucose produced aggregates and thus maintained a relatively lower sensitivity.…”

Section: Introductionmentioning

confidence: 99%

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Effect of boiling on the structure and immunoreactivity of recombinant peanut protein Ara h 1

Tian

Rao

Tao

et al. 2018

Food and Agricultural Immunology

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Ara h 1 is a key peanut allergen and its activity is significantly affected by protein intrinsic structure which is found to be regulated by heat treatment, although the molecular basis for this regulation has remained largely unknown. Here, we explored the effect of boiling on the structure and allergenicity of recombinant peanut protein Ara h 1 (rAra h 1). rAra h 1 was purified from E. Coli BL21(DE3) plysS cells and structurally studied. According to the results, rAra h 1 undergoes degradation during the heating process, and the aggregation of fragments happened after 20 min of heating. An increased surface hydrophobic index and a decreased content of α-helixes were found in rAra h 1, indicating a looser protein structure of rAra h 1 caused by heat treatment. Destroyed epitopes during protein degradation and aggregation could be a mechanism of reducing the allergenic nature of rAra h 1 by heat treatment. ARTICLE HISTORY

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Key factors affecting the immunoreactivity of roasted and boiled peanuts: Temperature and water

Cited by 25 publications

References 36 publications

Effects of the Varietal Diversity and the Thermal Treatment on the Protein Profile of Peanuts and Hazelnuts

Effects of the Varietal Diversity and the Thermal Treatment on the Protein Profile of Peanuts and Hazelnuts

Effects of heating, autoclaving and ultra-high pressure on the solubility, immunoreactivity and structure of major allergens in egg

Effect of boiling on the structure and immunoreactivity of recombinant peanut protein Ara h 1

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