Cottonseed flour protein solubility

The foaming capacity of succinylated soy protein was significantly better than those of the unmodifided proteins. Foam volumes progressively increased with pH from 3 to 10 (12). Succi-nylation caused a small increase in foaming capacity of cottonseed flour (38). Solubility is required for the production of protein foams (48), and succinylation substantially increased the foaming ability of soy isolate by enhancing their solubility. 

Biscuits were prepared from plant-protein flours based on 20Z replacement for wheat flour. In biscuits prepared with fractions isolated from cottonseed flours, the quantities used were calculated using the percentages these fractions represented of the original flour, e.g., the salt solution soluble fraction of LCP flour was 43X of the original flour and 8.6Z, (20 x 0.43) replacement for wheat was used to prepare the biscuit. 

Figure 12. E ect of succinylation on the foam and protein solubility properties of liquid cyclone processed cottonseed flour in suspensions at various pH values...

These data demonstrate that changes in foam properties of liquid cyclone processed cottonseed flour are inducible by treatment with succinic anhydride. Gel electrophoretic and solubility data show that there are alterations in the physical and chemical properties of proteins, and in certain cases these changes improve foam properties, that is, improve solubility and polypeptide dissociation of proteins at the interface of the foaming solution. Similar results have been reported for succinylated soybean and sunflower seed proteins (44. 46). 

Sato et a2- (34) demonstrated that a variety of common meat additives, inclucnrTg cottonseed flour, nonfat dry milk, spray-dried whey, wheat germ, and textured soy flour, inhibited WOF in the meat system. These products may have exerted their inhibitory effect on WOF through the Maillard reaction, since most of them contain some reducing sugars. Pratt (40) reported soybeans and soy protein concentrate had an inhibitory effect upon development of WOF and was able to demonstrate that the active components are water soluble. Fractionation and analysis of the water-soluble fraction showed the antioxidant activity was due to the presence of isoflavones and hydroxylated cinnamic acids (40). This confirms earlier work showing that the flavonoTcis present in plant extracts inhibit oxidation in sliced roast beef (41 ). 

Soluble proteins in various aqueous fractions of glandless cottonseed flour (hexane-defatted) and peanut products (whole peanuts, and full-fat and hexane defatted meal and flour) were determined by methods of Cherry et al (10), and McWatters et... 

Protein concentrates other than FPC have also been treated with proteolytic enzymes to modify their solubilities. Arzu et al. (17) hydrolyzed cottonseed protein from defatted cottonseed flour with nine proteases from animal, plant, or microbial sources. In these studies the enzymes were incubated with the substrate at their optimum pH values for 5 hr at 45°C. At a level of 0.25 g enzyme per 10 g protein, two bacterial proteinases and bromelain were most active. An interesting... 

---