Effects protein emulsifiers

The presence of a thermodynamically incompatible polysaccharide in the aqueous phase can enhance the effective protein emulsifying capacity. The greater surface activity of the protein in the mixed biopolymer system facilitates the creation of smaller emulsion droplets, i.e., an increase in total surface area of the freshly prepared emulsion stabilized by the mixture of thermodynamically incompatible biopolymers (see Figure 3.4) (Dickinson and Semenova, 1992 Semenova el al., 1999a Tsapkina et al., 1992 Makri et al., 2005). It should be noted, however, that some hydrocolloids do cause a reduction in the protein emulsifying capacity by reducing the protein adsorption efficiency as a result of viscosity effects. 

The protein ioad increases in the presence of hydrocolloids. In the presence of additional emulsifiers a very effective desorption of protein takes place during whipping and freezing in the ice cream machine. Effective protein desorption is facilitated by the increased viscosity of the mix due to increased surface shear forces, which makes the ice cream continuous freezer work better. 

Both hydrocolloids and emulsifiers increase the water-binding capacity in the mix (increased % of hydrogen atoms with low T2 and decreased T2 values). A synergistic effect is observed when both ingredients are present. From studies described earlier in this chapter, the effect of hydrocolloids is assumed to be due to simple water binding and increased thickness of protein layers around the fat globules, whereas the effect of emulsifiers may be due to the increased hydration of interfacially bound protein as well as increased hydration of polar groups of emulsifier at the oil-water interface. 

Another class of surfactants that are used in cosmetics and personal care products is the phosphoric acid esters. These molecules are similar to the phospholipids that are the building blocks of the stratum corneum (the top layer of the skin, which is the main barrier for water loss). Glycerine esters, in particular, triglycerides, are also frequently used. Macromolecular surfactants of the A-B-A block type [where A is PEO and B is polypropylene oxide (PPO)] are also frequently used in cosmetics. Another important naturally occurring class of polymeric surfactants is the proteins, which can be used effectively as emulsifiers. 

Tornberg and Ediriweera, 1987). Phase inversion temperature (Shinoda and Saito, 1969) and emulsifying capacity (Swift et al., 1961) have been used to evaluate the effects of low molecular weight and protein emulsifiers, respectively. Unfortunately, it is not possible to measure the size of the large droplets present in unhomogenized water-in-oil emulsions because the droplets coalesce very quickly. The phase inversion temperature is not a relevant test, as it may not be related directly to the stability to inversion at the emulsification temperature. Furthermore, it has been stated (Matsumoto and Sherman, 1970) that water-in-oil emulsions do not exhibit a true phase inversion temperature, unlike oil-in-water emulsions. 

Barfod, N.M., Krog, N., Larsen, G., Buchheim, W. 1991. Effects of emulsifiers on protein-fat interaction in ice cream mix during ageing. I Quantitative analyses. Fett.-Wissen.-Technol. 93, 24-35. 

In this section, emulsifier means a material that is on the list of permitted emulsifiers and stabilisers - there are some materials that are extremely effective emulsifiers but which, in fact, do not qualify as emulsifiers in food law. The main examples are the proteins contained in milk they are effective at emulsifying oils and fats but do not qualify for the legal description of emulsifiers. 

The cubic phases can also be dispersed by amphiphilic proteins. Caseins, for example, which also are very effective as emulsifiers, can disperse the cubic phase just as do simple surfactants, such as bile salts. The mechanism is exactly the same as the solubilisation of bilayers by detergents at the cmc - the mixed system has a different surfactant parameter, i.e. local curvature, and the system takes on a different structure. 

Barfod, N.M., N. Krog, G. Larsen, and W. Buchheim, Effect of Emulsifiers on Protein-Fat Interaction in Ice Cream Mix During Aging I. Quantitative Analyses, Fat Sci. Technol. 93 24-29 (1991). 

Mizuno, R., and Lucey, J.A. (2005). Effects of emulsifying salts on the turbidity and calcium phosphate-protein interactions in casein micelles. /. Dairy Sci. 88,3070-3078. 

To analyze the effect of emulsifier concentration and aqueous phase composition on the kinetics of diffusion (fcdifr)/ the evolution of the slope of tt vs. 9 or E vs. 9 is of great utility (Nino et al., 2003). We have observed that fcdiff increases with the emulsifier concentration in the bulk phase according to the Ward and Tordai equation. The presence of sucrose in the aqueous phase increases the diffusion of proteins towards the interface. However, is lower in ethanol aqueous solutions than in water. In addition, decreases with increasing ethanol or at higher sucrose concentrations in the aqueous phase (Nino et al., 2003). 

Spinelli et al. (14) determined the emulsion stability and emulsion capacity of polypeptides recovered from hydrolysates of fish myofibrillar protein using hexametaphosphate. In general the emulsion capacity and emulsion stability increased through 30 min of proteolysis but then declined. Even the unhydrolyzed protein-phosphate complex yielded better emulsion stability and capacity values compared with sodium caseinate. The effect of the residual hexametaphosphate in the hydrolysate conceivably could have a beneficial effect on emulsifying characteristics of the modified fish myofibrillar proteins. 

The emulsifying activity of proteins [143] increased in the pH range of 2-9 [144] upon hydrolysis of soy proteins. Emulsifying capacity was also increased by hydrolysis of soy. Proteolysis of soy protein had no effect on foam stability [144,118], but hydrolysis of zein increased foam stability [145]. 

The final pH of the emulsion will determine to a large extent which proteins will be functionally effective as emulsifiers. Hailing [6] suggested that the effects of pH on the emulsifying behavior of proteins could be explained by one or more of the following determining factors ... 

Williams and Janssen (20) studied the behavior of droplets in a simple shear flow in the presence of a protein emulsifier. The effect of two structurally diverse protein emulsifiers, P-lactoglobulin and P-casein, upon the breakup behavior of a single aqueous droplet in a Couette flow field has been studied over a wide range of protein concentrations. It was found that P-casein and low concentrations of P-lactoglobulin cause the droplets to be at least as stable as expected from conventional theories based on the equilibrium interfacial tension. In such cases the presence of the emulsifier at the deforming interface is thought to enhance the interfacial elasticity. This effect can be characterized by... 

As p-hydroxybenzoic acid esters present a relatively high pKa value (approx. 8.5), their antimicrobial action is less dependent on the pH value of the type of food to be preserved. In this respect they are superior to the organic preservative acids. Unfavourably, as in the case of phenol, p-hydroxybenzoic acid esters may be linked to some extent to proteins, emulsifiers or other food components on account of their phenolic hydroxylic-group and thus be inactivated. The antimicrobial action of the p-hydroxybenzoic acid esters is proportional to the alkyl chain length. Thus the antimicrobial action of the methyl ester is some 3 to 4 times, that of the ethyl ester some 5 to 8 times, that of the propyl ester about 25 times as powerful as phenol (Thompson, 1994). However, superimposed on this effect may be the water solubility of the esters, which is inversely proportional to the alkyl chain length. Since the activity spectra of the individual p-hydroxybenzoic acid esters are different, the application of mixtures can be profitable. 

Table 14. Effect of Protein and Emulsifier on Coffee Whitener Stability ...

Soy proteins are used extensively in meat and meat products by the military, the school lunch program and consumers to save money. Their ultimate acceptability is equally dependent upon the nutritional, chemical, sensory and shelf life changes which occur when they are added. Soy proteins in meat products such as ground beef inhibit rancidity, improve tenderness, increase moisture retention, decrease cooking shrink, fat dispersion during cooking and have no important effect on microbiological condition. Concomittantly, inordinate amounts of added soy protein may cause the meat product to be too soft, exhibit an undesirable flavor and may lead to a decreased PER and a deficiency in B-vitamins and trace minerals. In emulsified meat products, soy protein effectively binds water but does not emulsify fat as well as salt soluble muscle protein. Prudent incorporation of plant proteins can result in an improvement of the quality of the meat product with inconsequential adverse effects. 

The present study was conducted to obtain additional information on changes in soy protein subunits during limited proteolysis. Enzymatic soy protein deamidation that occurred, in addition to limited proteolysis, during germination of soybean seeds was investigated. The effects of proteolysis and deamidation on solubility and emulsifying activity were compared. Phosphorylation of soy protein with a commercially available protein kinase and its effects on subsequent changes in functional properties of the protein were also studied. 

Emulsifying activity index (EAI) is a measure of the ability of protein to emulsify oil, which depends on solubility, size, charge, and surface activity of the protein molecules. The effect of proteolysis with pronase E on EAI of the modified protein was relatively insignificant (Figure 6) However, deamidation appeared to enhance EAI, especially at pH values more basic than the isoelectric point (pH 4.7). 

In limited proteolysis, proteases such as pronase E hydrolyzed the 7S subunits of soy proteins more than the IIS subunits, resulting in enhanced protein solubility. Deamidation with relatively insignificant peptide bond hydrolysis that occurred during the germination of soybeans imparted to the storage protein improved solubility and emulsifying activity. On the other hand, the incorporation of phosphorus in soy proteins by the protein kinase cAMPdPK was too low to effect significant... 

Effective Hamaker constant, 234 Emulsifying activity index, 186,188/ Emulsions, concentrated oil-in-water, effea of interdroplet forces on centrifugal stability, 229-245 Enhancers of taste. See Taste enhancers Enzymatic modification of soy proteins, 181-190... 

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