Effect of natural pigments on the oxidative stability of sausages stored under refrigeration.

The objective was to use natural pigments to replace sodium erythorbate (NaEry), a synthetic compound used as an antioxidant in sausage formulations, and to evaluate the oxidative stability of the samples. Six assays were prepared in which sodium erythorbate (ERY) at 0.05 g/100 g was substituted by norbixin (NOR), lycopene (LYC), zeaxanthin (ZEA), beta-carotene (CAR) or dextrose (used as a control (CON)). Physical, chemical, color, texture and sensory parameters were measured on the first day and after 45 days of storage at 4 degrees C. All pigments used in the sausage formulations were able to maintain the oxidative stability of the sausages (MDA equivalents <0.38 mg/kg). Zeaxanthin and norbixin were the most efficient antioxidants of those tested. This antioxidant effect might be associated with the intermediate polarities of these two compounds, which would allow them to concentrate in the membrane lipids or emulsion interface, where lipid oxidation is most prevalent. Other volatile secondary products of oxidation besides MDA should be evaluated in further studies involving natural pigments and sensory oxidative stability.

Suitability of saturated aldehydes as lipid oxidation markers in washed turkey meat.

The aim of this study was to evaluate the suitability of saturated aldehydes as lipid oxidation markers in washed turkey muscle, by means of headspace solid phase microextraction-gas chromatography (HS-SPME-GC); the results were compared with the widely used thiobarbituric acid-reactive substances (TBARs) method. Changes in TBARs, propanal and hexanal concentrations were determined over time in a model system consisting of turkey muscle washed with a sodium phosphate buffer (pH 5.6). To stop oxidation from occurring during analysis, an antioxidant mixture (EDTA, trolox and propyl gallate) was added immediately before analyses. After antioxidant addition, propanal and TBARs concentrations did not increase during 8h of further storage, while an unexpected decrease in hexanal was observed. To determine if aldehydes were interacting with washed turkey muscle, hexanal and propanal were added to either phosphate buffer or washed muscle and concentrations were monitored for 24h. Neither propanal nor hexanal decreased in the phosphate buffer over time, but the headspace concentration of propanal and hexanal in washed turkey muscle were markedly lower (76% and 96%, respectively) at time zero and continued to decreased up to 24h of storage. Because of this decrease in headspace aldehyde concentrations, TBARs were found to be a more sensitive and accurate marker of oxidative deterioration in washed turkey muscle.

Chemical and physical stability of protein and gum arabic-stabilized oil-in-water emulsions containing limonene.

An important flavor component of citrus oils is limonene. Since limonene is lipid soluble, it is often added to foods as an oil-in-water emulsion. However, limonene-containing oil-in-water emulsions are susceptible to both physical instability and oxidative degradation, leading to loss of aroma and formation of off-flavors. Proteins have been found to produce both oxidatively and physically stable emulsions containing triacylglycerols. The objective of this research was to determine if whey protein isolate (WPI) could protect limonene in oil-in-water emulsion droplets more effectively than gum arabic (GA). Limonene degradation and formation of the limonene oxidation products, limonene oxide and carvone, were less in the WPI- than GA-stabilized emulsions at both pHs 3.0 and 7.0. These data suggest that WPI was able to inhibit the oxidative deterioration of limonene in oil-in-water emulsions. The ability of WPI to decrease oxidative reactions could be due to the formation of a cationic emulsion droplet interface at pH 3.0, which can repel prooxidative metals, and/or the ability of amino acids in WPI to scavenge free radical and chelate prooxidative metals.

Emulsion-based delivery systems for lipophilic bioactive components.

There is a pressing need for edible delivery systems to encapsulate, protect, and release bioactive lipids within the food, medical, and pharmaceutical industries. The fact that these delivery systems must be edible puts constraints on the type of ingredients and processing operations that can be used to create them. Emulsion technology is particularly suited for the design and fabrication of delivery systems for encapsulating bioactive lipids. This review provides a brief overview of the major bioactive lipids that need to be delivered within the food industry (for example, omega-3 fatty acids, carotenoids, and phytosterols), highlighting the main challenges to their current incorporation into foods. We then provide an overview of a number of emulsion-based technologies that could be used as edible delivery systems by the food and other industries, including conventional emulsions, multiple emulsions, multilayer emulsions, solid lipid particles, and filled hydrogel particles. Each of these delivery systems could be produced from food-grade (GRAS) ingredients (for example, lipids, proteins, polysaccharides, surfactants, and minerals) using simple processing operations (for example, mixing, homogenizing, and thermal processing). For each type of delivery system, we describe its structure, preparation, advantages, limitations, and potential applications. This knowledge can be used to facilitate the selection of the most appropriate emulsion-based delivery system for specific applications.

Improvement of stability of oil-in-water emulsions containing caseinate-coated droplets by addition of sodium alginate.

The potential of sodium alginate for improving the stability of emulsions containing caseinate-coated droplets was investigated. One wt% corn oil-in-water emulsions containing anionic caseinate-coated droplets (0.15 wt% sodium caseinate) and anionic sodium alginate (0 to 1 wt%) were prepared at pH 7. The pH of these emulsions was then adjusted to 3.5, so that the anionic alginate molecules adsorbed to the cationic caseinate-coated droplets. Extensive droplet aggregation occurred when there was insufficient alginate to completely saturate the droplet surfaces due to bridging flocculation, and when the nonadsorbed alginate concentration was high enough to induce depletion flocculation. Emulsions with relatively small particle sizes could be formed over a range of alginate concentrations (0.1 to 0.4 wt%). The influence of pHs (3 to 7) and sodium chloride (0 to 500 mM) on the properties of primary (0 wt% alginate) and secondary (0.15 wt% alginate) emulsions was studied. Alginate adsorbed to the droplet surfaces at pHs 3, 4, and 5, but not at pHs 6 and 7, due to electrostatic attraction between anionic groups on the alginate and cationic groups on the adsorbed caseinate. Secondary emulsions had better stability than primary emulsions at pH values near caseinate's isoelectric point (pHs 4 and 5). In addition, secondary emulsions were stable up to higher ionic strengths (< 300 mM) than primary emulsions (<50 mM). The controlled electrostatic deposition method utilized in this study could be used to extend the range of application of dairy protein emulsifiers in the food industry.

Effect of antioxidants on stabilization of meat products fortified with n-3 fatty acids.

The effects of an n-3 oil emulsion, with and without added antioxidants, on lipid oxidation in n-3 polyunsaturated fatty acid (PUFA)-fortified meat products were studied. An emulsion of n-3 PUFAs was prepared (25% algal oil, 2.5% whey protein isolates, 10mM sodium citrate, 0.2% potassium sorbate, 500ppm of 70% mixed tocopherols, 100µM EDTA, pH 3, pasteurized at 75°C for 30min) and incorporated into fresh ground turkey, and fresh pork sausage (20% fat) to achieve a concentration of 500mg n-3 PUFA/110g meat. An antioxidant combination containing rosemary (0.2% w/w; radical quencher), citrate (0.5% w/w; sequestrant) and erythorbate (1g/kg product; reductant) was prepared and incorporated into ground turkey patties (5cm dia, 1.5cm thick) or fresh pork sausages (5cm dia, 1.5cm thick). Meat products were stored at 4°C or -18°C and analyzed for color (L*, a*, b* values), lipid oxidation (TBARS and lipid hydroperoxides) and n-3 PUFA profile. a* Values of refrigerated ground turkey patties decreased with storage, and an antioxidant combination effect was observed after 4 days (P<0.05). For fresh pork sausages at 4°C, control+antioxidant (CON+ANTI), and n-3+antioxidant (n-3+ANTI) groups showed greater a* values than controls (CON) indicating that the antioxidant combination stabilized meat color. TBARS and lipid hydroperoxides of both n-3 PUFA-enhanced meat products increased with storage (P<0.05); there were no significant changes in TBARS or lipid hydroperoxides for treatments containing the antioxidant combination (P<0.05). The actual level of n-3 PUFA incorporation in both meat products was greater than 87%; n-3 PUFA concentrations did not change within any treatment during storage (P>0.05). These results provide support for including antioxidant protection in n-3 PUFA fortified meat products.

The effects of antioxidant combinations on color and lipid oxidation in n-3 oil fortified ground beef patties.

This study was carried out to determine an effective combination of chelators, reductants and free radical scavengers for enhancing color stability and minimizing lipid oxidation in muscle foods fortified with n-3 fatty acids. Chelators (sodium tripolyphosphate, STPP; sodium citrate, CIT), reductants (sodium erythorbate, ERY) and radical scavengers (butylhydroxyanisole, BHA; mixed tocopherols from two different sources, 30 or 95TOC; rosemary extract, ROSE) were incorporated in various combinations into ground beef (15% fat) with or without n-3 oil fortification (n=8). Individually, STPP and CIT had no significant effect on a* values except day 4, but showed higher a* values when combined with ERY (STPP+ERY and CIT+ERY) (P<0.05). CIT had lower hue angle values than STPP on days 4 and 6, but CIT+ERY showed more discoloration than STPP+ERY (P<0.05). CIT+ERY showed less lipid oxidation than CIT alone (P<0.05), whereas there was no difference between STPP and STPP+ERY. CIT+ERY+ROSE demonstrated higher a* values than CIT+ERY+95TOC on days 4 and 6 (P<0.05); there was no difference between ROSE and 95TOC groups when n-3 oil was incorporated into ground beef patties (P>0.05). The combination of ROSE and ERY appeared to be effective in slowing the decline of a* values. All antioxidant combinations were effective at delaying lipid oxidation when compared to CON or n-3. A combination of CIT, ERY and ROSE was most effective for stabilizing color and delaying lipid oxidation.

Influence of protein concentration and order of addition on thermal stability of beta-lactoglobulin stabilized n-hexadecane oil-in-water emulsions at neutral pH.

The influence of protein concentration and order of addition relative to homogenization (before or after) on the extent of droplet flocculation in heat-treated oil-in-water emulsions stabilized by a globular protein were examined using laser diffraction. n-Hexadecane (10 wt%) oil-in-water emulsions (pH 7, 150 mM NaCl) stabilized by beta-lactoglobulin (beta-Lg) were prepared by three methods: (1) 4 mg/mL beta-Lg added before homogenization; (2) 4 mg/mL beta-Lg added before homogenization and 6 mg/mL beta-Lg added after homogenization; (3) 10 mg/mL beta-Lg added before homogenization. The emulsions were then subjected to various isothermal heat treatments (30-95 degrees C for 20 min), with the 150 mM NaCl being added either before or after heating. Emulsion 1 contained little nonadsorbed protein and exhibited extensive droplet aggregation at all temperatures, which was attributed to the fact that the droplets had a high surface hydrophobicity, e.g., due to exposed oil or extensive protein surface denaturation. Emulsions 2 and 3 contained a significant fraction of nonadsorbed beta-Lg. When the NaCl was added before heating, these emulsions were relatively stable to droplet flocculation below a critical holding temperature (75 and 60 degrees C, respectively) but showed extensive flocculation above this temperature. The stability at low temperatures was attributed to the droplets having a relatively low surface hydrophobicity, e.g., due to complete saturation of the droplet surface with protein or due to more limited surface denaturation. The instability at high temperatures was attributed to thermal denaturation of the adsorbed and nonadsorbed proteins leading to increased hydrophobic interactions between droplets. When the salt was added to Emulsions 2 and 3 after heating, little droplet flocculation was observed at high temperatures, which was attributed to the dominance of intra-membrane over inter-membrane protein-protein interactions. Our data suggests that protein concentration and order of addition have a strong influence on the flocculation stability of protein-stabilized emulsions, which has important implications for the formulation and production of many emulsion-based products.

Influence of free protein on flocculation stability of beta-lactoglobulin stabilized oil-in-water emulsions at neutral pH and ambient temperature.

The influence of protein concentration and order of addition relative to homogenization (before or after) on the extent of droplet flocculation in oil-in-water emulsions stabilized by a globular protein was examined using laser diffraction. n-Hexadecane (10 wt%) oil-in-water emulsions (pH 7, 150 mM NaCl) stabilized by beta-lactoglobulin (beta-Lg) were prepared by three methods: (1) 4 mg/mL beta-Lg added before homogenization; (2)10 mg/mL beta-Lg added before homogenization; (3) 4 mg/mL beta-Lg added before homogenization and 6 mg/mL beta-Lg added after homogenization. Emulsion 1 contained little nonadsorbed protein (<3%) and underwent extremely rapid and extensive droplet flocculation immediately after homogenization. Emulsion 2 contained a significant fraction of nonadsorbed beta-Lg and exhibited relatively slow droplet flocculation for some hours after homogenization. Measurements on Emulsion 3 showed that the extremely rapid particle growth observed in Emulsion 1 could be arrested by adding native beta-Lg immediately after homogenization. The extent of particle growth in the three types of emulsions was highly dependent on the time that the salt was added to the emulsions, i.e., after 0 or 24 h aging. We postulate that the observed differences are due to changes in droplet surface hydrophobicity caused by differences in the packing or conformation of adsorbed proteins. Our data suggest that history effects have a strong influence on the flocculation stability of protein-stabilized emulsions, which has important implications for the formulation and production of protein stabilized oil-in-water emulsions.

Comparison of droplet flocculation in hexadecane oil-in-water emulsions stabilized by beta-lactoglobulin at pH 3 and 7.

The influence of surface and thermal denaturation of adsorbed beta-lactoglobulin (beta-Lg) on the flocculation of hydrocarbon oil droplets was measured at pH 3 and compared with that at pH 7. Oil-in-water emulsions (5 wt % n-hexadecane, 0.5 wt % beta-Lg, pH 3.0) were prepared that contained different levels of salt (0-150 mM NaCl) added immediately after homogenization. The mean particle diameter (d43) and particle size distribution of diluted emulsions were measured by laser diffraction when they were either (i) stored at 30 degrees C for 48 h or (ii) subjected to different thermal treatments (30-95 degrees C for 20 min). In the absence of salt, little droplet flocculation was observed at pH 3 or 7 because of the strong electrostatic repulsion between the droplets. In the presence of 150 mM NaCl, a progressive increase in mean particle size with time was observed in pH 7 emulsions during storage at 30 degrees C, but no significant change in mean particle diameter with time (d43 approximately 1.4 +/- 0.2 microm) was observed in the pH 3 emulsions. Droplet aggregation became more extensive in pH 7 emulsions containing salt (added before thermal processing) when they were heated above 70 degrees C, which was attributed to thermal denaturation of adsorbed beta-Lg leading to interdroplet disulfide bond formation. In contrast, the mean particle size decreased and the creaming stability improved when pH 3 emulsions were heated above 70 degrees C. These results suggest that the droplets in the pH 3 emulsions were weakly flocculated at temperatures below the thermal denaturation temperature of beta-Lg (T < 70 degrees C) but that flocs did not form so readily above this temperature, which was attributed to a reduction in droplet surface hydrophobicity due to protein conformational changes. The most likely explanation for the difference in behavior of the emulsions is that disulfide bond formation occurs much more readily at pH 7 than at pH 3.

Impact of protein surface denaturation on droplet flocculation in hexadecane oil-in-water emulsions stabilized by beta-lactoglobulin.

The influence of globular protein denaturation after adsorption to the surface of hydrocarbon droplets on flocculation in oil-in-water emulsions was examined. n-Hexadecane oil-in-water emulsions (pH 7.0) stabilized by beta-lactoglobulin (1-wt % beta-Lg) were prepared by high-pressure valve homogenization. NaCl (0-150 mM) was added to these emulsions immediately after homogenization, and the evolution of the mean particle diameter (d) and particle size distribution (PSD) was measured by laser diffraction during storage at 30 degrees C for 48 h. No change in d or PSD was observed in the absence of added salt, which indicated that these emulsions were stable to flocculation. When 150 mM NaCl was added to emulsions immediately after homogenization, d increased rapidly during the following few hours until it reached a plateau value, while the PSD changed from monomodal to bimodal. Addition of N-ethylmaleimide, a sulfhydryl blocking agent, to the emulsions immediately after homogenization prevented (at 20 mM NaCl) or appreciably retarded (at 150 mM NaCl) droplet flocculation. These data suggests that protein unfolding occurred at the droplet interface, which increased the hydrophobic attraction and disulfide bond formation between droplets. In the absence of added salt, the electrostatic repulsion between droplets was sufficient to prevent flocculation, but in the presence of sufficient salt, the attractive interactions dominated, and flocculation occurred.

Impact of tween 20 hydroperoxides and iron on the oxidation of methyl linoleate and salmon oil dispersions.

To determine the role of surfactant hydroperoxides on the oxidative stability of fatty acids, the oxidation of methyl linoleate micelles and salmon oil-in-water emulsions was measured as a function of varying Tween 20 hydroperoxide concentrations. Increasing Tween 20 hydroperoxide concentrations from 3.5 to 14.7 micromol hydroperoxide/g Tween 20 decreased the lag phase of headspace hexanal formation but did not increase the total amount of hexanal formed in methyl linoleate/Tween 20 micelles. In the micelle system, Fe(2+) decreased the lag phase of hexanal formation but increased total hexanal concentrations only in micelles with the highest Tween 20 hydroperoxide concentrations (14.7 micromol hydroperoxide/g surfactant). Increasing Tween 20 surfactant hydroperoxide concentrations also increased the oxidation of salmon oil-in-water emulsions as determined by lipid hydroperoxides and headspace propanal. In both the micelle and emulsion systems, the prooxidant effect of Fe(2+) decreased with increasing Tween 20 hydroperoxide concentrations. These data show that surfactant hydroperoxides such as those in Tween 20 could decrease the oxidative stability of lipids in food emulsions.

Comparison of low-density lipoprotein modification by myeloperoxidase-derived hypochlorous and hypobromous acids.

Myeloperoxidase (MPO), a heme enzyme secreted by activated phagocytes, catalyzes the oxidation of halides to hypohalous acids. At plasma concentrations of halides, hypochlorous acid (HOCl) is the major strong oxidant produced. In contrast, the related enzyme eosinophil peroxidase preferentially generates hypobromous acid (HOBr). Since reagent and MPO-derived HOCl converts low-density lipoprotein (LDL) to a potentially atherogenic form, we investigated the effects of HOBr on LDL modification. Compared to HOCl, HOBr caused 2-3-fold greater oxidation of tryptophan and cysteine residues of the protein moiety (apoB) of LDL and 4-fold greater formation of fatty acid halohydrins from the lipids in LDL. In contrast, HOBr was 2-fold less reactive than HOCl with lysine residues and caused little formation of N-bromamines. Nevertheless, HOBr caused an equivalent increase in the relative electrophoretic mobility of LDL as HOCl, which was not reversed upon subsequent incubation with ascorbate, in contrast to the shift in mobility caused by HOCl. Similar apoB modifications were observed with HOBr generated by MPO/H(2)O(2)/Br(-). In the presence of equivalent concentrations of Cl(-) and Br(-), modifications of LDL by MPO resembled those seen in the presence of Br(-) alone. Interestingly, even at physiological concentrations of the two halides (100 mM Cl(-), 100 microM Br(-)), MPO utilized a portion of the Br(-) to oxidize apoB cysteine residues. MPO also utilized the pseudohalide thiocyanate to oxidize apoB cysteine residues. Our data show that even though HOBr has different reactivities than HOCl with apoB, it is able to alter the charge of LDL, converting it into a potentially atherogenic particle.

Peroxynitrite-induced oxidation of lipids: implications for muscle foods.

Peroxynitrite (ONOO(-)), formed from the nearly diffusion limited reaction between nitric oxide and superoxide, could be an important prooxidant in muscle foods. The objective of this study was to determine whether peroxynitrite caused oxidation of pyrogallol red, liposomes, muscle microsomes, and skeletal muscle homogenate. Oxidation of pyrogallol red, liposomes, and microsomes initiated by peroxynitrite continuously produced by 3-morpholinosydnonimine (SIN-1, 2 mM) was time-dependent and enhanced by CO(2) (1 mM). Reagent peroxynitrite (2 mM) caused concentration-dependent oxidation of pyrogallol red, liposomes, and muscle microsomes that was very rapid with no change after 5 min. Peroxynitrite-induced oxidation was suppressed by CO(2) and low pH. Skeletal muscle homogenate oxidized by reagent peroxynitrite (0.5 mM) exhibited gradual oxidation with time and was suppressed by CO(2), low pH, and metal chelators. These data suggest that peroxynitrite could be an important prooxidant in muscle foods.

Inhibition of low-density lipoprotein oxidation by carnosine histidine.

Carnosine is a beta-alanylhistidine dipeptide found in skeletal muscle and nervous tissue that has been reported to possess antioxidant activity. Carnosine is a potential dietary antioxidant because it is absorbed into plasma intact. This research investigated the ability of carnosine to inhibit the oxidation of low-density lipoprotein (LDL) in comparison to its constituent amino acid, histidine. Carnosine (3 microM) inhibited Cu2+-promoted LDL (20 of protein/mL) oxidation at carnosine/copper ratios as low as 1:1, as determined by loss of tryptophan fluorescence and formation of conjugated dienes. Carnosine (6 microM) lost its ability to inhibit conjugated diene formation and tryptophan oxidation after 2 and 4 h of incubation, respectively, of LDL with 3 microM Cu2+. Compared to controls, histidine (3 microM) inhibited tryptophan oxidation and conjugated diene formation 36 and 58%, respectively, compared to 21 and 0% for carnosine (3 microM) after 3 h of oxidation. Histidine was more effective at inhibiting copper-promoted formation of carbonyls on bovine serum albumin than carnosine, but carnosine was more effective at inhibiting copper-induced ascorbic acid oxidation than histidine. Neither carnosine nor histidine was a strong inhibitor of 2,2'-azobis(2-amidinopropane) dihydrochloride-promoted oxidation of LDL, indicating that their main antioxidant mechanism is through copper chelation.

The effect of diet on vitamin E intake and oxidative stress in response to acute exercise in female athletes.

Vitamin E is the major lipid-soluble antioxidant found in foods, and its bioavailability is affected by the presence of dietary fats. Athletes often consume lowfat diets and may be more susceptible to the oxidative stress produced by exercise due to the low availability of vitamin E. In this study, the effects of a low-fat diet on vitamin E intake and oxidative stress markers were assessed in collegiate female rowers. All subjects habitually consumed either a low-fat (LF; <40 g fat x day(-1)) or a high-fat (HF; >60 g fat x day(-1) diet. Subjects ran downhill for 45 min at 75% of their age-predicted maximal heart rate. Blood samples were collected immediately pre- and post-exercise, and at 6, 24, and 48 h post-exercise. Subjects in the LF group consumed significantly less vitamin E (2.9 mg vitamin E x day(-1)) than advised by the Recommended Dietary Allowance (RDA; 8.0 mg vitamin E x day(-1)) and than those in the HF group (9.8 mg vitamin E x day(-1); P<0.05). Plasma concentrations of vitamin E, malondialdehyde, and conjugated dienes were not significantly different between LF and HF before or after exercise. Creatine kinase became significantly elevated above baseline at 6 h and 24 h post-exercise in both groups (P<0.05). We can conclude from these data that although the subjects in the LF group were not consuming the recommended amount of vitamin E in their diets, their vitamin E intake appears to be sufficient to protect against the oxidative stress produced by this moderate-intensity exercise.

Impact of dietary conjugated linoleic acid on the oxidative stability of rat liver microsomes and skeletal muscle homogenates.

Dietary conjugated linoleic acid (CLA; 0-2.0%) increased CLA concentrations in liver microsomes and skeletal muscle homogenates from rats. Dietary CLA decreased oleic and arachadonic acid concentrations in both liver microsomes and skeletal muscle. The presence of CLA in liver microsomes had no impact on linoleic acid, arachadonic acid, and alpha-tocopherol oxidation rates. Dietary CLA (2.0%) also did not alter alpha-tocopherol oxidation rates in liver microsomes or muscle homogenates. Formation of malonaldehyde (MDA) in oxidizing liver microsomes decreased with increasing CLA concentration as determined by measurement of thiobarbituric acid-MDA complexes by HPLC. The ability of CLA to decrease MDA formation without impacting other lipid oxidation markers such as the disappearance of fatty acid and alpha-tocopherol suggests that decreased MDA concentration was the result of CLA's ability to lower polyenoic fatty acids such as arachadonic acid. While CLA does not appear to act as an antioxidant, its ability to decrease polyenoic fatty acid concentrations could decrease the formation of highly cytotoxic lipid oxidation products such as MDA.

A re-evaluation of the antioxidant activity of purified carnosine.

The antioxidant activity of carnosine has been re-evaluated due to the presence of contaminating hydrazine in commercial carnosine preparations. Purified carnosine is capable of scavenging peroxyl radicals. Inhibition of the oxidation of phosphatidylcholine liposomes by purified carnosine is greater in the presence of copper than iron, a phenomenon likely to be due to the copper chelating properties of carnosine. Purified carnosine is capable of forming adducts with aldehydic lipid oxidation products. Adduct formation is greatest for alpha,beta-monounsaturated followed by polyunsaturated and saturated aldehydes. While the ability of carnosine to form adducts with aldehydic lipid oxidation products is lower than other compounds such as glutathione, the higher concentrations of carnosine in skeletal muscle are likely to make it the most important molecule that forms aldehyde adducts. Monitoring changes in carnosine concentrations in oxidizing skeletal muscle shows that carnosine oxidation does not occur until the later stages of oxidation suggesting that carnosine may not be as effective free radical scavenger in vivo as other antioxidants like alpha-tocopherol.

Ability of surfactant hydrophobic tail group size to alter lipid oxidation in oil-in-water emulsions.

Oxidation of oil-in-water emulsion droplets is influenced by the properties of the interfacial membrane surrounding the lipid core. Previous work has shown that an important factor in the oxidation of oil-in-water emulsions is surfactant properties that impact interactions between water-soluble prooxidants and lipids in the emulsion droplet. The purpose of this research was to study the impact of surfactant hydrophobic tail group size on lipid oxidation in oil-in-water emulsions stabilized by polyoxyethylene 10 lauryl ether (Brij-lauryl) or polyoxyethylene 10 stearyl ether (Brij-stearyl). The ability of iron to decompose cumene peroxide was similar in hexadecane emulsions stabilized by Brij-stearyl and Brij-lauryl. Oxidation of methyl linoleate in hexadecane emulsions containing cumene peroxide was greater in droplets stabilized by Brij-lauryl than in those stabilized by Brij-stearyl at pH 3 with no differences observed at pH 7.0. Oxidation of salmon oil was greater in emulsions stabilized by Brij-lauryl than in those stabilized by Brij-stearyl as determined by both lipid peroxides and headspace propanal. These results suggest that surfactant hydrophobic tail group size may play a minor role in lipid oxidation in oil-in-water emulsions.

Ability of surfactant headgroup size to alter lipid and antioxidant oxidation in oil-in-water emulsions.

Oxidation of oil-in-water emulsion droplets is influenced by the properties of the interfacial membrane surrounding the lipid core. To evaluate how surfactant headgroup size influences lipid oxidation rates, emulsions were prepared with polyoxyethylene 10 stearyl ether (Brij 76) or polyoxyethylene 100 stearyl ether (Brij 700), which are structurally identical except for their hydrophilic headgroups, with Brij 700 containing 10 times more polyoxyethylene groups than Brij 76. Fe(2+)-promoted decomposition of cumene hydroperoxide was lower in Brij 700-stabilized than in Brij 76-stabilized hexadecane emulsions. Fe(2+)-promoted alpha-tocopherol oxidation rates were similar in hexadecane emulsion regardless of surfactant type. Brij 700 decreased production of hexanal from methyl linoleate and the formation of lipid peroxides and propanal from salmon oil compared to emulsions stabilized by Brij 76. These results indicate that emulsion droplet interfacial thickness could be an important determinant in the oxidative stability of food emulsions.