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Use of hydrolyzed proteins is known to delay hardening of high-protein nutrition bars. Bars were formulated using ratios of 0%, 25%, 50%, 75%, or 100% partially hydrolyzed whey protein isolate (HWPI) to nonhydrolyzed whey protein isolate (WPI) in one experiment, and either WPI or HWPI combined with high-fructose corn syrup (HFCS) or sorbitol syrup (SS) in a 2nd experiment along with vegetable shortening such that initial aw was 0.59 for HWPI bars and 0.64 for WPI bars. After mixing, the dough was extruded into bars and stored at 32 °C for accelerated shelf-life testing. Hardness, color, and microstructure were measured during 42 d of storage. Bars initially had similar hardness of approximately 3.4 N that increased during storage. Bars with HWPI were softest with hardness at 37 d of 10 to 15 N compared to almost 100 N for bars with WPI. Water activity increased for WPI bars to 0.69 by 34 d. Bars became darker during storage depending on amount of Maillard browning reactants, that is, HWPI/HFCS bars ≫ HWPI/SS > WPI/HFCS bars > WPI/SS bars. Bar microstructure at day 2 showed protein and fat dispersed in particulate form throughout the carbohydrate syrup within the bar matrix. During storage, a single nonlipid phase developed in HWPI bars while in WPI bars a phase separation occurred between protein and carbohydrate. We propose that such phase separation initiates bar hardening and promotes subsequent protein aggregation. Successful formulation of HPN bars depends on cosolvent properties of the polyol/sugar toward the proteins and their preferential exclusion from the solvation layer surrounding the proteins. PRACTICAL APPLICATION: High-protein nutrition bars can be formulated so they remain soft during storage by selecting proteins and sugars that are compatible with each other. Otherwise, the protein and sugar will separate from each other which can then lead to hardening. [ABSTRACT FROM AUTHOR]

Barley contains several valuable nutrients including beta-glucan (BG), protein, and starch. Each has additional value when concentrated. Dehulled and hulless barleys were sequentially pearled for 1 to 6 cycles, each with 8% removal. The 6 pearled kernels and the initial kernel were subjected to impact or abrasive milling, followed by sieving with a series of U.S. standard sieves. Results of pearling fines show that protein was most concentrated in the outer area, and decreased all the way toward the core area (near 100% surface removal). Starch showed an opposite trend. BG followed the starch trend, but reached a peak at about 60% surface removal. Upon milling and sieving of kernel samples, genotype and particle size had significant effects on nutrient contents in sieved fractions. The pearling cycle had significant effects on protein and starch contents but little effect on BG content, while the milling method had significant effects on protein and BG contents but little on starch content. Abrasive milling produced sieved fractions with much higher variation in protein content than impact milling, but the opposite effect was observed for shifting BG content. Mass frequency influenced more on recovery rates of nutrients than their concentrations in individual fractions. When the recovery rate was also taken into consideration, pearling alone was found to be the most effective way to enrich protein in barley kernels. However, a combination of pearling with the method of milling and sieving was needed for maximally shifting BG and starch contents. PRACTICAL APPLICATIONS: Although dry fractionation is the method of choice for separating barley into fractions with varying levels of protein, BG, and/or starch, selection of a specific single or combined method is needed for achieving maximum shifts of a particular nutrient. Such information is significant to those who use dry fractionation methods to enrich protein, BG, and/or starch. [ABSTRACT FROM AUTHOR]

Dialdehyde starch (DAS) was added to pork ham batter. The effects of DAS on the meat protein gel during heating were investigated using thermal and rheological analyses. In this study, the degree of DAS oxidation was controlled by the reaction time. The DSC thermogram showed that increasing the degree of oxidation resulted in DAS having a higher gelatinization temperature and lower heat absorption. In dialdehyde starch/meat (DAS/M) composites, meat protein reduced the availability of water to starch and raised the gelatinization temperature and heat absorbed by the composites. The G′max of the composites was greater than the linear combination of their components. The rheological properties of DAS were a major factor affecting the properties of its composites. Scanning electron microscopy and light microscopy with the aid of histologic technique revealed the network and distribution of DAS and DAS/M composites. The protein matrix formed the backbone of the network and gelatinized starch was trapped in the protein structure. [ABSTRACT FROM AUTHOR]

The effect of heat treatment on the denaturation of Cry1A(b) protein expressed in transgenic maize was studied over a temperature range of 69 to 77 °C. Denaturation of Cry1A(b) protein was measured by the loss of reactivity with its specific antibodies using a sandwich ELISA. The process of denaturation was studied by analyzing the values of inmunoreactive protein after each heat treatment by kinetic analysis. Denaturation of Cry1A(b) protein was best described assuming a reaction order of 1.5. D-values calculated were 4338, 2350, 1272, 734, and 601 s at 69, 71, 73, 75, and 77 °C, respectively. Z-value was estimated to be 9.0 °C and the activation energy value was 266.15 kJ/mol. Thermodynamic parameters for the process of denaturation of Cry1A(b) protein were also calculated. The high values of the enthalpy of activation and the positive values of the entropy of activation obtained for Cry1A(b) protein are typical of a reaction in which the denaturation of the protein is the rate-determining process that predominates over an aggregation process during heating. [ABSTRACT FROM AUTHOR]

A 3-component mixture experiment was used to optimize the formulation of broken-rice based snack fortified with protein and fiber based on consumer sensory acceptability. Soy protein isolate and guar gum were used as a good source of protein and fiber, respectively, according to DRV (daily reference value) based on a 2000-calorie diet. A consumer panel evaluated sensory acceptability of color, crispness, and flavor, and overall liking of 12 experimental broken-rice based snack formulations. Predicted models derived from the restricted nonintercept regression analysis were used to plot mixture response surfaces (MRS) of each sensory attribute. Areas within the MRS plots having predicted acceptability scores of at least 6.5 (on a 9-point hedonic scale) for color, crispness, flavor, and overall liking were selected to derive a predicted optimum formulation range. Flavor acceptability was a limiting factor in attaining the optimum formulation range, which consisted of 40% to 48% broken-rice flour, 8% to 16% guar gum, and 20% to 33% soy protein isolate. To verify the obtained predicted models, the formulation containing 48% broken-rice flour, 8% guar gum, and 20% soy protein isolate, which was located in the optimum area, was chosen to support our effort to utilize and add value to broken rice. Selected physicochemical measurements of the chosen optimized formulation were determined. One serving size (30 g) of the chosen optimized snack product provided 6.58 g protein and 3.80 g dietary fiber, which met the US FDA definition of a good source of protein and dietary fiber. [ABSTRACT FROM AUTHOR]

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. [ABSTRACT FROM AUTHOR]

To evaluate a practical method of determining more accurately conversion factors for calculating the protein contents of foods from the total nitrogen content, 19 cereal products found in Japan were analyzed for total nitrogen, amino acid nitrogen, and amide nitrogen, and then the nitrogen-to-protein conversion factors were calculated. The average conversion factors were 5.75 for rice, 5.81 for wheat, and 5.95 for others. These values, corresponding to the proportion of the amino acid residue to amino acid nitrogen recovered from 20 amino acids, were lower than the currently applied factors to these foods, except for wheat flour and amaranth. The use of this factor for estimating the protein content results in a considerable difference from the estimate based on amino acid residue concentrations, due to the wide variations in amino acid composition and to the presence of a significant level of nonprotein nitrogen. The distribution of the protein nitrogen recovered from the amino acids to total nitrogen averaged 93%. Adjusted conversion factors corresponding to the proportion of the amino acid residue to total nitrogen averaged 5.26 for rice, 5.47 for wheat, and 5.54 for other cereal products. Protein contents estimated using these factors are in good agreement with the contents defined as amino acid residues. [ABSTRACT FROM AUTHOR]

Increasing interest in high-quality food products with increased shelf life and reduced environmental impact has encouraged the study and development of edible and/or biodegradable polymer films and coatings. Edible films provide the opportunity to effectively control mass transfer among different components in a food or between the food and its surrounding environment. The diversity of proteins that results from an almost limitless number of side-chain amino-acid sequential arrangements allows for a wide range of interactions and chemical reactions to take place as proteins denature and cross-link during heat processing. Proteins such as wheat gluten, corn zein, soy protein, myofibrillar proteins, and whey proteins have been successfully formed into films using thermoplastic processes such as compression molding and extrusion. Thermoplastic processing can result in a highly efficient manufacturing method with commercial potential for large-scale production of edible films due to the low moisture levels, high temperatures, and short times used. Addition of water, glycerol, sorbitol, sucrose, and other plasticizers allows the proteins to undergo the glass transition and facilitates deformation and processability without thermal degradation. Target film variables, important in predicting biopackage performance under various conditions, include mechanical, thermal, barrier, and microstructural properties. Comparisons of film properties should be made with care since results depend on parameters such as film-forming materials, film formulation, fabrication method, operating conditions, testing equipment, and testing conditions. Film applications include their use as wraps, pouches, bags, casings, and sachets to protect foods, reduce waste, and improve package recyclability. [ABSTRACT FROM AUTHOR]

Select grade strip loins ( n= 10) were enhanced 10% with either a phosphate or an acid solubilized protein solution. Color score, aerobic plate count, lipid oxidation, purge loss, cook yield, Warner–Bratzler shear force, and sensory analysis were measured to characterize storage quality. The phosphate injection consisted of 4.5% phosphate, 3.6% sodium chloride, 90.9% water, and 1% Herbalox seasoning. Two solutions were prepared for the protein injection: one consisting of 1:9 protein to water and the other an aqueous solution of 1% Herbalox seasoning and 3.6% sodium chloride. Enhancement solutions were injected twice at 5% to create a 10% total injection. It was found that the protein-enhanced steaks were comparable to phosphate-enhanced steaks for percent discoloration and overall acceptability. The phosphate-enhanced steaks performed better than the protein-enhanced steaks for lean color, fat color, aerobic plate count, lipid oxidation, percent purge, cook yield, and Warner–Bratzler shear force. It should be noted that for protein-enhanced steaks, lean color and cook yield, although statistically different, did perform similar to phosphate-enhanced steaks. [ABSTRACT FROM AUTHOR]

Both the dielectric constant and loss factor increased at a temperature that appeared to match the DSC denaturation temperature for collagen in beef, chicken breast, chicken thigh, perch, cod, and salmon. When the sample was reheated the change did not reoccur, indicating that the dielectric properties were measuring an irreversible change. At lower frequencies the increase in the dielectric properties was larger. When collagen and actomyosin denature, the muscle shrinks, expelling water and minerals. This makes the water and ions more mobile. The dielectric constant and loss factor measure the mobility of water and ions; therefore they may be able to determine the temperature of protein denaturation. [ABSTRACT FROM AUTHOR]

From 5% w/v whey protein isolate (WPI), whey protein/lipid emulsion edible films were produced that were sorbitol- or glycerol-plasticized, containing butterfat (0.2% w/v) or candelilla wax (0.8% w/v). Thermal properties of the films determined by Differential Scanning Calorimetry (DSC) showed onset temperatures (To) of 126 to 127 °C for sorbitol- and 108 to 122 °C for glycerol-plasticized films. To values were used as the basis for heat sealing temperatures. Temperature (110, 120, 130 °C], pressure (296, 445 kPa), and dwell time (1, 3 s) affected seal strength. Optimum heat sealing temperature was 130 °C for sorbitol- and 110 °C for glycerol-plasticized films. All films were heat sealable with an impulse heat-sealer. Electron Spectroscopy for Chemical Analysis (ESCA) of the surfaces of both sealed and unsealed films showed increase in hydrogen and covalent bonds involving C-O-H and N-C, which may be the main forces responsible for the sealed joint formation of the films. [ABSTRACT FROM AUTHOR]

Twenty (JAPANESE) vegetables in Japan were analyzed for total nitrogen, amino acid nitrogen, amide nitrogen, and nonprotein nitrogen and then calculated nitrogen-to-protein conversion factors were calculated. The average conversion factor based on quantitative amino acid composition data was 6.00. However, the use of this factor for estimating protein content led to a considerable difference from estimates based on amino acid residue concentrations, due to the presence of high levels of nonprotein nitrogen. The distribution of protein nitrogen to total nitrogen averaged 73%. Adjusted conversion factors, defined as the proportion of amino acid nitrogen to total nitrogen, averaged 4.39. Protein contents estimated with this factor agreed well with contents determined by amino acid residues. [ABSTRACT FROM AUTHOR]

Chemical analysis showed soft snow crab muscle to have a higher water content and a lower protein content than hard crab muscle. Histological observations revealed frequent occurrences of disintegrated regions in muscle fibers and pericellular connective tissue of soft snow crab muscle tissue. Salinity of the free body fluid recovered from the meropodites of the soft snow crab was significantly higher than that of the hard snow crab. Sensory evaluation revealed differences in texture and taste between soft and hard crabs, which corresponded well to their compositional and histological differences. [ABSTRACT FROM AUTHOR]

Interactions between bovine serum albumin (BSA) and 4 classes of flavor compounds (alcohols, esters, aldehydes, and ketones) in aqueous solution were investigated using solid phase microextraction (SPME) of sample headspace and gas chromatography. Alcohols did not bind significantly to BSA. The binding of fixed amounts of individual flavor compounds with each functional group to increasing amounts of BSA was modeled as a function of several descriptors using partial least squares regression (PLSR). Ester binding was modeled as a function of the number of carbon atoms in a molecule and its boiling point ( R2= 0.954). Aldehyde binding was modeled as a function of the number of hydrogen atoms and boiling point ( R2= 0.922). Ketone binding was modeled as a function of the numbers of carbon atoms, length of the longer hydrocarbon chain, and degree of branching ( R2= 0.961). [ABSTRACT FROM AUTHOR]

Purple corn ( Zea mays L.) is a rich and economic source of anthocyanin colorants and functional ingredients. However, high levels of anthocyanin-rich waste are generated during processing, reducing the yields and increasing the costs of the final product. This waste has been associated with anthocyanin complexation with tannins and proteins. Our objective was to evaluate anthocyanin extraction methods to reduce purple corn waste. Different solvents (water, 0.01%-HCl-acidified water, and 0.01%-HCl-acidified ethanol), temperatures (room temperature, 50, 75, and 100 °C), and times of exposure to the solvents were investigated. Acetone (70% acetone in water) extraction was used as control. Anthocyanins, total phenolics, tannins, and proteins in extracts were measured by the pH differential, Folin-Ciocalteu, protein precipitation, and BCA assay methods. Qualitative analyses were done by HPLC coupled to a PDA detector and SDS-PAGE analysis. Water at 50 °C achieved the highest yield of anthocyanins (0.94 ± 0.03 g per 100 g dry corncob) with relatively low tannins and proteins, comparable to the anthocyanin yield obtained by 70% acetone (0.98 ± 0.08 g per 100 g dry corncob). Extending the extraction time from 20 to 60 min and using consecutive reextraction procedures reduced anthocyanin purity, increasing the yields of other phenolics. A neutral protease was applied to the extracts and effectively decomposed the major protein that was believed to contribute to the development of anthocyanin complexation and waste generation. Extraction time, consecutive reextraction procedures, and enzyme hydrolysis should be considered for high yield of anthocyanins and waste reduction. [ABSTRACT FROM AUTHOR]

Colloidal hard-sphere (HS) particles of narrow-size distribution exhibit crystalline and glassy states beginning at the particle volume fractions φ= 0.494 and φG= 0.58, respectively. Dynamic rheological data on the dispersions were strongly modified to solid-like behavior as φ approached φG. In addition, cooperative motion in structural relaxation has been observed microscopically in the colloidal dispersions near the glassy state. Very high viscosities and glassy states were also found in high-concentration dispersions of sodium caseinate and the globular proteins: bovine serum albumin and β-lactoglobulin. Viscosity models developed for HS dispersions predicted accurately the trends but not the absolute values of protein dispersions. Dispersions of food colloidal particles may be employed in studies, in which volume fraction is the thermodynamic variable, for understanding the relaxation and transport processes related to 1st-order and colloidal glass transitions. [ABSTRACT FROM AUTHOR]

Amaranth protein–lipid (PL) and protein (P) films were elaborated and compared with amaranth flour films in order to determine the contribution of the interactions between the biopolymer (starch and protein) and the lipids to the film properties. The films were made by the casting method, using the same glycerol concentration (0.9 g glycerol/100 g solution). A separation of the lipid fraction in the PL films and a polymorphic transformation of the corresponding fatty acids were observed by differential scanning calorimetry (DSC) and verified by an analysis of the microstructure by scanning electron microscopy (SEM). The flour films showed no separation of the lipid fraction, evidence that the lipids were strongly associated with the proteins and homogenously distributed throughout the starch network, contributing to the good mechanical properties when compared to the PL films and to the excellent barrier properties when compared to both the PL and P films. The protein-protein interactions also contributed to the mechanical properties of the flour films. The presence of proteins and lipids in the flour films had an important effect on film solubility, and also on the color and opacity of the films. This study showed that the flour film properties depended on the interactions formed by their polymers (starches and proteins) and by the lipid, on the distribution of these interactions within the film matrix and on the concentrations of each component in the film. [ABSTRACT FROM AUTHOR]

Antioxidant properties in food are dependent on various parameters. These include the pH value and interactions with food components, including proteins or metal ions. Food components affect antioxidant stability and also influence the properties of microorganisms and their viability. This paper describes an investigation of the effect of pH on the antioxidant and antibacterial properties of caffeic acid in different media. The pH values studied, using an oil-in-water emulsion as model system, were 3, 5 (with and without phosphate buffer), and 9. Effects of mixtures of caffeic acid, bovine serum albumin (BSA), and Fe (III) on oxidative deterioration in the emulsion samples were studied. The results show that the antioxidant activity of caffeic acid was increased by the presence of BSA. This effect was pH dependent and was affected by the presence of iron ions. Antibacterial properties were also pH dependent. The minimum concentration of caffeic acid required to inhibit some microorganisms in the pH range of 5 to 7 was determined. A concentration of 0.4% (w/w) caffeic acid was enough to inhibit the growth of some of the studied microorganisms in the pH range of 5 to 7. However, near-neutral pH concentrations higher than 0.4% were needed to inhibit some microorganisms, including Listeria monocytogenes, E. coli, and Staphylococcus aureus, in the medium. [ABSTRACT FROM AUTHOR]

In order to determine whether milk proteins interact with cocoa polyphenols to modulate the uptake and concentration of polyphenols in plasma, 24 middle-aged men and women consumed 2 g of chocolate polyphenols, plus sugar and cocoa butter in 200 mL water, on 2 occasions. On 1 occasion, the chocolate mix contained 2.45 g of milk proteins. Blood samples were taken fasting and at regular intervals for 8 h. Catechin and epicatechins levels were measured in these samples and no differences were seen in average concentrations between the 2 treatments. Milk protein caused a slight increase in concentration at the early time points and a decrease at the later time points. In conclusion, milk powder did not influence the average concentration of polyphenols. While it slightly accelerated absorption, this is of no physiological significance. [ABSTRACT FROM AUTHOR]