Legumes peanuts

Vitamin (thiamine) prevents the disease or symptoms of beriberi. Food sources for this vitamin are meats, wheat germ, whole grain and enriched bread, legumes, peanuts, peanut butter, and nuts. 

Folate-rich foods and reduced risk of neural tube defects leafy vegetables, legumes, peanuts... 

Mycotoxias fiad thek way kito the human diet by way of mold-contaminated cereal and legume crops, meat, and milk products. Com and peanuts probably represent the most common sources of mycotoxias ki the human diet. Many mycotoxias are acutely toxic as well as being poteat carckiogeas (86). 

The dry seed crops that have been used as host plants for molecular farming include the cereals maize, rice, wheat and barley (see also Chapter 4), and the grain legumes soybean, pea, pigeon pea and peanut. Maize, rice, wheat, barley, soybean and pea have been investigated as general production platforms, while pigeon pea and peanut have been used solely for the expression of animal vaccine candidates. The major... 

The protein content of cookies was markedly influenced by the addition and protein content of the various legume flours (Figure 4). Each increment of peanut flour raised the total protein content in cookies by 1.5%. Increases of 1.4% occurred with soy flour and 0.5% with cowpea flour. 

Follow-up studies utilized finely-milled legume flours and the addition of soybean flour as a fat-control agent in an effort to improve doughnut quality (5). The legume products and doughnuts prepared from them are shown in Figure 5. On a dry weight basis, peanut flour from solvent extracted peanuts (PF-SE) contained 0.9% fat and 54.4% protein while cowpea flour (CF) contained 1.4% fat and 25.5% protein. Peanut flour from partially defatted untoasted peanuts (PF-PD-U) contained 34.5% fat and 34.9% protein while peanut flour from partially defatted peanuts toasted at 160°C contained 34.4% fat and 37.6% protein. 

LF = 10% legume flour (peanut or cowpea), LF + S 10% legume flour (peanut or cowpea) + 3% soybean flour. Reproduced with permission from Ref. 5. Copyright 1982, The American Peanut Research and Education Society. 

Some legumes, including raw soy or peanut flour are known to contain certain antinutritional factors such as proteinase inhibitors and hemagglutinins or lectins (21,22). These factors can be inactivated, for the most part, by moist heat, during processing. Interestingly, peanut flour contained more trypsin inhibitor and lectin than did soy flour (22). 

Wehmeyer et al. (1969), Bower et al. (1988), and Amarteifio and Moholo (1998) reported the content of carbohydrate to be 23%, 24%, and 19%, respectively. These values have been obtained indirectly as the difference between 100% and the content of proteins, lipids, and minerals. Holse et al. (2010) found that the content of carbohydrate was dominated by total dietary fiber as it varied between 18.7% and 26.8% dm (Table 5.2). The majority of the dietary fiber is insoluble as only about 4% of the dietary fibers are soluble. Comparing the content of total dietary fiber of morama bean with the content of peanut (9% dm) and soybean (10% dm) (U.S. Department of Agriculture, 2007), it appears that the morama bean has a considerably higher level of indigestible carbohydrates. Holse et al. (2010) also reported a very low starch content, which is in contrast to other legumes, in which starch is usually the most abundant carbohydrate... 

Sufficient protein can generally be obtained in a vegetarian diet by combining a legume, such as peas or beans, with a grain, such as wheat or corn. Familiar meals containing such a combination include a peanut butter sandwich, corn tortillas and refried beans, and rice and toffi. 

Isoflavones Inhibit estrogen uptake destroy cancer enzymes Beans, peanuts and other legumes, peas... 

The Bowman-Birk type protease inhibitors represent a class of low molecular weight, cysteine-rich proteins found in legume seeds (.10). The major Bowman-Birk inhibitor in soybean seeds is a double-headed protein capable of blocking the activity of both trypsin and chymotrypsin. This protein represents approximately 4% of the total protein in soybean seeds (1J ). In contrast to the soybean trypsin inhibitor (Kunitz), the "double-headed inhibitor (referred to as BB) is typical of protease inhibitors present in a large number of legume seeds for example, peanuts (12) chick peas (33)5 kidney beans (3JO adzuki beans (33) lima beans (16). 

Burks, A.W., Shin, D., Cockrell, G., Stanley, J.S., Helm, R.M., and Bannon, G.A. 1997. Mapping and mutational analysis of the IgE-binding epitopes onArah 1, a legume vicilin protein and a major allergen in peanut hypersensitivity. EurJ Biochem 245 334—339. 

CROSS-REACTIVITY AMONG PEANUT AND OTHER MEMBERS OF THE LEGUME FAMILY... 

Wensing et al. (2003) reported that three patients with histories of severe anaphylaxis after ingestion of pea had peanut-related symptoms that occurred due to cross-reactive IgE initially raised against pea allergens. The molecular basis for this cross-reactivity was vicilin homologues in pea and peanut (Ara h 1). Two patients also reported symptoms to other legumes (kidney bean, lentil, and... 

Bonds, R.S., Maleki, S.J., McBride, J., and Cheng, H. 2006. In vitro cross-reactivity of peanut allergens with other legumes. J Allergy Clin Immunol 11 154. 

Oleosins are hydrophobic plant proteins found only in association with small storage oil drops. These oil bodies are discrete spherical organelles, mainly composed of triacylglycerols and are surrounded by a phospholipids/oleosin annulus. Several oleosins were lately described, confirming that all of them comprise three distinct domains a conserved hydrophobic domain of about 70 amino acid residues being particularly rich in aliphatic amino acids flanked by an N- and a C-terminal domain, which are more hydrophilic with less conserved amino acid sequences. Allergenic oleosins were identified in sesame (Ses i 4 and Ses i 5), nuts (peanut and hazelnut oleosins), legumes, and seeds (Capuano et al. 2007, Leduc et al. 2006). 

Burks, A.W., Cockrell, G., Connaughton, C. et al. 1994. Identification of peanut agglutinin and soybean trypsin inhibitor as minor legume allergens. Int Arch Allergy Immunol 105 143-149. 

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