Functional properties of dehulled sesame (sesamum indicum L.) seed flour

Certain functional properties of sesame seed flour were obtained after oil extraction from dehulled seed meal was investigated. The protein content in the flour was 69.7% and the least gelation concentration was 6.0%. Water and oil absorption capacities at room temperature (31 ± 2°C) were 2.3 g H₂O/g sample and 3.0 g oil/g sample, respectively. The values were higher at 100°C. The emulsification capacity, which was more stable at alkaline conditions, ranged from 25.0 mL oil/g sample at pH 4 to 66.0 mL oil/g sample at pH 10. The foaming capacity was more stable at pH 4 but lower (205.0%). The highest foaming capacity (315.0%) was at pH 2 whereas at pH 10 it was 310.0%. Protein solubility, which was least at pH 4, ranged from 7.9% at pH 2 to 14.2% at pH 10. The viscosity of the flour dispersion ranged from 2.5 cps at 1% concentration to 7.0 cps at 10% concentration. The findings show that sesame flour could impart desirable characteristics when incorporated into products such as ice cream, frozen dessert, sausages, baked food and confections.     

Functional and nutritional properties of acylated rapeseed proteins

Rapeseed flour was acylated to various degrees with acetic and succinic anhydrides to produce acetylated rapeseed protein concentrates (SRPC) and succinylated rapeseed protein concentrates (SRPC), respectively. With both acylating agents, approximately 5–82% (ARPC-5 to ARPC-82) and 5–56% (SRPC-5 to SRPC-56) of ε-amino groups of lysine were acylated. Changes in functional properties were monitored; nitrogen solubility, emulsifying properties and specific viscosity were improved by acylation. The effects on functional properties were more pronounced with succinylation than acetylation. The nutritive value of succinylated rapeseed protein concentrates was determined and compared with those of unmodified rapessed protein concentrate and rapessed flour. Succinylation reduced the availability of lysine and decreased (p<0.05) the net protein ratio (NPR) and apparent digestibility coefficient (ADC) of nitrogen in rapessed protein concentrates. Supplementation of SRPC with lysine improved the NPR compared to that of SRPC-56.     

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 oilseed proteins

The functional and physical properties, rather than the nutritional value, of protein in protein-containing products will largely determine their acceptability as ingredients in prepared foods. The nature of the protein per se, the presence of other constituents naturally present in protein-containing products, the degree to which the protein product is refined, the presence of other ingredients in a food system to which protein products are added, manufacturing conditions and a number of other factors, working singly or together, will influence the way proteins (as well as other ingredients) exert their functional characteristics. Differences in these characteristics are presented with examples of the manner in which various factors can influence functionality. Nonfunctional properties may be of interest for certain applications. Presented at the AOCS-AACC Joint Protein Short Course, French Lick, Indiana, July 13–16, 1969.     

可得然胶功能特性及在肉及肉制品中的应用进展

可得然胶是一种微生物胞外多糖,因其良好的增稠、持水、凝胶以及成膜等性能,近些年在肉类加工及保鲜领域得到了广泛的应用。该文综述了可得然胶的功能特性,重点阐述了可得然胶对肉及肉制品品质特性的影响及其对肉品的品质提升机制,最后总结了由可得然胶制备的不同类型可食性复合膜在肉类保鲜中的应用效果,以期为可得然胶在肉类加工和保鲜领域的广泛应用提供理论参考。     

Adhesive properties of soy proteins modified by urea and guanidine hydrochloride

An investigation was conducted on the adhesive and water-resistance properties of soy protein isolates that were modified by varying solutions of urea (1, 3, 5, and 8 M) or guanidine hydrochloride (GH) (0.5, 1, and 3 M) and applied on walnut, cherry, and pine plywoods. Soy proteins modified by 1 and 3 M urea showed greater shear strengths than did unmodified protein. The 3 M urea modification gave soy protein the highest shear strength. Soy proteins modified with 0.5 and 1 M GH gave greater shear strengths than did the unmodified protein. The 1 M GH-modified soy protein gave the highest shear strength. Compared to the unmodified protein, the modified proteins also exhibited higher shear strengths after incubating with two cycles of alternating relative humidity, zero delamination, and higher remaining shear strengths after three cycles water soaking and drying. These results indicate that soy proteins modified with urea and GH enhance water resistance as well as adhesive strength. Secondary structures of globule proteins may enhance adhesion strength, and the exposure of hydrophobic amino acids may enhance water resistance. Proteins modified by 3 M urea or 1 M GH may have higher content of secondary structure and more exposed hydrophobic amino acids, compared with other modifications or unmodified proteins.     

Emulsifying capacity of coconut proteins as a function of salt,phosphate, and temperature

Nitrogen solubilities of proteins in defatted coconut flour (CF) and coconut protein concentrate (CPC), prepared by ultrafiltration, were determined in water and 2% NaCl. The effect of temperature, disodium phosphate, and salt on emulsifying capacities (EC) of these products also were investigated by a model system. Between pH 4.0 and 5.0, nitrogen solubilities of CF and CPC in water were lower than those in salt solutions. In salt solutions, the nitrogen solubility was lowest at pH 1, and increased steadily as pH increased from 3.0 to 6.0. CF had higher EC values than CPC at all salt and phosphate levels. Additionally, increased phosphate level generally increased the EC at both salt levels, but these increases were not significant at 0.9% phosphate level as compared to the 0.7% phosphate level (P<0.05). Although the emulsifying temperature of 40°C showed higher EC values than both 60 and 80°C at all salt and phosphate levels, the overall temperature effect was not significant (P>0.05). However, EC decreased significantly with the addition of salt at all phosphate levels.     

Heat-induced gelation of rapeseed proteins: Effect of protein interaction and acetylation

The gel-forming abilities of a rapeseed protein isolate, composed of 70% globulin (cruciferin) and 30% albumin (napin), and their individual protein components, were investigated. The influence of acetylation upon the gelation properties was also studied. Highest gel strength (measured as shear modulus) of the isolate was obtained at pH values around 9, which is between the isoelectric points of both major proteins. Purified cruciferin gave the highest shear modulus values, with maxima at pH 6 and 8. Weak and poorly stable gels exhibiting strong hysteresis were obtained with isolated napin. Acetylation resulted in a pH shift of the shear modulus maximum of the protein isolate to about 6. The gelation temperature of the acetylated isolate had the highest pH and concentration dependence compared with the other proteins.     

Physicochemical properties of pronase-treated rice glutelin

Rice glutelin protein was extracted from defatted medium-grain rice by alkali extraction followed by acid precipitation. Extracted glutelin was hydrolyzed with Pronase E, a bacterial protease, and the functional properties of hydrolysates were evaluated. Nitrogen solubility of pronase-treated glutelin protein increased from pH 2 to pH 12. Similarly, foaming and emulsion properties of hydrolyzed protein also showed improved characteristics. The emulsion activity, expressed as the turbidity of diluted emulsions, was significantly greater (P≤0.05) for hydrolyzed samples. However, turbidity for all samples decreased with increased homogenization time, indicating a decrease in the volume of dispersed oil. There were significant changes in apparent viscosity as a function of shear rate, with viscosity decreasing with increasing shear rate. The viscosity of dispersions of all hydrolyzed samples was significantly lower than that of the native sample at all shear rates tested. Enzymatic hydrolysis of rice endosperm storage glutelin proteins appeared to improve the functional characteristics of the hydrolyzed proteins.     

Functional properties of chemically modified egg white proteins

Functional properties of egg white proteins can be altered through selected chemical reactions. Acylations with acid anhydrides have received the greatest amount of attention. Oleic acid and sodium dodecyl sulfate (SDS) have also been used to affect function of egg white proteins. The charge characteristics of acylated proteins are altered through modification of the N-terminal and epsilon-amino groups. The acid anhydride used and the extent of modification have a major effect on the ionic properties of the protein. The altered ionic properties have been shown to affect the optical properties of protein sols, heat stability, foaming, performance in angel cakes, initiation of gelation, ultimate strength and freeze-thaw stability of heat-set gels. Although exact explanations of the mechanisms for the interactions of oleic acid and SDS with egg white protein are not available, increases in charge occur and result in gels with physical properties very similar to gels made from succinylated egg protein.     

Functional properties of hydrothermally cooked soy protein products

The effects of hydrothermal cooking on the functional properties of defatted soy flour, aqueous alcohol washed soy protein concentrate, and soy protein isolate were determined in samples that were treated at 154°C by infusing steam under pressure for 11, 19, 30, and 42 s, and then spray dried. Hydrothermal cooking increased the nitrogen solubility index (NSI) of the concentrate from 15 to 56% and altered the solubility profile from a flat profile to one more typical of native soy protein. Hydrothermal cooking also improved foaming and emulsifying properties of the concentrate. For isolate, hydrothermal cooking also improved NSI and foaming and emulsifying properties, although the improvements were less dramatic than with concentrate. NSI and emulsifying properties of the flour were improved by some processing conditions, but foaming properties were not improved by hydrothermal cooking. Dramatically increased protein solubility of concentrate and modestly improved protein solubilities of flour and isolate by hydrothermal cooking, which will also inactivate trypsin inhibitors and microorganisms, have considerable practical significance to protein ingredient manufacturers and those who use these ingredients in foods and industrial products.     

A universal expression tag for structural and functional studies of proteins

Modified ubiquitin sequences, each completed with a His tag and a TEV cleavage site, were designed to enhance the expression of protein/peptide targets. With this new system we have been able to characterize several peptide-protein interactions by ITC and by NMR and CD spectroscopic methods, including the interactions of LIR domains with autophagy modifiers.     

Cure and properties of thermosetting systems

A generalised time-temperature-transformation cure diagram for thermosetting systems is discussed from the point of view of understanding relationships between cure, properties, and thermal degradation.     

Adhesive properties of soy proteins modified by sodium dodecyl sulfate and sodium dodecylbenzene sulfonate

A study was conducted on adhesive and water-resistance properties of soy protein isolates modified by sodium dodecyl sulfate (SDS) (0.5, 1, and 3%) and sodium dodecylbenzene sulfonate (SDBS) (0.5, 1, and 3%) and applied on walnut, cherry, and pine plywoods. Soy proteins modified by 0.5 and 1% SDS showed greater shear strengths than did unmodified protein. One percent SDS modification had the highest shear strength within each wood type tested. Soy proteins modified with 0.5 and 1% SDBS also showed greater shear strengths than did the unmodified protein. The 1% SDBS-modified soy protein had the highest shear strength in all wood samples tested. Compared to the unmodified protein, the modified proteins also exhibited higher shear strengths after incubation with two cycles of alternating relative humidity and zero delamination rate and higher remaining shear strengths after three cycles of water soaking and drying. These results indicate that soy proteins modified with SDS and SDBS have enhanced water resistance as well as adhesive strength. Possible mechanisms for the effects of SDS and SDBS also are discussed.     

不同保水剂对石膏性能的影响

本文研究半水石膏中掺入甲基纤维素、羧甲基纤维素、糊精和膨润土四种保水剂后石膏基料浆保水性及凝固件储水性与强度的变化趋势.结果表明:掺入0.5％甲基纤维素时石膏基料浆保水性最好,扩展直径和滤纸吸水率分别为81 cm和52 mg/cm2;掺入保水剂可提高石膏基凝固件水分保持率,延长水分保持时间;掺入保水剂后凝固件强度明显降低,掺入25％膨润土后凝固件抗折和抗压强度值分别仅为3.02 MPa和5.96 MPa,分别为纯石膏凝固件的41.83％和37.94％.掺入沙粒后会加快凝固件中水分释放速率并降低凝固件强度.     

Preparation and photochromic properties of waterborne polyurethane containing spirooxazine groups

Two novel photochromic spirooxazines, SO 1 and SO 3, were successfully prepared and characterized by Fourier transform infrared spectroscopy (FTIR), ¹H-NMR, and mass spectrometry with electrospray ionization (ESI-MS). SO 1 was doped and grafted with waterborne polyurethane (WPU) to afford D₁-WPU and G₁-WPU. D₃-WPU was prepared by doping SO 3 with waterborne polyurethane. FTIR spectra indicated that SO 1 was grafted onto waterborne polyurethane successfully. Scanning electron microscopy proved that spirooxazines of D-WPU can be effectively dispersed in a waterborne polyurethane matrix, and spirooxazines of G-WPU are evenly distributed in the copolymer. The results showed that the light transmittance of modified waterborne polyurethane films decreased compared with pure waterborne polyurethane films, but the water resistance and tensile strength were better. Ultraviolet–visible spectra demonstrated that the thermal stability of spirooxazine derivatives improved significantly after being modified. The fading rate constant of the D₃-WPU film (k = 0.0079 s^-1) during the discoloration process decreased 9.77 times in contrast to SO 3 in ethanol, which showed that the thermal stability of spirooxazine in WPU film was obviously enhanced. © 2018 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2019 , 136, 47067.     

Functional Characterization of Cardiac Actin Mutants Causing Hypertrophic (p.A295S) and Dilated Cardiomyopathy (p.R312H and p.E361G)

Human wild type (wt) cardiac α-actin and its mutants p.A295S or p.R312H and p.E361G correlated with hypertrophic or dilated cardiomyopathy, respectively, were expressed by using the baculovirus/Sf21 insect cell system. The c-actin variants inhibited DNase I, indicating maintenance of their native state. Electron microscopy showed the formation of normal appearing actin filaments though they showed mutant specific differences in length and straightness correlating with their polymerization rates. TRITC-phalloidin staining showed that p.A295S and p.R312H exhibited reduced and the p.E361G mutant increased lengths of their formed filaments. Decoration of c-actins with cardiac tropomyosin (cTm) and troponin (cTn) conveyed Ca²⁺-sensitivity of the myosin-S1 ATPase stimulation, which was higher for the HCM p.A295S mutant and lower for the DCM p.R312H and p.E361G mutants than for wt c-actin. The lower Ca²⁺-sensitivity of myosin-S1 stimulation by both DCM actin mutants was corrected by the addition of levosimendan. Ca²⁺-dependency of the movement of pyrene-labeled cTm along polymerized c-actin variants decorated with cTn corresponded to the relations observed for the myosin-S1 ATPase stimulation though shifted to lower Ca²⁺-concentrations. The N-terminal C0C2 domain of cardiac myosin-binding protein-C increased the Ca²⁺-sensitivity of the pyrene-cTM movement of bovine, recombinant wt, p.A295S, and p.E361G c-actins, but not of the p.R312H mutant, suggesting decreased affinity to cTm.     

Rheological properties of new polymer compositions for sand consolidation and water shutoff in oil wells

The rheological properties of some newly developed polymer compositions have been investigated with and without crosslinking. These polymer compositions were developed as a water shutoff and sand consolidation treatment agents for producing oil and gas wells. The effects of several variables on the rheology of the compositions were evaluated over a wide range of temperatures (25–110°C), shear rates (0–500 s^?1), brine percentages (0–15%), crosslinker types and concentrations (0–3%), and polymer concentrations (6–50%). It was found that increasing the shear rate from 0 s^?1 to 100 s^?1 caused shear thinning and reduction of the viscosity of the dilute solutions (6–13%) from 25 cP to ～ 3 cP at 80°C. In contrast, for the concentrated solutions (20–50%), the viscosity dropped slightly in the shear rate range 0–10 s^?1, and subsequently decreased more slowly up to shear rates of 500 s^?1. The viscosities of all polymer solutions dropped by a factor of 2 as the brine concentration increased from 0% to 15%. Finally, aging time coupled with shear rates and higher percentages of crosslinkers accelerate the buildup of viscosity and gelation time of the polymer compositions. For concentrated solutions, shear rates ranging within 0–200 s^?1 accelerated gelation time from 9.75 h to 2–3 h, when they were sheared at 80°C. The polymeric solutions exhibited Newtonian, shear‐thinning (pseudo‐plastic), and shear‐thickening (dilatant) behavior, depending on the concentration, shear rate, and other constituents. In most cases, the rheological behavior could be described by the power law. © 2007 Wiley Periodicals, Inc. J Appl Polym Sci 2007     

Functional properties of protein ingredients prepared from high-sucrose/low-stachyose soybeans

High-sucrose/low-stachyose (HS/LS) soybeans were used to prepare ethanol-washed soy protein concentrate (EWSPC), soy protein isolate (SPI), and a new low-fiber soy protein concentrate (LFSPC) in which the protein was extracted with alkali to remove fiber and the protein extract was neutralized and freeze-dired. LFSPC prepared from HS/LS soybeans contained significantly higher ratios of β-conglycinin to glycinin (1∶1.32) than did EWSPC (1∶1.75) or SPI (1∶1.69), which may have affected functional properties. The LFSPC were also high in soluble sugars (14.7%) and low in fiber (0.3%) compared with traditional EWSPC (2.9 and 3.4%, respectively) and SPI (1.8 and 0.3%, respectively). For both normal and HS/LS soybean varieties, the LFSPC, especially when extracted at pH 7.5 as opposed to pH 8.5, had higher denaturation enthalpies than did EWSPC and SPI, indicating less denaturation had occurred. Water solubilities, surface hydrophobicities, and emulsification properties were highest for the LFSPC and lowest for EWSPC. The LFSPC also had good foaming properties and low viscosities. These desirable functional properties of the LFSPC make them unique among alternative soy protein ingredients and highly suitable for industrial applications as food additives and ingredients.     

Functional characteristics of cowpea flours in foods

Functionality of legume flours as food ingredients is influenced by genetic and agronomic factors, storage, composition and processing. The processing of flour from dry cowpeas (Vigna unguiculata) is a simpler technology than that utilized for oilseed flour production. A defatting step is not required because the crude fat content of cowpeas is low (∼1–2%); however, decortication (seed coat removal) is necessary if a light-colored flour is to be obtained from cultivars with dark testa or eyes. Process condition employed in the decortication of cowpeas and production of cowpea flour influence the quality of subsequent products made from the flour. Functionality of cowpea flour as an ingredient in wheat flour mixtures, akara and moin-moin (fried and steamed cowpea paste, respectively), extruded products and meat products will be reviewed. Presented at the 78th American Oil Chemists' Society Annual Meeting, May 17–21, 1987, New Orleans, LA.