Peanut as a source of protein for human foods

Singh, Bharat; Singh, Ummed

doi:10.1007/bf02194085

Cited by 98 publications

(68 citation statements)

References 21 publications

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“…Horsegram is a short day, twining, succulent, annual climbing herb which has trifoliate leaves, white coloured flowers, long linear pubescent pods with curved beak, flattened small seeds with light red, brown, grey, black or mottled testa (Singh, 1991) with photo andthermo sensitive nature (Kumar, 2006). It is mostly grown as catch crop especially under late summer (Kharif) or with the rains after a prolonged drought condition (Prakash et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Seed Borne Mycoflora of Macrotyloma uniflorum L (Horse gram)

Kumari¹,

Saxena²

2017

Int.J.Curr.Microbiol.App.Sci

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Section: Introductionmentioning

confidence: 99%

Seed Borne Mycoflora of Macrotyloma uniflorum L (Horse gram)

Kumari¹,

Saxena²

2017

Int.J.Curr.Microbiol.App.Sci

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“…The crude protein content of whole seed peanuts ranges between 22% -30% [4]. Peanuts have a distinct nutty flavor and desirable texture that places it above all other legumes and oilseeds [5]. Study has shown that, peanut flour which is most commonly used for fortification contains protein ranging in between 47% -55% i.e.…”

Section: Introductionmentioning

confidence: 99%

Effect of Partially De-Oiled Peanut Meal Flour (DPMF) on the Nutritional, Textural, Organoleptic and Physico Chemical Properties of Biscuits

Yadav¹,

Thakur²,

Sunooj³

2012

FNS

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Partially de-oiled peanut meal flour (DPMF) was blended with wheat flour for making biscuits. DPMF at 5, 10, 15 and 20% was used to partially replace wheat flour in biscuits formulation and biscuits thus made were evaluated for nutritional composition, physical characteristics and sensory quality. Chemical analysis of DPMF showed 30.26% crude protein, 10.1% crude fat and 43.65% carbohydrates. The protein content increased nearly 1.5 times in biscuits as a result of incorporated DPMF, coupled with increase in ash content. The force required for breaking biscuits decreased with DPMF addition. On a 9-point hedonic scale, the highest overall acceptability score of 8.6 was obtained with 5% fortification, which was similar to control (8.8). Results demonstrated that biscuits made up of 15% DPMF exhibited all the values within an acceptable range.

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“…They are of particular importance as a nutritional source in developing countries that lack ample supplies of animal protein (1). Peanuts are widely used for the preparation of a variety of foods in the U.S. and are also relied on as a protein extender in developing countries.…”

mentioning

confidence: 99%

Structure of the Major Peanut Allergen Ara h 1 May Protect IgE-Binding Epitopes from Degradation

Maleki

Kopper²,

Shin³

et al. 2000

The Journal of Immunology

240

210

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In the past decade, there has been an increase in allergic reactions to peanut proteins, sometimes resulting in fatal anaphylaxis. The development of improved methods for diagnosis and treatment of peanut allergies requires a better understanding of the structure of the allergens. Ara h 1, a major peanut allergen belonging to the vicilin family of seed storage proteins, is recognized by serum IgE from >90% of peanut-allergic patients. In this communication, Ara h 1 was shown to form a highly stable homotrimer. Hydrophobic interactions were determined to be the main molecular force holding monomers together. A molecular model of the Ara h 1 trimer was constructed to view the stabilizing hydrophobic residues in the three dimensional structure. Hydrophobic amino acids that contribute to trimer formation are at the distal ends of the three dimensional structure where monomer-monomer contacts occur. Coincidentally, the majority of the IgE-binding epitopes are also located in this region, suggesting that they may be protected from digestion by the monomer-monomer contacts. On incubation of Ara h 1 with digestive enzymes, various protease-resistant fragments containing IgE-binding sites were identified. The highly stable nature of the Ara h 1 trimer, the presence of digestion resistant fragments, and the strategic location of the IgE-binding epitopes indicate that the quaternary structure of a protein may play a significant role in overall allergenicity.

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Peanut as a source of protein for human foods

Cited by 98 publications

References 21 publications

Seed Borne Mycoflora of Macrotyloma uniflorum L (Horse gram)

Seed Borne Mycoflora of Macrotyloma uniflorum L (Horse gram)

Effect of Partially De-Oiled Peanut Meal Flour (DPMF) on the Nutritional, Textural, Organoleptic and Physico Chemical Properties of Biscuits

Structure of the Major Peanut Allergen Ara h 1 May Protect IgE-Binding Epitopes from Degradation

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