Soluble protein isolate

Kinesin a soluble protein isolated from the axoplasm of squid giant axons apparent M, 600,000. In the presence of the non-hydrolysable ATP analog, adenylyl imidodiphosphate, it binds tightly to microtubules, but it is released from them by ATP. K. apparently consists of subunits of M, 110,000, 70,000 and 65,000. Polypeptides from bovine brain with similar binding properties and M, 120,000 and 62,000 have also been isolated. In the presence of ATP, K. causes... 

FIGURE 4.2 Effect of pH on nitrogen solubility index of rapeseed protein isolates. PPI—precipitated protein isolate SPI—soluble protein isolate. (From Xu, L. and Diosady, L. L. 1994. J. Amer. Oil Chem. Soc. 71 935-939. With permission.)... 

Commercial soy protein concentrates typically contain 70 to 72% cmde protein, ie, nitrogen x 6.25, dry wt basis. Soy protein isolates are prepared from desolventhed, defatted flakes. A three-stage aqueous countercurrent extraction at pH 8.5 is used to disperse proteins and dissolve water-soluble constituents. Centrifugation then removes the extracted flakes, and the protein is precipitated from the aqueous phase by acidifying with HCl at pH 4.5. 

SolubiHty is used in the refining of oilseed meals to give protein isolates and concentrates (18). Proteins are highly soluble in basic solutions and the... 

Water soluble protein with a relative molecular mass of ca. 32600, which particularly contains copper and zinc bound like chelate (ca. 4 gram atoms) and has superoxide-dismutase-activity. It is isolated from bovine liver or from hemolyzed, plasma free erythrocytes obtained from bovine blood. Purification by manyfold fractionated precipitation and solvolyse methods and definitive separation of the residual foreign proteins by denaturizing heating of the orgotein concentrate in buffer solution to ca. 65-70 C and gel filtration and/or dialysis. 

Recently, water-soluble protein fractions, isolated from extracts of bone matrix, were incorporated into a collagen matrix and shown to induce bone (67,68) and cartilage formation both in vitro and in vivo (69,70). In the latter studies, in the absence of the collajgen delivery system, the proteins were incapable of inducing cartilage formation in vivo when implanted intramuscularly into mice. The success of this approach appears to depend on delivering the active agents at an effective dose over an extended time period. 

The Water Unextractable Solids were isolated from dehulled, defatted, untoasted soy bean meal (particle size < 0.5 mm) by removal of cold water solubles, proteins and starch. The soy bean meal was extracted with cold water, a solution containing sodium dodecylsulphate and 1,4-dithiothreitol, and incubated with a-amylase, to yield the CWS, SDSS and HWS... 

The yield and the composition of the fractions from soy bean meal obtmned with isolating WUS is shown in Table 1. The removal of cold water solubles, proteins and starch from soy meal was successful. The larger part of the material appeared in CWS, 59.1%. UFF contained mainly oligosaccharides and some water soluble proteins and UFR contained mainly water soluble proteins. The solution of SDSS and DTT extracted the residual proteins from the soy meal and the extract consisted for over 80% of proteins. Since the yield of the HWS fraction is only 0.4%, the composition is not discussed here. The remaining WUS contained 90% of NSP and the yield was 15.7%, which indicates that from the polysaccharides present in soy meal 92% was recovered in the WUS. By isolating WUS a fraction is obtained in which almost all cell wall polysaccharides are recovered and which contained only little other components. 

FIGURE 5.6 Solubility of texturized dairy protein products extruded at different temperatures, 25 (control), 50, 75, and 100 C Nonfat dried milk (NDM) whey protein concentrate (WPC80), containing 80% protein and whey protein isolate (WPl), containing 95% protein (Onwulata et at, 2003a). 

The alkali-soluble protein of the peel of lemons treated with hydrogen sulfide, sulfur dioxide, and sulfuric acid contained radioactive sulfur, but the fruit treated with hydrogen sulfide had a significantly lower per cent specific activity in the alkali-soluble protein fraction than did the sulfur dioxide or sulfuric acid treated fruits (Table VII). These results suggest that sulfur dioxide and sulfuric acid react with protein more directly, while hydrogen sulfide perhaps must be oxidized first, as indicated in Table III. It also appears (from Table VII) that the alkali-soluble protein may have been dismuted as the amounts isolated were less in both the hydrogen sulfide and sulfur dioxide treated fruit than in the incubated or nonincubated controls. Other evidence of dismutation has been obtained in experiments where incubation at 60° C. was accompanied by the production of free ammonia (18), and the recovery of free ammonia and six amino acids in the exudates of incubated and sulfur-dusted fruits (18). 

Figure 2. Relationship between calcium solubility and pH after complete digestion for four soy products. Key solid line, full-fat soy flour long-dashed line, soy protein isolate short-dashed line, soy protein concentrate and dotted line, defatted soy flour...

Water Absorption. Water absorption of pea protein isolates depends on pH and processing method used to produce the isolate. Isoelectric pea protein isolate absorbed 2.7 to 2.8 times its weight of water at pH 7 while UF pea protein isolate absorbed 3.3 times its weight of water at pH 2.5 and twice its weight in water at pH 8.5 (13). These low water absorption values may be due to the high nitrogen solubilities of these proteins (35). 

Isolated Soy Proteins. Isolated soy proteins (90% protein dry basis) are highly dispersible, highly soluble, highly functional soy products (8 9, H > 17, 18) Designed to replace a portion of... 

PMR studies have been performed on a number of other ribosomal proteins isolated by the acetic acid/urea method (Morrison etal., 1977a). The results of these studies have shown that acedc acid/urea-extracted proteins contain little tertiary structure. However, some structure was seen in protein S4 and especially in protein S16 as indicated by the appearance of ring-current shifted resonances in the apolar region of the spectrum (Morrison et al., 1977b). These are due to the interaction of apolar methyl groups with aromatic amino acids in the tertiary structure of the protein. The PMR spectra were recorded either in water or in dilute phosphate buffer at pH 7.0—conditions under which the proteins were soluble. 

Vesicular transport of bile acids has not been demonstrated under normal conditions, shown by using isolated rat hepatocyte couplets and fluorescently labelled bile acids. In these experiments confocal microscopy found no evidence of sequestering into clusters and colchicine disruption of microtubular function did not affect bile-acid transport. This makes it unlikely that vesicle transport plays a role and it is now believed that bile acids traverse the hepatocyte by diffusion through the cytosol while bound to soluble proteins. It is worth considering the caveat that fluorescently labelled bile acids, while very useful tools, do differ structurally from endogenous bile acids with increased hydro-phobicity leading to greater retention by cells. ... 

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