John E. Kinsella

Functional properties of soy proteins

Soy protein ingredients must possess appropriate functional properties for food applications and consumer acceptability. these are the intrinsic physicochemical characteristics which affect the behavior of protein in food systems during processing, manufacturing, storage and preparation, e.g., sorption, solubility, gelation, surfactancy, ligand-binding, and film formation. These properties reflect the composition and conformation of the proteins, their interactions with other food components, and they are affected by processing treatments and the environment. Because functional properties are influenced by the composition, structure and conformation of ingredient proteins, systematic elucidation of the physical properties of component protein is expedient for understanding the mechanism of particular functional traints. The composition and properties of the major components of soy proteins are summarized, and the functional properties of soy proteins of importance in current applications (e.g., hydration, gelation, emulsifying, foaming and flavorbinding characteristics) are briefly reviewed.

Functional properties of proteins in foods: A survey

Proteins for foods, in addition to providing nutrition, should also possess specific functional properties that facilitate processing and serve as the basis of product performance. Functional properties of proteins for foods connote the physicochemical properties which govern the behavior of protein in foods. This general article collates the published information concerning the major functional properties of food proteins, e.g., solubility, binding properties, surfactant properties, viscogenic texturizing characteristics, etc. The effects of extraction and processing on functional properties and possible correlations between structure and function are discussed, in relation to practical performance in food systems. Modification of proteins to improve functional characteristics is briefly mentioned.

Proteins in whey: chemical, physical, and functional properties

There is abundant information concerning the functional behavior of whey proteins in model systems. The data on functional properties reported by different researchers, however, reveal wide discrepancies in values. For example, in the case of comparable whey preparations, apparent solubilities may range from 10 to 100%; strength of gels from 0.3 to greater than 10 N, foam overruns from 250 to 1500%, and foam stabilities from 0.5 to 30 min. Many of the data are of limited value in assessing the true functional characteristics of different preparations, treatments, or processing effects. Reports to date are useful in indicating the relative behavior of different proteins; however, the data do not always predict the performance of such proteins in actual food systems. This reflects the fact that in foods, extensive interactions with other components may occur, resulting in modified behavior of the proteins. Harper, (1984) has advocated the testing of these various preparations in simulated food systems which should validly relate the behavior to performance in commercial systems. Emphasis on standardization of specific protocols, with regard to order of addition in ingredients, temperature, pH control, and amount of energy input during mixing, homogenization, emulsification, etc. deserves serious consideration. While this approach is justifiable in terms of providing valuable data to commercial users, it does not minimize the importance of examining these proteins in model systems where the physicochemical basis of each functional attribute can be described in molecular terms (Kinsella, 1987). Such information is necessary to expedite appropriate methods of processing in order to control compositional variability, extent of denatauration, and possible protein modification. In addition, rapid, reliable tests for routine quality assurance that can provide practical information concerning functional applications would be of great value. Whey protein preparations vary immensely in functional behavior and are presently relegated to limited use as functional ingredients in the food industry. This need not be the case since conventional and new technologies permit rigorous control of production protocols, e.g., careful control of heat treatments can result in the production of whey protein preparations with consistent, reliable functional properties (deWit, 1981, 1984; Harper, 1984; Morr, 1985). As the market for functional proteins continues to expand, the whey industry must seek the means to refine whey protein products; determine useful functional properties; develop standardized manufacturing protocols; demonstrate the effectiveness of whey as a functional ingredient; promote, and then market, whey on the basis of performance at competitive cost.

Milk proteins: Physicochemical and functional properties

Because of the growing trend toward widespread use of protein ingredients in food formulation and fabrication, an understanding of the relationships between the physical properties of proteins and their behavior in food systems is desirable. A range of milk-derived protein preparations, i.e., dry milk, milk proteins, caseins, whey proteins, and lactalbumin, are used in a range of food products for their specific functional attributes. In this paper some of the apparent relationships between the properties of the protein components and specific functional properties are discussed. Thus, the roles of milk proteins in determining some important physical characteristics (i.e. color, bulk density, sinkability, dispersibility) of milk powders and their involvement in a range of functional properties (water holding, solubility, rheological behavior, gelation, film formation, emulsification, and foaming) are reviewed. Because of the various methods and conditions used in determining functional properties and the variability in composition of preparations it is difficult to compare data and/or reconcile differences in published information. The desirability of developing standard methods is emphasized.

Initiation of lipid peroxidation in biological systems

The direct oxidation of PUFA by triplet oxygen is spin forbidden. The data reviewed indicate that lipid peroxidation is initiated by nonenzymatic and enzymatic reactions. One of the first steps in the initiation of lipid peroxidation in animal tissues is by the generation of a superoxide radical (see Figure 16), or its protonated molecule, the perhydroxyl radical. The latter could directly initiate PUFA peroxidation. Hydrogen peroxide which is produced by superoxide dismutation or by direct enzymatic production (amine oxidase, glucose oxidase, etc.) has a very crucial role in the initiation of lipid peroxidation. Hydrogen peroxide reduction by reduced transition metal generates hydroxyl radicals which oxidize every biological molecule. Hydrogen peroxide also activates myoglobin, hemoglobin, and other heme proteins to a compound containing iron at a higher oxidation state, Fe(IV) or Fe(V), which initiates lipid peroxidation even on membranes. Complexed iron could also be activated by O2- or by H2O2 to ferryl iron compound, which is supposed to initiate PUFA peroxidation. The presence of hydrogen peroxide, especially hydroperoxides, activates enzymes such as cyclooxygenase and lipoxygenase. These enzymes produce hydroperoxides and other physiological active compounds known as eicosanoids. Lipid peroxidation could also be initiated by other free radicals. The control of superoxide and perhydroxyl radical is done by SOD (a) (see Figure 16). Hydrogen peroxide is controlled in tissues by glutathione-peroxidase, which also affects the level of hydroperoxides (b). Hydrogen peroxide is decomposed also by catalase (b). Caeruloplasmin in extracellular fluids prevents the formation of free reduced iron ions which could decompose hydrogen peroxide to hydroxyl radical (c). Hydroxyl radical attacks on target lipid molecules could be prevented by hydroxyl radical scavengers, such as mannitol, glucose, and formate (d). Reduced compounds and antioxidants (ascorbic acid, alpha-tocopherol, polyphenols, etc.) (e) prevent initiation of lipid peroxidation by activated heme proteins, ferryl ion, and cyclo- and lipoxygenase. In addition, cyclooxygenase is inhibited by aspirin and nonsteroid drugs, such as indomethacin (f). The classical soybean lipoxygenase inhibitors are antioxidants, such as nordihydroguaiaretic acid (NDGA) and others, and the substrate analog 5,8,11,14 eicosatetraynoic acid (ETYA), which also inhibit cyclooxygenase (g). In food, lipoxygenase is inhibited by blanching. Initiation of lipid peroxidation was derived also by free radicals, such as NO2. or CCl3OO. This process could be controlled by antioxidants (e).(ABSTRACT TRUNCATED AT 400 WORDS)

Oxidation of Polyunsaturated Fatty Acids: Mechanisms, Products, and Inhibition with Emphasis on Fish

Publisher Summary This chapter presents the ubiquitous nature and pervasiveness of lipid oxidation ex vivo in foods and in vivo , and demonstrates that oxidation generally has deleterious results in both systems. This dramatizes the need for more effective strategies for controlling lipid oxidation, both in food materials and in tissues in vivo . The chapter discusses the existing practices using antioxidants, chelators, enzyme inactivation, and anoxic and low-temperature storage conditions. The oxidative degradation of the unsaturated fatty acid components of food lipids may be beneficial in some foods in generating low levels of desirable flavorful carbonyl compounds. However, in general, oxidation causes deleterious changes in flavor, taste, color, texture, and possibly safety of foods. The polyunsaturated fatty acids (PUFA)—particularly the trienoic, pentaenoic, and hexaenoic PUFA commonly found in oilseeds and seafoods—render these foods, which are particularly sensitive to oxidative changes which limit their self-life.

Functional properties of proteins: Possible relationships between structure and function in foams

Abstract Proteins via interactions with other components in food systems perform several desirable functions which are related to their structure and physico-chemical properties. In this paper the nature of food foams, the possible relationships between the molecular structure and the foaming capacity of different proteins, and factors affecting these are discussed.

Dietary unsaturated fatty acids: interactions and possible needs in relation to eicosanoid synthesis.

In addition to providing energy and essential fatty acids, dietary fatty acids can affect numerous biochemical and physiologic reactions related to secretory, cardiovascular, and immune functions. The major dietary unsaturated fatty acid, linoleic acid, affects tissue arachidonic acid and can influence eicosanoid-mediated reactions. Chronic, excess, or imbalanced eicosanoid synthesis may be conductive to excessive inflammation, thrombotic tendencies, atherosclerosis, and immune suppression. Dietary n-3 polyunsaturated fatty acids (PUFAs) may ameliorate eicosanoid-related phenomena by reducing tissue arachidonic acid and by inhibiting eicosanoid synthesis. This review summarizes information concerning the metabolism of unsaturated fatty acids, with emphasis on tissue arachidonic acid levels and eicosanoids, and discusses the need for data concerning the appropriate intake of dietary n-6 and n-3 PUFAs to modulate arachidonic acid and eicosanoid synthesis and to minimize possible adverse reactions.

Fatty acid content and composition of freshwater finfish

Abstract and SummaryThe fatty acid content and composition of 18 species of freshwater fish filets were determined. The fat content and composition varied with anatomical location. The anterior ventral regions of trout and salmon contained more lipids than the posterior dorsal sections. Marked variations in fatty acid composition between species were observed. Palmitic (C16:0), palmitoleic (C16:1), oleic (C18:l), eicosapentaenoic (C20:5 ω3), and docosahexaenoic (C22:6 ω3) were the most abundant fatty acids. The fatty acids were tabulated according to the number and positions of the double bonds. Significant quantities of ω6 C18:2 and C20:4 fatty acids were found in several species.

Stearyl CoA as a precursor of oleic acid and glycerolipids in mammary microsomes from lactating bovine: Possible regulatory step in milk triglyceride synthesis

The stearyl desaturase of lactating bovine mammary tissue is located in the microsomes and requires activated fatty acid and NADH for activity. Other enzymes, acyl-transferase(s) and deacylase which apparently compete with the desaturase for substrate are also present. Both the substrate 1-14C-stearyl CoA and the oleic acid produced by desaturase are esterified into the various lipid classes. The oleic acid is preferentially acylated into positionsn-3 of the triglycerides andsn-2 of the phosphatidylcholine. Experimental conditions causing reduced desaturase activity depressed triglyceride synthesis, and stimulation of desaturation by NADH L−α GP, acidic pH, 5.6, was accompanied by increased incorporation of radioactive fatty acids into the triglycerides. These data indicated that desaturase and glyceride acyl transferase were located contiguously within the microsomal membranes. The possibility that desaturase activity might control triglyceride synthesis in vivo is discussed. It was observed that mammary tissue from nonlactating cows 1–2 weeks and 2 days prior to calving lacked or possessed very low stearyl desaturase activity.