Protein functional properties, determination

Functional properties determine the overall behavior or performance of proteins in foods during manufacturing, processing, storage, and consumption (1). They reflect those properties of the protein that are influenced by its composition, its conformation, and its interactions with other food components as affected by the immediate environment (Table I). 

Capozzi F, Ciurli S, Luchinat C (1998) Coordination Sphere Versus Protein Environment as Determinants of Electronic and Functional Properties of Iron-Sulfur Proteins 90 127-160... 

Protein kinases differ in their cellular and subcellular distribution, substrate specificity and regulation. These properties determine the functional roles played by the very large number of protein kinases that have been found in mammalian tissues, most of which are known to be expressed in neurons [3]. The major classes of protein serine-threonine kinase in the brain, listed in Table 23-1, are covered in this chapter. The major classes of protein tyrosine kinases in the brain are discussed in Chapter 24. 

In the absence of a correlation between the local dynamics and the overall rotational diffusion of the protein, as assumed in the model-free approach, the total correlation function that determines the 15N spin-relaxation properties (Eqs. (1-5)) can be deconvolved (Tfast, Tslow < Tc) ... 

It is also essential that any functional properties of the mutant protein that can be assessed be assessed. Although the substitution of one particular residue for another may be made in an attempt to determine the effect of the mutation on a specific property of a protein, it is quite possible that other properties that are not of immediate concern may be modified unintentionally and that these modifications may have important, otherwise occult, implications for the functional studies that are of immediate interest (vide infra). In the case of electron transfer proteins it may be useful, for example, to produce a family of mutants the members of which differ from each other only in their reduction potentials. This result may prove to be difficult to achieve because many mutations that perturb the reduction potential of a protein may also change its electrostatic properties or its reorganizational barrier to electron transfer. Depending on the experiments to be conducted with the mutants, these other properties may prove to be more important considerations than the reduction potentials of the mutants. In summary, new mutant proteins are ideally studied as if they were altogether new proteins of the same general class as the wild-type protein, and assumptions regarding the properties of such mutants should be kept to a minimum. 

Proteins are important food components mainly due to their nutritional and functional value. Dietary proteins provide amino acids and nitrogen necessary for organisms. They also play a major role in determining the sensory and textural characteristics of food products. The functional properties are related to their ability to form viscoelastic networks, bind water, entrap flavors, emulsify fat and oil, and form stable foams [105]. 

Nowadays it is well established that the interactions between different macromolecular ingredients (i.e., protein + protein, polysaccharide + polysaccharide, and protein + polysaccharide) are of great importance in determining the texture and shelf-life of multicomponent food colloids. These interactions affect the structure-forming properties of biopolymers in the bulk and at interfaces thermodynamic activity, self-assembly, sin-face loading, thermodynamic compatibility/incompatibility, phase separation, complexation and rheological behaviour. Therefore, one may infer that a knowledge of the key physico-chemical features of such biopolymer-biopolymer interactions, and their impact on stability properties of food colloids, is essential in order to be able to understand and predict the functional properties of mixed biopolymers in product formulations. 

Environment. The physical and chemical environments have been shown to affect the functional performance of proteins. Factors, such as concentration, pH, temperature, ionic strength, and presence of other components, affect the balance between the forces underlying protein-protein and protein-solvent interactions (9). Most functional properties are determined by the balance between these forces. Although the comparison of discrete data from various studies might be of limited value, consideration of the response patterns of protein additives to changes in the environment of simple and/or food systems might be fruitful. 

Considerable effort has been devoted to the improvement of functional properties of fish protein concentrate. Spinelli et al. (44) conducted a study to determine the feasibility of modifying myofibrillar fish proteins by partially hydrolyzing them... 

To develop a model for a particular research experiment to study functional properties of a food protein, the researcher must obviously have some knowledge concerning which factors are potentially important determinants of the level of the functional property to be studied. The researcher must select 1) each of the factors for which there is to be some variation in level within the experiment, 2) the levels to be used for each variable factor, 3) the number of combinations of levels of the different factors to be used, and 4) the level at which each nonvariable, but potentially important, factor is to be set throughout the experiment. 

The a-helix is the most abundant secondary structural element, determining the functional properties of proteins as diverse as a-keratin, hemoglobin and the transcription factor GCN4. The average length of an a-helix in proteins is approximately 17 A, corresponding to 11 amino acid residues or three a-helical turns. In short peptides, the conformational transition from random coil to a-helix is usually entropically disfavored. Nevertheless, several methods are known to induce and stabilize a-helical conformations in short peptides, including ... 

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