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Peanut proteins

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. [Pg.18]

Soya proteins mid derivatives (globulin 7s, globulin 11s) Rice and manioc proteins Pea proteins Peanut (conarachin), pistachio, cotton, sunflower, and rapeseed proteins... [Pg.549]

Food proteins are important in determining the characteristics of many food products. Frequently the protein used influences more than one characteristic of the food. The protein selected will vary as a function of the protein, the formulation of the food, and the processing of the product. The most common proteins used as food ingredients include egg proteins [83,84], soy proteins [85,86], milk proteins [87,88,89], wheat gluten [90], and fish proteins [91]. Other proteins have been used to a lesser degree and include rapeseed protein, sunflower protein, pea protein, cottonseed protein, peanut protein, and blood plasma. [Pg.303]

Specificity Almond Hazelnut Hazelnut Peanut residue Peanut proteins Peanut proteins. Peanut... [Pg.386]

Specificity Standards Ara hi 6 (10% protein) Peanut proteins 5 Peanut proteins 5 Ara h2 6 protein 7 5... [Pg.394]

Table P-1 presents in summary form the story of peanut products and uses for human food. In addition to the products listed therein, the following human food products are among those that have not yet reached wide distribution peanut protein, peanut milk, peanut cheese, boiled fresh peanuts, canned boiled peanuts-shelled and unshelled, frozen boiled peanuts, peanut bread, peanut cereals, and numerous products that may be developed from these. Table P-1 presents in summary form the story of peanut products and uses for human food. In addition to the products listed therein, the following human food products are among those that have not yet reached wide distribution peanut protein, peanut milk, peanut cheese, boiled fresh peanuts, canned boiled peanuts-shelled and unshelled, frozen boiled peanuts, peanut bread, peanut cereals, and numerous products that may be developed from these.
The nutritional value of peanut protein compares favorably with other vegetable proteins however, when compared with animal proteins, peanut protein is found to be deficient in lysine and methionine. [Pg.408]

Soybean meal is the most frequently used source of supplemental protein in the United States (5). Cottonseed meal is another important protein supplement. Both meals are by-products from oil extraction of the seeds. Canola meal is derived from rapeseed low in emcic acid [112-86-7] and glucosinolates. Linseed (derived from flax seed), peanut, sunflower, safflower, sesame, coconut, and palm kernel meals are other sources of supplemental protein that are by-products of oil extraction (4). [Pg.156]

Vegetable proteins other than that from soy have potential appHcability in food products. Functional characteristics of vegetable protein products are important factors in determining their uses in food products. Concentrates or isolates of proteins from cotton (qv) seed (116), peanuts (117), rape seed (canola) (118,119), sunflower (120), safflower (121), oats (122), lupin (123), okra (124), and com germ (125,126) have been evaluated for functional characteristics, and for utility in protein components of baked products (127), meat products (128), and milk-type beverages (129) (see Dairy substitutes). [Pg.470]

Baits include mixtures of toxicant, usually at l ndash 5%, with a carrier especially attractive to the insect pest. Carriers include sugar for the houseflies, protein hydrolysates for fmit flies, bran for grasshoppers, and honey, chocolate, or peanut butter for ants. [Pg.301]

Defatted peanuts are high in protein, low in moisture, contain only 20% of the naturally occurring fat, and have better stability than whole peanuts. Monosodium glutamate (MSG) has been used as a flavor enhancer for defatted nuts, but the result has not been entirely satisfactory as the addition of MSG produces a meaty rather than nutty flavor. This meaty flavor is more compatible with salted butter and nuts than with candy. [Pg.278]

Arachin, the counterpart of glycinin in peanuts, consists of subunits of 60,000—70,000 mol wt which on reduction with 2-mercaptoethanol yield polypeptides of 41,000—48,000 and 21,000 mol wt (17) analogous to the behavior of glycinin. In addition to the storage proteins, oilseeds contain a variety of minor proteins, including trypsin inhibitors, hemagglutinins, and enzymes. Examples of the last are urease and Hpoxygenase in soybeans. [Pg.293]

The edible oilseed protein industry is comparatively small and is restricted to peanut and soybean proteins. One company manufactures partially defatted peanut flours made by hydraulic pressing. The products contain 40—42% protein. Production estimates for edible soybean proteins in the United States in 1993—1994 (56) and wholesale prices as of November 1995 are given in Table 15. [Pg.300]

Pea.nuts, The proteins of peanuts are low in lysine, threonine, cystine plus methionine, and tryptophan when compared to the amino acid requirements for children but meet the requirements for adults (see Table 3). Peanut flour can be used to increase the nutritive value of cereals such as cornmeal but further improvement is noted by the addition of lysine (71). The trypsin inhibitor content of raw peanuts is about one-fifth that of raw soybeans, but this concentration is sufficient to cause hypertrophy (enlargement) of the pancreas in rats. The inhibitors of peanuts are largely inactivated by moist heat treatment (48). As for cottonseed, peanuts are prone to contamination by aflatoxin. FDA regulations limit aflatoxin levels of peanuts and meals to 100 ppb for breeding beef catde, breeding swine, or poultry 200 ppb for finishing swine 300 ppb for finishing beef catde 20 ppb for immature animals and dairy animals and 20 ppb for humans. [Pg.301]

Edible Protein Ingredients. As of the mid-1990s only peanuts and soybeans are converted iato proteia iagredients for use ia food products. Peanuts are hydraulically pressed to remove about 55% of the oil and the pressed peanuts are then ground iato flours and sold raw or roasted for use ia baked products, snacks, and confections. [Pg.303]

Milk. Imitation milks fall into three broad categories filled products based on skim milk, buttermilk, whey, or combinations of these synthetic milks based on soybean products and toned milk based on the combination of soy or groundnut (peanut) protein with animal milk. Few caseinate-based products have been marketed (1,22,23). Milk is the one area where nutrition is of primary concern, especially in the diets of the young. Substitute milks are being made for human and animal markets. In the latter area, the emphasis is for products to serve as milk replacers for calves. The composition of milk and filled-milk products based on skim milk can be found in Table 10. Table 15 gives the composition of a whey /huttermilk-solids-hased calf-milk replacer, which contains carboxymethyl cellulose (CMC) for proper viscosity of the product. [Pg.447]

Biotin can be synthesized by the human colon flora. The question to which extent this production contributes to covering the host-organism s requirements is, however, subject to discussion. In most foods of animal origin as well as in cereals, biotin prevails in the protein (= enzyme)-bound form as e-N-biotinyl-L-lysine (= biocytin). Brewer s yeast, liver, soya beans, and peanuts number among the biotin rich foods [1]. [Pg.270]

FASPEK KIT for buckwheat Soluble peanut protein mixture... [Pg.155]

Peanut FASTKIT ELISA Ver.II for peanut Peanut soluble protein... [Pg.155]


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See also in sourсe #XX -- [ Pg.231 , Pg.238 , Pg.239 ]




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