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Properties peanut

Composition or property Peanut Cotton- seed Corn Soybean Linseed... [Pg.613]

Sheppard, J.A. and Rudolf, T.S. (1991) Analysis of peanuts and peanut products for total lipids and fatty acid properties. Peanut Sci. 18, 51-54. [Pg.176]

Other than fuel, the largest volume appHcation for hexane is in extraction of oil from seeds, eg, soybeans, cottonseed, safflower seed, peanuts, rapeseed, etc. Hexane has been found ideal for these appHcations because of its high solvency for oil, low boiling point, and low cost. Its narrow boiling range minimises losses, and its low benzene content minimises toxicity. These same properties also make hexane a desirable solvent and reaction medium in the manufacture of polyolefins, synthetic mbbers, and some pharmaceuticals. The solvent serves as catalyst carrier and, in some systems, assists in molecular weight regulation by precipitation of the polymer as it reaches a certain molecular size. However, most solution polymerization processes are fairly old it is likely that those processes will be replaced by more efficient nonsolvent processes in time. [Pg.406]

Figure 38.19 shows the contour plots of the foaming behaviour, uniformity of air cells and the sweetness of a whipped topping based on peanut milk with varying com syrup and fat concentrations [16]. Clearly, fat is the most important variable determining foam (Fig. 38.19A), whereas com syrap concentration determines sweetness (Fig. 38.19C). It is rather the mle than the exception that more than one sensory attribute are needed to describe the sensory characteristics of a product. An effective way to make a final choice is to overlay the contour plots associated with the response surfaces for the various plots. If one indicates in each contour plot which regions are preferred, then in the overlay a window region of products with acceptable properties is left (see Fig. 38.19D and Sections 24.5 and 26.4). In the... Figure 38.19 shows the contour plots of the foaming behaviour, uniformity of air cells and the sweetness of a whipped topping based on peanut milk with varying com syrup and fat concentrations [16]. Clearly, fat is the most important variable determining foam (Fig. 38.19A), whereas com syrap concentration determines sweetness (Fig. 38.19C). It is rather the mle than the exception that more than one sensory attribute are needed to describe the sensory characteristics of a product. An effective way to make a final choice is to overlay the contour plots associated with the response surfaces for the various plots. If one indicates in each contour plot which regions are preferred, then in the overlay a window region of products with acceptable properties is left (see Fig. 38.19D and Sections 24.5 and 26.4). In the...
What properties of foamed polystyrene make it amenable for the manufacture of packing peanuts ... [Pg.341]

Peanut Protein Isolation, Composition, and Properties Jett C. Arthur, Jr. [Pg.389]

Other Protein Components. Other protein components In complex food systems and In protein Ingredient preparations may Interfere with or modify gelation reactions. Protein Interaction between whey protein and casein upon heating has a profound Influence on the characteristics of the casein gel structure In cheesemaking. Similarly protein Interactions are Important to meat structures. Protein-protein Interaction between soy and meat proteins has also been demonstrated with heat treatment (28). While concrete Interaction data have not been collected on protein gels formed from protein combinations, gelation properties of whey proteln/peanut flour blends have been Investigated GU) ... [Pg.138]

Multiple regression analysis is a useful statistical tool for the prediction of the effect of pH, suspension percentage, and composition of soluble and insoluble fractions of oilseed vegetable protein products on foam properties. Similar studies were completed with emulsion properties of cottonseed and peanut seed protein products (23, 24, 29, 30, 31). As observed with the emulsion statistical studies, these regression equations are not optimal, and predicted values outside the range of the experimental data should be used only with caution. Extension of these studies to include nonlinear (curvilinear) multiple regression equations have proven useful in studies on the functionality of peanut seed products (33). [Pg.163]

Figure 8. Effect of pH and salt concentration on the foam and protein solubility properties of peanut meal suspensions (25)... Figure 8. Effect of pH and salt concentration on the foam and protein solubility properties of peanut meal suspensions (25)...
Foam properties related to heat. Peanut kernels were moist heated in a temperature-controlled retort at 50, 75, and lOQOC for 15-min intervals ranging from 15 to 90 min (30). Quantities of water-extractable proteins decreased as heating time increased from 15 to 90 min at all three temperatures (Figure... [Pg.165]

Figure 9. Gel electrophoretic properties of peanut meal proteins that are soluble in suspensions that contain various levels of salt and are at different pH values (25)... Figure 9. Gel electrophoretic properties of peanut meal proteins that are soluble in suspensions that contain various levels of salt and are at different pH values (25)...
Figure 14. Foam capacity and protein solubility properties of defatted soybean, peanut, field pea, and pecan seed flour suspensions at various pH values (4T)... Figure 14. Foam capacity and protein solubility properties of defatted soybean, peanut, field pea, and pecan seed flour suspensions at various pH values (4T)...
Wang and Kinsella (19) studied the fat absorption, and other properties of alfalfa leaf protein (ALP) concentrate and used the soy protein concentrate and isolate Promosoy-lOO and Promine-D,respectively, as the references. The fat absorption values are reported in ml oil/g sample. Converting these to percent fat absorbed (based on the specific gravity of peanut oil) results in values that are higher than those reported by Lin et al. (17) this was most evident in the case of the isolate. [Pg.193]

Peanut Seed. Ramanatham et al. (21) studied the influence of such variables as protein concentration, particle size, speed of mixing, pH, and presence of sodium chloride on emulsification properties of peanut flour (50% protein) and peanut protein isolate (90% protein). Emulsions were prepared by the blender... [Pg.220]

Attention has been directed toward modifying functional properties of peanut proteins by chemical, enzymatic, and physical approaches. Chemical modification has included acetylation and succinylation treatments (28, 29). Marked improvement in emulsion capacity occurred as a result of this treatment if the proteins were extracted in acid 28). Beuchat et al. [Pg.221]

Exposure of proteins to heat has been shown to adversely affect peptization properties (22). The critical denaturation temperature for peanut protein in meal is above 118OC (dry heat) and above 80OC at 100% relative humidity. Although heat treatments routinely employed in a majority of peanut oil mills are insufficiently controlled to prevent denaturation of meal protein, the authors suggest that temperature and moisture control during processing can be maintained at levels sufficient to achieve oil extraction without drastic denaturation of protein. [Pg.283]

A concentration of 0.03M Ca2+ has been prescribed as a minimum in the formulation of imitation milk. Evidence from the study reported by Beuchat et al. (24) suggests that enzymatic hydrolysis of peanut flour modifies protein to the extent that it is highly soluble in 0.03M Ca2+ at a pH range normally associated with fluid milk. Further studies are required to assess the effect of enzyme-induced proteolysis on organoleptic properties of hydrolyzed peanut protein solutions. [Pg.284]

Sekul et al. (29) studied the nitrogen solubility properties of enzyme-hydrolyzed peanut proteins. A deionized water dispersion of peanut flour (1 10, w/v) was treated with papain (0.5% total volume) at 45OC for 15 min. Solubility was tested over a range of pH 1 to 9. In general, papain treatment improved solubility at all levels examined except pH 2 and 8 (Figure 6). [Pg.284]

The effects of fungal fermentation on the moisture adsorption and retention properties of defatted peanut flour have been reported (28). At 8 and 21OC, little difference was noted between the moisture contents of freeze-dried ferments and untreated samples equilibrated at relative humidities ranging from 14 to 75%. However, marked changes were noted above 75% equilibrium relative humidity (ERH), where the control samples did not adsorb as much moisture as did the ferments. These differences were attributed to an increased ratio of exposed hydrophilic to hydrophobic groups resulting from fermentation. [Pg.291]

Beuchat (60) investigated the performance of enzyme-hydrolyzed defatted peanut flour in a cookie formula. Flour slurries were treated with pepsin at pH 2.0, bromelain at pH 4.5, and trypsin at pH 7.6. After readjustment to pH 6.9, materials were freeze-dried, pulverized (60-mesh), and then substituted for wheat flour at 5, 15, and 25%. Adjustment of peanut flour to pH 2.0, as well as treatment with pepsin at this pH, greatly improved the handling characteristics of dough in which these flours were incorporated. Use of peanut flours treated at pH 4.5, with or without bromelain, and at pH 7.6, with or without trypsin, improved handling properties of cookie dough. These doughs did not tend to crumble... [Pg.293]

McWatters and Holmes ( ) developed multiple regression models of the effects of pH and salt concentration on functional properties of soy flour. Design of the experiment and selection of the factors to be Included were based. In part, on earlier findings that emulsion capacity of defatted peanut meal was Inhibited around the Isoelectric point (ca pH 4.0)... [Pg.305]


See other pages where Properties peanut is mentioned: [Pg.470]    [Pg.276]    [Pg.300]    [Pg.54]    [Pg.23]    [Pg.340]    [Pg.262]    [Pg.203]    [Pg.329]    [Pg.155]    [Pg.179]    [Pg.106]    [Pg.15]    [Pg.3]    [Pg.147]    [Pg.402]    [Pg.151]    [Pg.234]    [Pg.280]    [Pg.103]    [Pg.54]    [Pg.165]    [Pg.221]    [Pg.221]    [Pg.223]    [Pg.237]   
See also in sourсe #XX -- [ Pg.40 , Pg.231 , Pg.238 , Pg.239 ]




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