Comparison of recovery and immunochemical detection of peanut proteins from differentially roasted peanut flour using ELISA

2019 ◽  
Vol 292 ◽  
pp. 32-38 ◽  
Author(s):  
Shyamali Jayasena ◽  
Stef J. Koppelman ◽  
Balunkeswar Nayak ◽  
Steve L. Taylor ◽  
Joseph L. Baumert
2021 ◽  
Author(s):  
Apekshita Singh ◽  
Soom Nath Raina ◽  
Manisha Sharma ◽  
Manju Chaudhary ◽  
Suman Sharma ◽  
...  

Peanut (Arachis hypogaea L.) is an important grain legume crop of tropics and subtropics. It is increasingly being accepted as a functional food and protein extender in developing countries. The seed contains 36% to 54% oil, 16% to 36% protein, and 10% to 20% carbohydrates with high amounts of P, Mg, Ca, riboflavin, niacin, folic acid, vitamin E, resveratrol and amino acids. Seed contains 32 different proteins comprised of albumins and globulins. The two-globulin fractions, arachin and non-arachin, comprise approximately 87% of the peanut seed proteins. Peanut worldwide is mainly used for oil production, consumption as raw, roasted, baked products, peanut butter, peanut flour, extender in meat product formulations, confectionary and soups. Peanut proteins have many properties such as good solubility, foaming, water/oil binding, emulsification that make them useful in various food products. Very limited studies have been carried out in peanut functional properties, which has been reviewed in the present article. Adequate modifications can be done in protein functionality that are influenced by pH, temperature, pressure etc. However, some individuals develop severe IgE-mediated allergies to peanut seed proteins. Thus, methods to improve nutrition and reduce allergenicity have also been discussed. Within the last decade, manipulations have been done to alter peanut chemistry and improve nutritional quality of peanuts and peanut products. Hence, improved comprehensive understanding of functional properties and nutritional chemistry of peanut proteins can generate better source of food grain to meet nutritional requirement of growing population. In the present review, composition of peanut seed proteins, functional properties, nutritional components and nutraceutical value have been discussed with respect to beneficial aspects to health, reducing hunger and usage in food end products.


2005 ◽  
Vol 68 (8) ◽  
pp. 1712-1719 ◽  
Author(s):  
L. CHEN ◽  
R. D. PHILLIPS

Partially defatted peanut flour was processed in a twin-screw extruder. Resulting extrudates were dried, ground, and incubated with simulated gastric fluid for various time periods. Soluble protein content of the resulting digesta was measured after 10% trichloroacetic acid treatment to evaluate the digestibility. In vitro digestion using pepsin increased the solubility of peanut protein in 10% trichloroacetic acid solution from 2 to 6% to 65 to 75%. Four strong IgE-binding subunits (65, 22, 17, and 14 kDa) were found with immunoblotting in peanut proteins extracted from unextruded peanut flour; no IgE-binding bands were observed in extrudates. The 65-kDa (putative Ara h 1) subunit was insolubilized during extrusion, and its IgE-binding property was susceptible to in vitro digestion. Following extrusion cooking, no IgE-binding bands were detected by immunoblotting, including the strongly IgE-binding 14-kDa fraction, a strong IgE-binding band from native peanut protein that is stable in pepsin. The 22- and 17-kDa (putative Ara h 2) subunits retained a small amount of IgE-binding potential and became susceptible to pepsin hydrolysis after extrusion.


Nutrients ◽  
2018 ◽  
Vol 10 (9) ◽  
pp. 1281 ◽  
Author(s):  
Stef Koppelman ◽  
Mieke Smits ◽  
Monic Tomassen ◽  
Govardus de Jong ◽  
Joe Baumert ◽  
...  

The oral mucosa is the first immune tissue that encounters allergens upon ingestion of food. We hypothesized that the bio-accessibility of allergens at this stage may be a key determinant for sensitization. Light roasted peanut flour was suspended at various pH in buffers mimicking saliva. Protein concentrations and allergens profiles were determined in the supernatants. Peanut protein solubility was poor in the pH range between 3 and 6, while at a low pH (1.5) and at moderately high pHs (>8), it increased. In the pH range of saliva, between 6.5 and 8.5, the allergens Ara h2 and Ara h6 were readily released, whereas Ara h1 and Ara h3 were poorly released. Increasing the pH from 6.5 to 8.5 slightly increased the release of Ara h1 and Ara h3, but the recovery remained low (approximately 20%) compared to that of Ara h2 and Ara h6 (approximately 100% and 65%, respectively). This remarkable difference in the extraction kinetics suggests that Ara h2 and Ara h6 are the first allergens an individual is exposed to upon ingestion of peanut-containing food. We conclude that the peanut allergens Ara h2 and Ara h6 are quickly bio-accessible in the mouth, potentially explaining their extraordinary allergenicity.


Diabetes ◽  
1993 ◽  
Vol 42 (6) ◽  
pp. 826-832 ◽  
Author(s):  
T. Mitsuhashi ◽  
H. Nakayama ◽  
T. Itoh ◽  
S. Kuwajima ◽  
S. Aoki ◽  
...  

2021 ◽  
Vol 345 ◽  
pp. 128764
Author(s):  
Yeming Chen ◽  
Hongsheng Zhang ◽  
Caimeng Zhang ◽  
Xiangzhen Kong ◽  
Yufei Hua

1994 ◽  
Vol 77 (5) ◽  
pp. 1275-1287 ◽  
Author(s):  
Petra M Krämer ◽  
Qing X Li ◽  
Bruce D Hammock

Abstract The integration of liquid chromatography (LC) with immunochemical detection combines the superior separation power of LC and the sensitivity and specificity of immunoassays. This approach is shown with 3 LC systems (Perkin-Elmer, C18 RP, 4.6 mm; Varian, C18 RP, 1 mm microbore; Michrom, C18 RP, 1 mm microbore) Integrated with an enzyme-linked immunosorbent assay (ELISA) selective for five 4-nitrophenols. The nitrophenols were separated with the 3 LC systems with isocratic runs of 15 to 20 min. Microbore LC separation showed a 10-20 times reduction in solvent amount compared to conventional separation. LC–immunoassay was about 8- to 10-fold more sensitive compared with LC with UV detection. Integrated LC–immunoassay proved to be a very selective method when 2-methylphenol was injected with an equimolar mixture of 2-amino-4-nitrophenol and 3-methyl-4-nrtrophenol; 2-methy I phenol does not crossreact with the serum used. Only 2 peaks could be seen in the detection, even when 2-methylphenol was present in very high amounts (3000 pmol). Further, the EUSA-LC detection proved to be selective and sensitive for complex matrixes. 2-Amlno-4-nitrophenol was clearly identified in spiked extracts of soil and plant, even when a very small amount (2.4 ng) was injected. Although LC–immunoassay is more labor intensive than LC with UV detection, it offers great advantages in multiresidue analysis and is generally applicable for peak confirmation.


2010 ◽  
Vol 88 (5) ◽  
pp. 727-732 ◽  
Author(s):  
Shao Bing Zhang ◽  
Qi Yu Lu ◽  
Hongshun Yang ◽  
Yu Li ◽  
Shuai Wang

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