Whey foaming properties

Hawks, S.E., Phillips, L.G., Rasmussen, R.R., Barbano, D.M., and KinseUa, J.E., Effects of processing treatment and cheesemaking parameters on foaming properties of whey protein isolates, J. Dairy Sci. 76, 2468, 1993. 

Zhu, H. and Damodaran, S., Effects of calcium and magnesium ions on aggregation of whey protein isolate and its effect on foaming properties, J. Agric. Food Chem., 42, 856, 1994. 

Firebaugh, J.D., and Daubert, C.R. (2005). Emulsifying and foaming properties of a derivatized whey protein ingredient. Int. J. Food Prop. 8,243-253. 

Konrad, G., Kleinsclamidt, T., Rohenkohl, H., and Reimerdes, E.H. (2005). Peptic partial hydrolysis of whey protein concentrate for modifying tire surface properties of whey protein. II. Effects on the emulsifying and foaming properties. Milchwissenschaft 60,195-198. 

Proteins and polysaccharides (PS) are present in many kinds of foods. The main role of proteins in foamed products is to stabilize the air-water interface through their capacity to lower the surface tension of water (Damodaran and Paraf, 1997). p-Lactoglobulin ((3-lg), the most abundant protein in whey, is a globular protein of molecular mass 18.3 kDa being stabilized by two internal disulfide cross-linkings, and exhibits good foaming properties. 

Lim et al. (2008a,b) demonstrated that application of high pressnre (300 MPa, 15 min) conld enhance the foaming properties of WPG, which was added to low-fat ice cream to improve its body and texture. Due to the impact of high pressure on the fnnctional properties of whey proteins, the ice-cream mix containing the pressnre-treated whey protein exhibited increased overrun and foam stability and hardness than ice cream produced with untreated whey protein. 

Phillips, L.G., Young, S.T., Schulman, W. and Kinsella, J.E. (1989) Effect of lysozyme, clupeine and sucrose on the foaming properties of whey protein isolate and p-lactoglobulin. J. Food Sci. 54, 743-747. 

Trade Names Foam Pro Foam Pro L Proleinvit Protelan AG 11 Trade Names Containing Cromoisl WHYA ProtaFlor-W 25 Hydrolyzed whey protein Properties Bitter taste... 

WPI Whey protein isolates. Properties of nonextmded WPI moisture 1.94%, gel strength 52.3 (N), foam volume 288%, and foam stability 28.7%. Value not reported. Means with different letters within a column are significantly (p < 0.05) different. 

A whey protein hydrolysate BioZate , containing ACE-inhibitory peptide was recently developed by Davisco Foods International Inc. The effect on blood pressure was studied with 30 unmedicated, non-smoking, borderline hypertensive men and women, and daily dose was 20 g. The results indicated that there was a significant drop in both systolic and diastolic blood pressure after 1-week treatment, which persisted throughout the study of 6 weeks. The application of this product is varied and flexible. In addition to the bioactive peptides, it has functional properties such as emulsification and foaming (Klink, 2002). 

Although whey protein concentrates possess excellent nutritional and organoleptic properties, they often exhibit only partial solubility and do not function as well as the caseinates for stabilizing aqueous foams and emulsions (19). A number of compositional and processing factors are involved which alter the ability of whey protein concentrates to function in such food formulations. These include pH, redox potential, Ca concentration, heat denaturation, enzymatic modification, residual polyphosphate or other polyvalent ion precipitating agents, residual milk lipids/phospholipids and chemical emulsifiers (22). 

In protein-stabihzed foams, protein flexibility is critical to the molecule functionality in stabilizing interfaces (Hailing 1981 Lemeste et al. 1990). This has important consequences in the development and stability of dairy foams and emulsions, where the heat treatment received by the material can define its foamability and dispersion properties. A symbiotic effect between native and denatured proteins on the emulsifying properties of whey proteins isolate blends has been observed by (Britten et al. 

The casein retentate, when used as cheese milk, can almost be fully depleted of all whey proteins through a sufficient number of diafiltration volume turnovers. In contrast to conventional cheese technology, it is then possible to UHT treat the cheese milk in order to destruct spore formers. The whey proteins can be used as a WPG or WPI product or treated further in order to fractionate the whey proteins in their main components. Alternatively the whey proteins can particulated to form WPP see Section 19.5.1. Both approaches are options to build a platform for novel product matrices with specific properties such as gelling, foaming or emulsification. 

As with other viscous polyanions such as carrageenan, pectin may be protective towards milk casein colloids, enhancing the properties (foam stability, solubility, gelation and emulsification) of whey proteins whilst utilizing them as a source of calcium. 

Interactions between proteins and polysaccharides give rise to various textures in food. Protein-stabilized emulsions can be made more stable by the addition of a polysaccharide. A complex of whey protein isolate and carboxymethylcellulose was found to possess superior emulsifying properties compared to those of the protein alone (Girard et al., 2002). The structure of emulsion interfaces formed by complexes of proteins and carbohydrates can be manipulated by the conditions of the preparation. The sequence of the addition of the biopolymers can alter the interfacial composition of emulsions. The ability to alter interfacial structure of emulsions is a lever which can be used to tailor the delivery of food components and nutrients (Dickinson, 2008). Polysaccharides can be used to control protein adsorption at an air-water interface (Ganzevles et al., 2006). The interface of simultaneously adsorbed films (from mixtures of proteins and polysaccharides) and sequentially adsorbed films (where the protein layer is adsorbed prior to addition of the polysaccharide) are different. The presence of the polysaccharide at the start of the adsorption process hinders the formation of a dense primary interfacial layer (Ganzelves et al., 2008). These observations demonstrate how the order of addition of components can influence interfacial structure. This has implications for foaming and emulsifying applications. 

The conformational changes in /J-lactoglobulin during foaming and thermal denaturation were studied by H NMR and 2H exchange spectroscopy.92-93 The properties of three equine whey proteins, alpha-lactoalbumin, /J-lactoglobulin, and lysozyme, have been studied and compared with those of the corresponding bovine milk.94... 

Xin Yang, E. Allen Foegeding. Effects ofsucrose on egg white protein and whey protein isolate foams Factors determining properties of wet and dry foams (cakes) Food Hydrocolloids, 2010,24,227-238. 

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