Characteristics of Isolation and Functionality of Protein from Tomato Pomace Produced with Different Industrial Processing Methods

The seeds separated from tomato pomace may contain valuable protein with unique functional properties. The objectives of this research were to study the impact of industrial hot and cold break tomato processes on protein isolation from defatted tomato seed meal and determine the protein-related functional properties of defatted and non-defatted seed meals. The results showed that the high temperature of hot break process denatured the protein, resulting in the lower protein extraction yield from 9.07 % to 26.29 % for defatted hot break tomato seed (DHTS) compared to from 25.60 % to 32.56 % for defatted cold break tomato seed (DCTS) under various extraction conditions. Hot break process also significantly influenced protein-related functional properties of seed meals. Compared to DCTS, DHTS had higher water absorption capacity (WAC) and oil absorption capacity (OAC) based on the protein weight in the seed meal, but lower emulsifying ability (EA), emulsifying stability (ES), foaming capacity (FC), and foaming stability (FS) based on the whole seed sample weight. When compared to commercial soybean protein isolate (SP), the meals of hot break tomato seed (HTS), DHTS, and DCTS showed higher bulk density and WAC values. The FC and FS of tomato meals were inferior while the ES was superior to SP. High alkaline pH was beneficial to the protein extraction and achieved better EA, ES, FC and FS of all the samples. The results indicated that tomato seed meals have a great potential to be used as functional food ingredients.     

Protein Isolates from Bambara Groundnut (Voandzeia Subterranean L.): Chemical Characterization and Functional Properties

The physicochemical, functional, and thermal properties of protein isolates obtained from two varieties of Bambara groundnut were evaluated. Proteins were isolated using alkaline extraction (isoelectric precipitation [IEP]) and micellisation techniques. IEP recorded a higher protein yield (56.3–58.2 g/100 g) than the micellised protein (MP) (14.2 – 15.6 g/100 g). A similar trend was observed for the protein content of the isolates. The isolates contained a high level of lysine, arginine, and glutamic acid compared to soy protein. Minimum solubility of the flours of the two varieties occured at pH 5. MP isolates exhibited higher solubility than the corresponding isoelectric (IEP) isolates over all pH values. The micellised protein recorded superior functional characteristics than the isoelectric isolates. The micellised isolates also showed a significantly higher (P < 0.05) foam capacity and stability, oil and water absorption properties than the isoelectric isolate. The MP of both varieties also recorded significantly higher emulsifying properties-+ than their isoelectric protein isolates. The micellised protein also had better gelation properties than the isoelectric isolate. Micellised and isoelectric isolates did not reveal major differences in the electrophoretic patterns; both isolates had three major bands at 35.0, 43.0, and 112.0 kDa. The bands in the isoelectric protein isolate however, were well defined compared with the micellised isolate. All Bambara isolates were not dissociated by 1,4-Dithiothreitol (DTT) suggesting that they do not contain subunits linked by a disulphide bond. This suggests that 7S vicilin may be the major storage protein in Bambara groundnut isolates. Differential scanning calorimetry studies (DSC) of the two varieties of bambara groundnut proteins indicated that the thermograms of the micellised isolates have a higher denaturation temperature Td (97.9–108.4°C) than their corresponding isoelectric isolates (89.5–90.6°C).     

Fermentation of locust bean (Parkia biglobosa): modulation in the anti-nutrient composition,bioactive profile,in vitro nutrient digestibility,functional and morphological characteristics

The present investigation was undertaken with an objective to assess the impact of fermentation temperatures (22, 30, 38 and 46 °C for 72 h) on physico-chemical, functional and structural characteristics of locust bean (Parkia biglobosa). Alkaline fermentation treatment caused drastic reduction in anti-nutritional factors including tannins (~65%), phytates (~60%) and saponins (~70%) owing to hydrothermal treatment and production of microbial enzymes during fermentation. Furthermore, phytochemical profile and associated antioxidant potential were enhanced due to the breakdown of cell-wall components and polyphenolic complexes, liberating phenolic acids and flavonoids available for extraction. With respect to bioactive properties and in vitro starch and protein digestibility, the most pronounced effect was observed after fermentation at 38 °C for 72 h. The trend was also supported by scanning electron micrographs, which revealed modulation in the macromolecular-structural arrangement. Significant and negative correlation coefficients between anti-nutritional factors and protein digestibility (r > −0.95, P < 0.05) confirmed the degradation of protein–polyphenol matrix. Exposure of hydrophobic regions due to fermentation resulted in altered functional properties including better oil absorption capacity, higher water solubility index, reduced water absorption potential, and lower emulsification and gelation properties. Principal component analysis was further employed to statistically validate the differences among variables and observations.     

乙醇、氯化钙对大豆蛋白凝胶性影响的研究

研究了以大豆蛋白为原料制备的水凝胶、CaCl2凝胶和乙醇凝胶的流变学性质与吸水性,探讨了溶剂乙醇和无机盐CaCl2对大豆蛋白凝胶性及吸水性的影响。结果显示, 在动态应变扫描下,储能模量(G')的比较为:G'乙醇凝胶> G'C2Cl2凝胶>G'水凝胶,而产生损耗的应变值(S)为:S乙醇凝胶< SCaCl2凝胶相似文献   

Foaming Characteristics of Commercial Soy Protein Isolate as Influenced by Heat-Induced Aggregation

The foaming properties of commercial soy protein isolate subjected to different temperatures (20–90°C) were assessed. The results revealed that the solubility and surface hydrophobicity of a 5% (w/v) commercial soy protein isolate suspension increased with increasing temperature, which increased foaming capacity and reduced foaming stability. Commercial soy protein isolate supernatant (i.e., soluble fraction) had higher foaming capacity at low temperatures (20–50°C). A high content of commercial soy protein isolate soluble fraction increased foaming capacity but decreased foaming stability. The SDS-PAGE patterns and molecular weight distribution of commercial soy protein isolate revealed that there were soluble, large molecular weight aggregates (>400 kDa) formed mainly from A and B-11S polypeptides of commercial soy protein isolate via disulfide bonds. Additionally, some aggregates also dissociated into small polypeptides and subunits after heat treatment. Commercial soy protein isolate precipitate (i.e., insoluble fraction) had a high content of proline and cysteine, which probably contributed to the foaming stability of commercial soy protein isolate.     

Interactions and gel strength of mixed myofibrillar with soy protein, 7S globulin and enzyme-hydrolyzed soy proteins

The mixed protein gels were prepared adding soy protein isolate (SPI), 7S globulin, enzyme-hydrolyzed soy proteins, 10- to 100-kDa ultrafiltration fraction and 0.5- to 10-kDa ultrafiltration fraction to myofibril protein isolate (MPI) gels, and five chemical interactions namely nonspecific associations, ionic bonds, hydrogen bonds, hydrophobic interactions and disulfide bonds in these gels were investigated by means of determining gel solubility within 20–75 °C. Furthermore, correlations between gel strength and different chemical interactions were evaluated statistically by Pearson’s correlation test. The gels with 0.5- to 10-kDa fraction presented the biggest gel strength below 60 °C, and the gels with SPI had better gel strength above 65 °C. At different endpoint temperatures, nonspecific associations decreased in order of MPI mixed with 0.5- to 10-kDa fraction, 10- to 100-kDa fraction, enzyme-hydrolyzed soy proteins, 7S globulin and SPI. Gels with ultrafiltration fractions had higher ionic bonds. Hydrogen bonds fluctuated in small scale below 55 °C and reduced at higher temperature. Hydrophobic interactions increased to maximum before decreasing slowly as the temperature went on. In short, both hydrophobic interactions and ionic bonds had significantly positive correlation with gel strength for mixed gels with enzyme-hydrolyzed soy proteins, whereas for the other four mixed gels, it was hydrophobic interactions and nonspecific associations.     

Rheological Properties of Mozzarella Cheese Filled with Dairy, Egg, Soy Proteins, and Gelatin

The Rheological behavior of mozzarella cheese filled with various proteins (whey protein, caseinate, egg white, soy protein isolate, gelatin) incorporated was determined by uniaxial compression at 10°C and the effect of temperature (10°C?60°C) by dynamic measurement. Mozzarella cheese with whey protein, caseinate, egg white, and soy protein isolate showed significant water retention during heating. Among the proteins, soy protein isolate induced the strongest gel network structure with mozzarella cheese. All proteins altered the viscoelastic properties of mozzarella cheese.     

Isolation and characterization of proteins from soymilk residue (okara)

Protein was extracted from okara at pH 9.0 and 80 °C for 30 min, giving a recovery of 53% protein. The extracted protein was isolated by isoelectric precipitation at pH 4.5, and the dried, defatted protein isolates (prepared at 25 and 80 °C) had over 80% protein.

The okara protein isolates have essential amino acid profiles similar to the FAO scoring pattern, and high in vitro protein digestibility, with methionine and cysteine as the limiting amino acids. Polyacrylamide gel electrophoresis in sodium dodecyl sulfate showed that okara protein isolates had a large quantity of high molecular weight components suggesting protein aggregation. Differential scanning calorimetry and hydrophobicity data suggested extensive protein unfolding in the okara products.

Okara protein isolates had lower solubility than a commercial soy protein isolate at both acidic and alkaline pH, probably due to protein aggregation. Other functional properties, including emulsifying, water and fat binding, and foaming properties, were found to be comparable to the commercial soy isolate.     

Proximate composition and functional properties of African breadfruit kernel and flour blends

African breadfruit seeds (ABS) were toasted at 80 and 120°C for varied period of times. The effects of the toasting temperature and time on selected functional properties of the seed flours were determined. Flour blends were prepared from the toasted ABS and wheat flours. The chemical composition and functional properties of the blends were determined. Toasting increased the water absorption capacity (WAC) of ABS flours with increased toasting time at both toasting temperatures. The oil absorption capacity (OAC) on the other hand, increased up to 20 min of seed toasting at both 80 and 120°C and thereafter decreased. At both 80 and 120°C, the foaming capacity (FC) of the seeds decreased with increased toasting time, with greater decreased at 120°C. The protein, fat, ash and crude fibre contents of the flour blends increased while carbohydrate and moisture contents decreased with increased levels of toasted African breadfruit flour (TABF) in the blends. The TABF showed significantly higher (P<0.05) WAC, OAC, FC and emulsion activity (EA) than wheat flour (WF). These properties increased with increased amounts of TABF in the blends. All the flour blends exhibited a least gelation concentration of 8% (W/V). The bulk density (g/cm³) and wettability values of flour blends varied from 0.74 to 0.84 and 19 to 31, respectively. Heating increased the swelling capacity of the flour blends.     

Solubility and Foaming Properties of Phytate-Reduced Soy Protein Isolate

A pilot scale ion exchange process was developed to produce a 75 - 77% phytate-reduced soy protein isolate. The solubility and foaming properties of this isolate were compared to those of control and commercial soy protein isolates as a function of protein concentration (5 and 10%, w/v), pH (3, 6 and 9) and preheat temperature (25, 60 and 80°C). Phytate-reduced soy protein extract exhibited minimum solubility at pH 4.8 - 5.0, compared to 4.2 - 4.5 for control soy extract. Phytate-reduced soy protein isolate was most soluble and functional at pH values below its isoelectric point (pH 3), whereas control and commercial soy isolates were generally most soluble and functional at pH values above their isoelectric point (pH 6 and 9).     

Investigations of Soybean 11S Protein and Myosin Interaction by Solubility, Turbidity and Titration Studies

Solubility tests, turbidity tests, and titration experiments were employed to study the possible protein-protein interactions between purified soybean 11S protein and skeletal muscle myosin and the involvement of protein subunits in the interactions. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was used as an analytical tool for identification of the protein species. These tests indicate that these proteins interacted at temperatures between 85°C and 100°C. Solubility and titration experiments showed that acidic subunits of soybean US protein had little or no interaction with myosin heavy chain subunits. In contrast, soybean 11S basic subunits interacted with myosin heavy chains. The SDS-PAGE method indicated that eight commercial soy protein isolates had a similar protein species composition, but certain proteins in some isolates had lost their availability for water extraction. This may account for different functional properties exhibited by differen soy protein isolates.     

Rice Dreg Protein as an Alternative to Soy Protein Isolate: Comparison of Nutritional Properties

Rice dreg protein could be a valuable source of plant-based proteins, as an alternative to soy proteins in some food products. Here, nutritional properties of rice dreg protein were compared with those of soy protein isolate. The protein content of rice dreg protein was approximately 62.6 g/100 g sample, with large amounts of fat, carbohydrate, and ash. The denaturation temperatures of rice protein isolate from rice dreg protein were 47.4 and 97.2°C, respectively. This indicated that these proteins could be denatured during rice syrup processing to form aggregates, but were relatively more stable than rice endosperm protein and soy protein isolate. The main amino acids in rice dreg protein and rice protein isolate were Glu, Pro, Arg, Asp, and Leu, with Lys as the lowest content. Most of essential amino acids and nutritional parameters of rice protein isolate and rice dreg protein met the suggested nutritional requirements for a child according to FAO/WHO, and were relatively higher than those of soy protein isolate. In addition, rice protein isolate showed better digestibility than soy protein isolate during four hours sequential pepsin and pancreatin digestions. The final digestibility value was 96.66% for rice protein isolate compared to 91.41% for soy protein isolate. Thus rice dreg protein could potentially replace soy proteins as a good source of value-added protein for human nutrition in response to the increasing demand for plant proteins.     

Effects of Microwave and Ultrasound Assisted Extraction on the Recovery of Soy Proteins for Soy Allergen Detection

The extraction of soy proteins for soy allergen detections is conventionally achieved with PBS buffer for at least 2 h at room temperature or 4 °C. This method has been reported to be inefficient due to time consumption and inadequate protein extraction resulting in false negative allergen detection and mislabeling of foods containing allergenic proteins. This study investigated the application of microwave (MAE) and ultrasound assisted extraction (UAE) techniques to extract and improve recovery of allergens from various soy matrices. Soy proteins were extracted from raw soy flour, soy protein isolate (SPI) and soy milk using MAE at 60, 70, and 100 °C for 5 and 10 min and UAE at 4 and 23 °C for extraction times of 1, 5, and 10 min with PBS, Laemmli and urea buffers. Extracts were analyzed for total proteins, protein profile, and antibody‐based detection (ELISA) of soy proteins. Conventional extraction with each of the buffers was used as controls. Overall, proteins recovered from MAE and UAE samples were higher than recoveries from the controls in all soy matrices. Under all extraction conditions, Laemmli and urea buffer recovered more proteins than PBS. Electrophoresis analysis of protein showed bands around 75, 50, and 33 kDa indicating the presence of soy allergenic proteins β‐conglycinin and glycinin, in all samples. Using sandwich ELISA, control and UAE extracts resulted in high soy protein detection but this reduced in MAE extracts.     

THE FORMATION OF HEAT AND ENZYME INDUCED (PLASTEIN) GELS FROM PEPSIN-HYDROLYZED SOY PROTEIN ISOLATE1

A gel prepared by heating pepsin-hydrolyzed soy protein isolate (HSPI) had a higher turbidity and viscosity and less solubility than did its starting hydrolyzate. The gelling characteristics of the heated hydrolyzate were possibly due to hydrophobic interactions, as opposed to peptide bond reformation. The presence of pepsin was found to be necessary for gel formation at 37°C but could be successfully replaced by heat. Incubation of the concentrated HSPI at 95°C for 30 min was optimal for heat-induced gel formation. When soy protein isolate (SPI) was hydrolyzed with papain or bacterial protease, little gelation occurred (either by heat or enzyme induced gelation treatments).     

Amino acid profile,protein digestibility,thermal and functional properties of Conophor nut (Tetracarpidium conophorum) defatted flour,protein concentrate and isolates

Functional properties, amino acid compositions, in vitro protein digestibility, electrophoretic and thermal characteristics of conophor defatted flour (CDF), conophor protein concentrate (CPC), isoelectric protein isolate (CII) and neutral protein isolate (CNI) were evaluated. The isolates (CII and CNI) showed significantly lower (P < 0.05) water and oil absorption capacities, emulsifying and gelling capacities, but higher emulsion stability and foaming capacity. In vitro protein digestibility, enthalpy and denaturation temperature varied between 52.28% and 73.4%, 1.62–4.04 J g^?1 protein and 79.7–89.3 °C, respectively. The native proteins were comprised of subunits with molecular weights ranging between 15.3 and 129.3 kDa. The major amino acids in all the samples were aspartic acid, glutamic acid and arginine, whereas the percentages of essential amino acids in CDF, CPC, CII and CNI were 39.35%, 40.46%, 44.54% and 46.04%, respectively. Conophor protein products could be used as functional ingredients in food formulations and for enriching low quality protein diets.     

Nutrient-based Corn and Soy Products by Twin-screw Extrusion

Blends were developed to provide 20% protein, 12% fat, 68% carbohydrate and 8% moisture. High protein soy products (full fat flakes, protein isolate and/or concentrate) were formulated with corn meal and soybean oil to provide high protein and fat. The blends were extruded to provide pre-cooked foods that could be reconstituted at 40°C to a porridge or gruel, eliminating prolonged cooking or degradation of heat labile nutrients. Two types of soy isolate and concentrate were evaluated under extrusion temperatures from 100 to 130°C and feed moistures 8.5 to 18%. The extrusion of lower valued concentrates at 100 to 115°C with moisture from 12 to 18% produced a precooked mix that was high in nutrients and contained the most available lysine.     

Internal quality of coated eggs with soy protein isolate and montmorillonite: Effects of storage conditions

The development of the bio-nanocomposite coating materials for eggshells has received more attention because of the decline in interior egg quality. This work evaluated the effects of weight loss, Haugh unit, yolk index, air space and albumen pH, eggshell strength, number of microorganisms on eggshells, contact angle and water vapor permeability of uncoated eggs and eggs coated with soy protein isolate/montmorillonite emulsions (5/0, 5/0.20, 5/0.50, 5/0.80; w/w) during 6 weeks at 25°C. A scanning electron microscope was used to visualize morphologies of soy protein isolate and the soy protein isolate/montmorillonite composite coatings, and the scanning probe microscope was determined. Compared with uncoated and soy protein isolate-coated eggs, the interior egg quality was improved by the increase of Haugh unit, yolk index, air space or eggshell strength, and decrease in weight loss, albumen pH, or the number of microorganisms on eggshells. The higher contact angle indicated the hydrophobicity of coatings. The values of water vapor permeability with 0.2% montmorillonite, 0.5% montmorillonite, and 0.8% montmorillonite were reduced by 21.14, 57.78, and 69.13%, respectively, as compared to those of soy protein isolate coatings. The images by a scanning electron microscope indicated that coatings could cover the cracks of eggshells to preserve the interior egg quality. The experimental values of the scanning probe microscope showed that montmorillonite would not penetrate through the eggshell pores, and it was safe to coat with montmorillonite. This study highlights the use of soy protein isolate/montmorillonite coating to maintain the internal quality and enhance the shelf life of eggs stored at 25°C.     

Emulsifying Capacity and Emulsion Stability of Soy Proteins Compared with Corn Germ Protein Flour

Both emulsifying capacity (EC) and emulsion stability (ES) increased with increasing concentrations from 0.4% to 0.8% of soy flour (SF), soy concentrate (SC), soy isolate (SI) and corn germ protein flour (CGPF) when studied by response surface methodology. EC and ES increased as pH increased from 6 to 8 in all samples. Increasing incubation temperatures of protein solutions from 20–70°C or from 4–20°C did not affect EC or ES, respectively. SF had the highest EC, followd by SI, SC, and CGPF.     

Characteristics and Functionality Enhancement by Glycosylation of Bitter Melon (Momordica charantia) Seed Protein

Seeds of ripe bitter melon (Momordica charantia) contain approximately 30% protein. However, this protein, which is less functional than soy protein, may have desirable functionalities as a food ingredient after modification. Bitter melon seed protein isolate (BMSPI) was prepared under optimal extraction conditions (defatted meal to 1.3 M NaCl was 1:10 w/v; pH 9.0) and its functional properties were investigated before and after modification by glycosylation. Glycosylation was conducted at varying relative humidities (50%/65%/80%) and temperatures (40 °C/50 °C/60 °C) using a response surface central composite design. Degree of glycosylation (DG) ranged from 39.3 to 52.5%, 61.7 to 70.9%, and 81.2 to 94.8% at 40 °C, 50 °C, and 60 °C, respectively (P values < 0.0001). Denaturation temperatures of all DGs ranged from 111.6 °C to 114.6 °C, while unmodified/native BMSPI had a value of 113.2 °C. Surface hydrophobicity decreased to approximately 60% when the DG was maximal (94.8%). Solubility decreased almost 90% when the DG was maximal in comparison to the native BMSPI (62.0%). Emulsifying activity increased from 0.35 to 0.80 when the DGs were ≥80%, while emulsion stability increased from 63 to 72 min when the DGs were greater than 70%. A similar trend was observed with foaming capacity and foaming stability of the glycosylated proteins. This glycosylated BMSPI with improved emulsifying and foaming properties could be used as an ingredient in food products where such properties are required.     

Improvement of the Functionalities of Soy Protein Isolate through Chemical Phosphorylation

A method of chemical phosphorylation was developed to modify soy protein so as to improve its functional properties. The reaction was carried out by incubating soy protein isolate and cyclic sodium trimetaphosphate in an aqueous solution at pH 11.5 and 35°C for about 3 hours. The reactions ensued were the phosphoesterification of serine residues and the phosphoramidation of lysine residues in soy protein. The phosphorylated soy protein isolate prepared there-from exhibited much improved functional properties in terms of aqueous solubility, water-holding capacity, emulsifiability and whippability. The nutritive bioavailability of soy protein isolate was not impaired by phosphorylation.