Physico-Chemical Properties of the Flour, Protein Concentrate, and Protein Isolate of the Cupuassu (Theobroma grandiflorum Schum) Seed

ABSTRACT:  Defatted flour, protein concentrate, and protein isolate obtained from Amazonian cupuassu seeds were evaluated for their solubility properties, water and oil retention capacity, foam formation and stability, gelling properties, emulsifying ability, and emulsion stability. The protein contents of defatted flour, the concentrate, and the isolate were 27.65%, 31.18%, and 64.29%, respectively. As expected, the protein isolate exhibited higher solubility than the protein concentrate, achieving more than 90% solubility at pH 8.0. The flour and the protein concentrate, however, showed excellent water and oil retention capacities. High emulsifying capacity at pH 7.0 was also observed for all 3 products: 987 mL oil/g, 977 mL oil/g, and 1380 mL oil/g for the flour, protein concentrate, and protein isolate, respectively. Gelling properties were not exhibited by any of the products, but all of them exhibited good utilization potential, not only to enrich other foods but also to enhance relevant functional properties.     

Structural and Functional Properties of Hemp Seed Protein Products

The effects of pH and protein concentration on some structural and functional properties of hemp seed protein isolate (HPI, 84.15% protein content) and defatted hemp seed protein meal (HPM, 44.32% protein content) were determined. The HPI had minimum protein solubility (PS) at pH 4.0, which increased as pH was decreased or increased. In contrast, the HPM had minimum PS at pH 3.0, which increased at higher pH values. Gel electrophoresis showed that some of the high molecular weight proteins (>45 kDa) present in HPM were not well extracted by the alkali and were absent or present in low ratio in the HPI polypeptide profile. The amino acid composition showed that the isolation process increased the Arg/Lys ratio of HPI (5.52%) when compared to HPM (3.35%). Intrinsic fluorescence and circular dichroism data indicate that the HPI proteins had a well‐defined structure at pH 3.0, which was lost as pH value increased. The differences in structural conformation of HPI at different pH values were reflected as better foaming capacity at pH 3.0 when compared to pH 5.0, 7.0, and 9.0. At 10 and 25 mg/mL protein concentrations, emulsions formed by the HPM had smaller oil droplet sizes (higher quality), when compared to the HPI‐formed emulsions. In contrast at 50 mg/mL protein concentration, the HPI‐formed emulsions had smaller oil droplet sizes (except at pH 3.0). We conclude that the functional properties of hemp seed protein products are dependent on structural conformations as well as protein concentration and pH.     

Physicochemical and functional properties of full‐fat and defatted Moringa oleifera kernel flour

Full‐fat and defatted Moringa oleifera kernel flours were analysed for their functional properties. The effect of pH and NaCl concentrations on the functional properties of the flours was investigated following standard procedures. The protein content of full‐fat and defatted flour was 36.18 and 62.76 g/100 g, respectively. The concentrations of other proximate constituents of the defatted flour were higher than those of the full‐fat flour. Nitrogen solubility was lowest at pH of 4.0 and 9.0, respectively, with maximum solubility occurring at pH of 6.0. Defatting increased the water absorption and fat absorption capacities of Moringa oleifera kernel flour. The foaming capacity and foam stability of the defatted flour were 86.0% and 82.0 mL, whereas that of full‐fat flour were 20.6% and 18.5 mL respectively. The defatted flour showed better emulsification (97.2 mL g^?1) than full‐fat flour (66.0 mL g^?1). The least gelation concentration of the defatted and full‐fat flours was 14% and 16% (w/v) respectively. Moringa oleifera kernel flour can be a valuable source of vegetable protein in fortified food products formulation.     

Functionality of Flours, Protein Fractions and Isolates from Field Peas and Faba Bean

Field pca and faba bean proteins are rich sources of lysine, and air classification of the pin milled flours essentially doubled the protein contents in the protein fractions. The proteins in these flours and protein fractions were highly soluble at acid pH and exhibited only a narrow range of insolubility at pH 4–5. Water holding and oil absorption capacities increased in proportion to protein contents of the flour, protein fraction, and isolate of each legume, including soybean flour and isolate, but oil emulsification properties were uniformly high among all products. The protein fractions exhibited excellent whipp-ability and foam stability compared to soybean controls, and their promising functional properties suggested potential applications in meat emulsions, beverages and bakery products.     

Influence of enzymatic hydrolysis,pH and storage temperature on the emulsifying properties of canola protein isolate and hydrolysates

The aim of this work was to enhance emulsification properties of canola proteins through enzymatic proteolysis and pH variaton. Canola protein isolate (CPI) and hydrolysates (CPHs) were used to form emulsions at pH 4.0, 7.0 and 9.0 followed by storage at 4 or 25 °C for 7 days. Controlled enzymatic hydrolysis led to increased peptide bond cleavage with time (0.23 g/100 g in CPI to 7.18 g/100 g after 24‐h Alcalase hydrolysis). Generally, oil droplet sizes were smaller for emulsions made at pH 9.0, which suggest better quality than those made at pH 4.0 and 7.0. Trypsin hydrolysate emulsions were the most physically stable at pH 7.0 and 9.0; in contrast, the pepsin hydrolysate emulsions were unstable at all conditions. The results suggest that selective enzymatic hydrolysis could play an important role in enhancing successful incorporation of canola proteins and peptides into food systems as protein emulsifiers.     

Chickpea protein isolates obtained by wet extraction as emulsifying agents

BACKGROUND: Wet extraction of protein from defatted chickpea (variety Thiva (T), Greece) flour, at alkaline or slightly acidic pH, followed by isoelectric precipitation (pI) or ultrafiltration (UF) to recover the protein, was employed to obtain a number of chickpea protein isolates, enriched either in protein constituents belonging to the globulin (TpI, TUF, TUFG) or to the albumin fraction (TUFA). RESULTS: The interfacial activity and film‐forming ability of the isolate protein constituents as well as their emulsifying properties were evaluated. The method applied for chickpea protein isolate preparation influenced to an appreciable extent their composition, adsorption behaviour to oil–water interfaces and emulsion formation and stabilization characteristics, especially with respect to oil droplet flocculation and coalescence. The isolates also differed in their ability to stabilize emulsions subjected to thermal processing or following storage under freezing conditions. The results are discussed in terms of compositional and, possibly, structural differences existing between the protein constituents of the chickpea isolates that may influence their functional behaviour in emulsion systems. CONCLUSION: The method applied for isolate preparation influenced to an appreciable extent the ability of proteins to adsorb to the oil–water interface and stabilize emulsions during long‐time ageing or following heat treatment or freezing. Copyright © 2009 Society of Chemical Industry     

Effect of high-pressure treatment on rheology of oil-in-water emulsions prepared with hen egg yolk

This study evaluated the potentiality of high-pressure treatment to stabilise microbiologically emulsions made with yolk without causing destabilisation and gelation. The effects of two levels of treatment (200 or 500 MPa) on the properties (oil droplet size, interfacial protein concentration and composition), the rheology, and the microbiology of yolk emulsions prepared at two pH values (3.0 and 7.0) were determined. Our results showed that, oil droplet size, interfacial protein concentration and composition were not altered by the high-pressure treatments. The rheological study demonstrated that high-pressure treatment induced a significant increase of viscosity in emulsions prepared at pH 7.0, whereas no obvious thickening was noticed in emulsions prepared at pH 3.0. Furthermore, as the protein concentration increased, the effect of high-pressure was more pronounced. Microbial analysis revealed that high-pressure treatment allowed an efficient reduction of the microbial charge of emulsions and that this effect was better at acidic pH than at neutral pH. Consequently, high-pressure treatment could be used to stabilise yolk emulsions in acidic conditions.     

Bayberry (Myrica rubra Sieb. et Zucc.) kernel: A new protein source

Bayberry (Myrica rubra Sieb. et Zucc.) kernel protein isolate (BKPI) was isolated from bayberry kernel defatted flour (BKDF) by isoelectric precipitation. BKPI was evaluated for chemical composition and selected functional properties with defatted kernel flour as reference. BKPI contained over 90% dry weight (DW) of protein versus 60.5% DW of protein in BKDF. It possessed a well-balanced amino acid composition according to the FAO/WHO reference except for a low content of lysine. BKPI had a solubility profile similar to that of BKDF, with minimum solubility observed at pH 4.0 and maximum solubility at pH 12.0. BKPI exhibited minimum foaming capacity (FC) (31.1%) and maximum foaming stability (FS) (72.7%) at pH 4.0. Minimum emulsifying capacity (EC) and emulsifying stability (ES) of BKPI and BKDF were observed at pH 4.0. BKPI had a least gelation concentration of (LGC) of 6% (w/v) at pH 4.0. Results indicated that bayberry kernel has potential to be exploited as a new protein source in China.     

Interfacial composition and stability of emulsions made with mixtures of commercial sodium caseinate and whey protein concentrate

The interfacial composition and the stability of oil-in-water emulsion droplets (30% soya oil, pH 7.0) made with mixtures of sodium caseinate and whey protein concentrate (WPC) (1:1 by protein weight) at various total protein concentrations were examined. The average volume-surface diameter (d₃₂) and the total surface protein concentration of emulsion droplets were similar to those of emulsions made with both sodium caseinate alone and WPC alone. Whey proteins were adsorbed in preference to caseins at low protein concentrations (<3%), whereas caseins were adsorbed in preference to whey proteins at high protein concentrations. The creaming stability of the emulsions decreased markedly as the total protein concentration of the system was increased above 2% (sodium caseinate >1%). This was attributed to depletion flocculation caused by the sodium caseinate in these emulsions. Whey proteins did not retard this instability in the emulsions made with mixtures of sodium caseinate and WPC.     

Chemical, Functional, and Nutritional Properties of Egusi (Colocynthis citrullus L.) Seed Protein Products

Egusi (Colocynthis citrullus L.) kernels contain 52.0% oil, 28.4% protein (60% in defatted flour), 2.7% fiber, 3.6% ash, and 8.2% carbohydrate. They are good sources of essential amino acids, especially arginine, tryptophan and methionine, vitamins B₁, B₂, and niacin, and S, Ca, Mg, Mn, K, P, Fe, and Zn. The oil contains mostly oleic (15.9%) and linoleic (62.8%) acids. Protein isolates that differ in gel electrophoretic patterns and amino acid content can be prepared from the flour in one- or two-step water and sodium hydroxide extractions. The water and oil holding capacities of the flour are 0.7 and 2.6 ml/g, respectively. Thick (mayonnaise-type) emulsions form in the alkaline pH range and a stable foam forms at pH 5.0. Nutritionally, lysine is the most limiting amino acid (chemical score, 52.4).     

Heat Stability of Oil-in-Water Emulsions Containing Milk Proteins: Effect of Ionic Strength and pH

Emulsions (20 wt% soybean oil; 2 wt% protein) made with caseinate at pH 7 and with whey protein isolate (WPI) at pH 7 and 3 were stable to heating at 90 and 121°C. WPI emulsions destabilized at pH values between 3.5 and 4.0. In the presence of KCI (12.5–200 mM), large particles were formed in WPI emulsions at pH 3 and the emulsions were viscous. At pH 7, moderate concentrations of KCI decreased the heat stability and gels were formed. KCI had less effect on WPI emulsions made at pH 3. Combining the emulsions with caseinate allowed some control of the heat-induced gelation.     

THERMAL BEHAVIOR, SOLUBILITY AND STRUCTURAL PROPERTIES OF SOY CONCENTRATE HYDROLYZED BY NEW PLANT PROTEASES

A soy concentrate prepared by alcoholic extraction of defatted soy flour was hydrolyzed with three plant proteases: hieronymin and macrodontin, cysteine proteases, and pomiferin, a serine protease. A commercial microbial protease (alcalase) was included for comparative purposes. Working at optimal conditions for each enzyme, 5–15% degree of hydrolysis (DH) values were obtained. Hydrolysates exhibited a characteristic SDS-PAGE pattern: the plant proteases attacked the polypeptides of 7S and 11S proteins with different intensity and selectivity, especially the A and B polypeptides of the 11S protein. Intermediate molecular weight peptides (24 and 60 kDa) were produced as the hydrolysis progressed. Differential Scanning Calorimetry (DSC) thermograms of flour. concentrate and hydrolysates were analyzed to evaluate the thermal stability and denaturation enthalpies of the major proteins. An increase in the degree of protein denaturation resulting from enzymatic action and a lower thermal stability at low pH were detected. The surface hydrophobicity of all hydrolysates, unlike expected, did not increase. Solubility at pH 7.0 is closely related to the DH, independent of the protease used. Solubility at pH 4.5 appeared to be related to the extent of hydrolysis of polypeptide A by each protease.     

Some Functional and Utilization Characteristics of Sesame Flour and Proteins

Sesame defatted flour was prepared from dehulled seeds and the proteins extracted by isoelectric precipitation from an alkaline suspension of the flour. Temperature and pH effects on viscosity of a protein dispersion were measured using a Brookfield viscometer. Emulsifying capacity and emulsion stability were measured in mayonnaise and meat-type emulsions, respectively. Sesame flour was texturized by a simple method to produce a ground meat-like product with a hydration capacity of 380–440%. Sensory evaluation of meat loaves with 0–40% meat replaced by hydrated textured defatted sesame flour indicated no significant difference between samples. Viscosity of sesame protein dispersions at 90°C increased with increasing pH. The proteins did not form a self-supporting gel. Their emulsifying capacity proved to be relatively high when compared with traditional proteins.     

Peanut protein concentrate: Production and functional properties as affected by processing

Peanut protein concentrate (PPC) was isolated from fermented and unfermented defatted peanut flour by isoelectric precipitation and physical separation procedures. PPC was dried by spray or vacuum drying. PPC powders from each drying technique were evaluated for proximate composition and functional properties (protein solubility, water/oil binding capacity, emulsifying capacity, foaming capacity and viscosity) along with defatted peanut flour and soy protein isolate as references. PPC contained over 85% protein versus 50% protein in the defatted peanut flour used as raw material for PPC production. PPC had a solubility profile similar to that of peanut flour, with minimum solubility observed at pH 3.5–4.5 and maximum solubility at pH 10 and higher. Roasting of peanut reduced all functional properties of defatted peanut flour while fermentation had the reverse effect. The type of drying significantly affected the functional properties of PPC. Spray dried PPCs exhibited better functional properties, particularly emulsifying capacity and foaming capacity, than vacuum oven dried PPC. Spray dried PPCs also showed comparable oil binding and foaming capacity to commercially available soy protein isolate (SPC). At equivalent concentrations and room temperature, PPC suspension exhibited lower viscosity than soy protein isolate (SPI) suspensions. However, upon heating to 90 °C for 30 min, the viscosity of PPC suspension increased sharply. Results obtained from this study suggest that the PPC could be used in food formulations requiring high emulsifying capacity, but would not be suitable for applications requiring high water retention and foaming capacity. PPC could be a good source of protein fortification for a variety of food products for protein deficient consumers in developing countries as well as a functional ingredient for the peanut industry. The production of PPC could also add value to defatted peanut flour, a low value by-product of peanut oil production.     

Functional properties of protein fractions obtained from commercial yellow field pea (Pisum sativum L.) seed protein isolate

Commercial pea protein isolate was separated into water-soluble (WS), salt-soluble (SS), alkaline-soluble (AS) and ethanol-soluble (ES) fractions. AS fraction was the most abundant, constituting about 87% of the proteins in PPI followed by WS, SS and ES fractions in decreasing order. ES fraction consistently formed emulsions with a narrow range of smaller oil droplet sizes (0.6–19 μm) at pH 4.0, 7.0 or 9.0 compared to a wider range of sizes for emulsions stabilised by WS, SS and AS fractions. Emulsions formed with ES fraction were also the most stable (p < 0.05) over the 3 h test period at all the pH values used in this work. The WS fraction had significantly highest (p < 0.05) protein solubility and foaming capacity at all the pH values when compared to solubility of PPI, SS, and ES. Except for AS and ES fractions, foaming capacities of the protein fractions were higher at pH 9.0 than at pH 4.0 or 7.0.     

Emulsifying properties of sweet potato protein: Effect of protein concentration and oil volume fraction

The effect of protein concentrations (0.1, 0.25, 0.5, 1.0, 1.5 and 2.0% w/v) and oil volume fractions (5, 15, 25, 35 and 45% v/v) on properties of stabilized emulsions of sweet potato proteins (SPPs) were investigated by use of the emulsifying activity index (EAI), emulsifying stability index (ESI), droplet size, rheological properties, interfacial properties and optical microscopy measurements at neutral pH. The protein concentration or oil volume fraction significantly affected droplet size, interfacial protein concentration, emulsion apparent viscosity, EAI and ESI. Increasing of protein concentration greatly decreased droplet size, EAI and apparent viscosity of SPP emulsions; however, there was a pronounced increase in ESI and interfacial protein concentration (P < 0.05). In contrast, increasing of oil volume fraction greatly increased droplet size, EAI and emulsion apparent viscosity of SPP emulsions, but decreased ESI and interfacial protein concentration significantly (P < 0.05). The rheological curve suggested that SPP emulsions were shear-thinning non-Newtonian fluids. Optical microscopy clearly demonstrated that droplet aggregates were formed at a lower protein concentration of <0.5% (w/v) due to low interfacial protein concentration, while at higher oil volume fractions of >25% (v/v) there was obvious coalescence. In addition, the main components of adsorbed SPP at the oil–water interface were Sporamin A, Sporamin B and some high-molecular-weight aggregates formed by disulfide linkage.     

Study of emulsions and foams stabilized with Phaseolus vulgaris or Phaseolus coccineus with the addition of xanthan gum or NaCl

The properties of oil/water emulsions stabilized with 1% w/v common bean (Phaseolus vulgaris L.) or scarlet runner bean (P. coccineus L.) proteins, extracted by isoelectric precipitation or ultrafiltration, at pH 7.0 and 5.5 were studied. The stability of emulsions, evaluated on the basis of droplet size, creaming, viscosity and protein adsorption measurements, is increased by the addition of xanthan (0.1 and 0.25% w/v). This is probably due to the increase in the continuous phase viscosity and the creation of a network, which prevents the oil droplets from coalescing. Also, the ability and stability of 1 or 2% w/v foams was studied. Xanthan (0.25% w/v) does not enhance foam formation, but promotes foam stability, possibly owing to the increased viscosity of the aqueous phase, making it more difficult for air to enter the system and create a satisfactory foam volume. The addition of NaCl destabilizes emulsions by lowering the energy barrier and therefore increasing the tendency of the oil droplets to aggregate. However, NaCl at a certain concentration seems to promote the emulsion stability and foaming ability and foam stability. This could be attributed to the alteration of the protein molecule configuration leading to the building of a rigid and viscoelastic protein film around the droplet. Copyright © 2006 Society of Chemical Industry     

食品蛋白新资源——元宝枫蛋白

对元宝枫种子蛋白质的含量、化学组成和其主要功能特性的研究表明:元宝枫种仁的蛋白质含量为27.15%,仅次于大豆。元宝枫蛋白含有人体必需的8种氨基酸,为完全蛋白。其蛋白的等电点为4.38;在等电点附近,种仁脱脂粉的溶解度、起泡性、泡沫稳定性最低,而当pH 6～7时,表现较佳。与大豆脱脂粉相比,元宝枫种仁脱脂粉具有更好的吸油性,种仁蛋白具有更好的起泡性。     

SOLUBILIZATION AND FUNCTIONAL PROPERTIES OF MOTH BEAN (VIGNA ACONITIFOLIA (Jacq.) Marechal AND HORSE GRAM (MACROTYLOMA UNIFLORUM (Lam.) Verdc. PROTEINS

Horse gram and moth bean seeds contained 23.6% and 21.9% protein (N x 6.25), respectively. Both the legumes are rich sources of iron. The iron contents in horse gram and moth beans were 11.0 and 9.6 mg/100 g, respectively. NaCl at 10% (w/v) and Na₂CO₃ at 0.5% (w/v) were found to be effective in extracting 89% and 80% of moth bean and horse gram proteins from defatted flour The minimum solubility of horse gram proteins from defatted flour was at pH 4.0 whereas proteins from moth bean exhibited minimum solubility at pH 4.5. The water and oil absorption, and foaming capacities in case of horse gram and moth bean flours were 2.0 g/g and 2.2 g/g, 23.0% and 2.0 g/g, 1.6 g/g, 27.6%, respectively.     

Impact of a thermal treatment on the emulsifying properties of egg yolk. Part 2: Effect of the environmental conditions

The protein solubility and emulsifying properties of native and heat-treated egg yolk (EY) suspensions were investigated in various environmental conditions. Four distinct conditions were tested by combining two levels of pH, namely pH 4.0 and 6.5, and two levels of ionic strength, namely 0.15 and 0.52 M NaCl, in a model oil-in-water (O/W) emulsion containing 30% oil (v/v). Although the protein solubility was greatly reduced by the thermal denaturation in all tested environmental conditions, the average size of oil droplets obtained in emulsions made with heated EY was observed to be either similar or slightly smaller than that obtained with native EY, depending on the environmental conditions. Using heat-treated EY rather than native EY led to a significant increase of the interfacial protein concentration in all environmental conditions. This increased interfacial protein concentration was shown to have a major impact on the flocculation behaviour of the emulsions, as well as on their rheological properties and stability to creaming. Hypotheses regarding the mechanisms by which insoluble protein aggregates stabilise O/W emulsions at various pH and ionic strengths are discussed.