Peanut Protein Research Paper

Nutritional composition of peanuts
The types of protein in different varieties of peanuts collected from different part of the world were found same, while the amount of these proteins was different in those varieties. Beside this the IgE binding properties of different peanut varieties were also the same as Koppleman et al., [12]. Highly processed oil (acid extracted, heat distilled) on other hand does not contain peanut protein and can safely be consumed by allergic patients. However, the cold pressed or cold extruded peanut oils, with processing at lower temperatures may contain traces of peanut protein and may induce allergic reactions in allergic subjects [13]. Table-1 shows the nutritional composition of peanuts and Table -2 shows amino

The molecular weight of this glycoprotein is about 65,000. This protein is similar to the conglycinin from soy proteins with the major IgE epitopes within this extension region. Ara h 1 is a protein with high thermal stability but showed minor structural changes in 5M urea. It has also been observed that few of the IgE binding epitopes of Ara h1 are resistant to pepsin degradation [22].
ARA h 2
Ara h 2 is a glycoprotein of 17.5 kDa and was initially identified from crude peanut extracts. Ara h 2, a glycoprotein with an isoelectric point (pI) of 5.2 that resembles to a protein from 2S albumin family i.e. delta conglutin. Ara h 2 is known to be a storage protein that can act as a trypsin inhibitor [19]. The Ara h 2 is an aciduric protein that can with stand the degradation by the digestive enzymes that might be the reason that it is recognized by serum IgE from most peanut-allergic patients [23].
ARA h

The amino acid sequence of Ara h 7 is 53% similar to Ara h 6, while 35% similar to Ara h 2 [27], but are less stable than both due to conservation of only two disulphide bonding. Schmidt et al., [30] enriched and separated peanut proteins of molecular weight less than 20 kDa on 2D gel electrophoresis. After mass spectroscopic analysis, two isoallergens were found one of which had an additional pro-peptide cleavage point. Furthermore, the putative cleavage point demonstrates the biological function of conglutins as an amylase/trypsin