Partially hydrolyzed rapeseed protein isolates with improved functional properties

Limited rapeseed protein hydrolysates ranging from 3.1 to 7.7% hydrolysis were produced from isoelectric-precipitated protein isolate. Water absorption, oil absorption, whippability, foam capacity and stability, emulsifying activity, and emulsion stability of the hydrolysates were determined. All protein hydrolysates showed better functional properties than the original protein isolate. Foam and emulsion stability decreased as the degree of hydrolysis increased. The hydrolysate with the lowest degree of hydrolysis showed the best functional properties. These improved functional properties make rapeseed protein hydrolysates a useful product to be used in foods such as breads, cakes, ice creams, meat products, desserts, and salad dressings.     

Functional properties of pea (Pisum sativum, L.) protein isolates modified with chymosin

In this paper, the effects of limited hydrolysis on functional properties, as well as on protein composition of laboratory-prepared pea protein isolates, were investigated. Pea protein isolates were hydrolyzed for either 15, 30 and 60 min with recombined chymosin (Maxiren). The effect of enzymatic action on solubility, emulsifying and foaming properties at different pH values (3.0; 5.0; 7.0 and 8.0) was monitored. Chymosin can be a very useful agent for improvement of functional properties of isolates. Action of this enzyme caused a low degree of hydrolysis (3.9-4.7%), but improved significantly functional properties of pea protein isolates (PPI), especially at lower pH values (3.0-5.0). At these pH values all hydrolysates had better solubility, emulsifying activity and foaming stability, while longer-treated samples (60 min) formed more stable emulsions at higher pH values (7.0, 8.0) than initial isolates. Also, regardless of pH value, all hydrolysates showed improved foaming ability. A moderate positive correlation between solubility and emulsifying activity index (EAI) (0.74) and negative correlation between solubility and foam stability (-0.60) as well as between foam stability (FS) and EAI (-0.77) were observed. Detected enhancement in functional properties was a result of partial hydrolysis of insoluble protein complexes.     

Enzymatic modification of sesame seed protein,sourced from waste resource for nutraceutical application

The functional characteristics which include protein solubility at different pH, emulsifying and foaming properties, degree of hydrolysis, molecular weight distribution, antioxidant and ACE inhibitory activity of sesame protein hydrolysates prepared with pepsin, papain and alcalase enzymes were evaluated. The rate of degree of hydrolysis was found to reach maximum (25–30%) within the first time fragment i.e 10 min but 80% of hydrolysis was obtained in 120 min with alcalase. SDS-PAGE of hydrolysates with papain, pepsin and alcalase evinced bands of low molecular weight protein of 14.3 kDa and even lower for alcalase treatment of 120 min. Hydrolysates so formed were of improved functional properties as evident from emulsifying and foaming property. Hydrolysis with different proteases enhanced the protein solubility significantly at pH 7.0. Antioxidative assay revealed radical scavenging activity of the hydrolysates with papain hydrolysates showing maximum antioxidative efficacy. The ultra-filtered peptide fractions which showed comparable ACE inhibitory activity were sequenced by MALDI-TOF and matched to that of previously identified ACE inhibitory peptides. The results corroborate the ACE inhibitory effect of the peptides. Hence, these highly bioactive protein hydrolysates produced from waste sesame meals can be successfully employed in various functional food formulations.     

Extraction,Composition and Functional Properties of Pennycress (Thlaspi arvense L.) Press Cake Protein

This study compared two methods for extracting the protein in pennycress (Thlaspi arvense L.) press cake and determined the composition and functional properties of the protein products. Proteins in pennycress press cake were extracted by using the conventional alkali‐solubilization–acid‐precipitation (AP) method or saline‐based (SE) procedure (0.1 M NaCl at 50 °C). The extraction method has a major influence on the purity and functional properties of press cake protein products. AP had a lower protein yield (23 %) but much higher purity (90 % crude protein) compared with SE (45 % yield, 67 % crude protein). AP protein isolate had high foam capacity (120 ml), high foam stability (96 % foam volume retention) and high emulsion stability (24–35 min), and it was resistant to heat denaturation (3 % loss of solubility at pH 2 and pH 10). On the other hand, SE protein concentrate showed remarkably high solubility (>76 %) between pH 2 and 10 and exceptional emulsifying activity (226–412 m²/g protein), but was more susceptible to heat denaturation at pH 7 and pH 10 (65–78 % loss of solubility). These results strongly demonstrate that higher purity pennycress press cake protein can be produced by either saline extraction or acid precipitation and have functional properties that are desirable for non‐food uses.     

Functional properties of a protein product from Caryodendron orinocense (Barinas nut)

The functional properties of Caryodendron orinocense protein product were investigated and compared with those of soybean (Glycina maxima). The product protein content was 24.47 g/100 g (Nx6.25). Solubility increased at both sides of the isoelectric point (pH 4.0) and with increased NaCl concentration up to 0.5M. Compared with soybean flour (50% protein), the protein product exhibited higher water and oil absorption, but lower emulsifying activity, emulsion stability, foaming capacity, and foam stability, the last one increase at higher pH. Emulsifying activity, foaming capacity, and foam stability were ionic strength dependent. C. orinocense protein product increased its emulsifying activity steadily from 0.05M to 0.75M NaCl, while it remained almost constant for soybean flour. Foaming capacity increased drastically at pH 10. The minimum time and concentration to form a gel was 20% in 4 min and 10% in 8 min for the Caryodendron protein product and soybean flour, respectively. The bulk density was 0.5056+/-0.0041 g/mL.     

Sesame cake protein hydrolysis by alcalase: Effects of process parameters on hydrolysis, solubilisation, and enzyme inactivation

We investigated the effects of process parameters (substrate concentration, enzyme concentration, temperature and pH) on the hydrolysis and solubilization of sesame cake protein as well as enzyme stability. The sesame cake protein was hydrolyzed by Alcalase enzyme (a bacterial protease produced by a selected strain of Bacillus Licheniformis) that was chosen among five commercial enzymes examined. The optimum process conditions for hydrolysis and solubilization were obtained as 15 g L^?1 substrate concentration, 3 ml L^?1 enzyme concentration, 50 °C and pH 8.5. Under these conditions, the values of degree of hydrolysis and solubilization were found as 26.3% and 82.1%, respectively, and enzyme lost its activity by approx. 56% at the end of 120 min processing time. Modeling studies were performed to determine the kinetics of hydrolysis, solubilization and enzyme inactivation. The relationship between hydrolysis and solubilization was found linear for all experimental conditions examined. The inactivation energy of Alcalase at the temperature range of 45–55 °C was determined to be 25544 J mol^?1.     

Functional and nutritional properties of modified proteins of sesame (Sesamum indicum, L.)

A study on the functional and nutritional properties of sesame (Sesamum indicum, L.) flour, concentrate and enzymatic hydrolysates, demonstrated that nitrogen solubility of the hydrolysates is improved, in water (85%) and at different pHs (91-95%), by the action of neutrasa 0.5L and alcalasa 0.6L, yielding a product with good emulsifying and improved foaming properties. Hydrolysates produced by the pH-stat method, then freeze-dried and spray-dried presented a PER of 1.1 and 0.9, respectively. The flour and the concentrate had PER values of 1.2. Supplementation of one of the hydrolysates with soya hydrolysate (1:1), improved the PER to a value similar to that of casein. Use of neutrasa 0.5L and alcalasa 0.6L enzymes, enhances the sesame protein solubility without modifying extensively the PER. Besides, it yields a dehydrated product with improved emulsifying and foaming properties.     

Preparation of fish protein isolate and hydrolyzate (Mugil cephalus) and their incorporation into Mexican foods

Fish protein isolates (FPI) and hydrolyzates (FPH) were obtained from mullet (Mugil cephalus) through alkali solubilization and HCl precipitation for FPI, as well as enzymatic hydrolysis for FPH. The powdered products showed solubilities of 50 and 89%, and emulsifying capacities of 36 and 39 ml oil/100 mg for FPI and FPH, respectively, with protein contents of 90% and oil contents lower than 1.6%. Both products were used to enrich cereals and legumes in order to increase their protein content and quality. The resulting mixtures were used to prepare common Mexican dishes. When up to 20 and 35% of the total protein was provided by FPI and FPH, respectively, the dishes were well accepted by 70% of the panel.     

Functional Food Ingredients Based on Sunflower Protein Concentrates Naturally Enriched with Antioxidant Phenolic Compounds

The functional properties of three sunflower protein concentrates having different content of phenolic compounds (mainly chlorogenic and caffeic acids) obtained from sunflower oil cake, a by-product of the oil industry, were evaluated. Sunflower protein concentrates exhibited high water solubility and moderate water-imbibing and water-holding capacities. It was possible to obtain foams and emulsions of different stability at different pH and ionic strength from these protein concentrates, as well as self-supporting gels produced by thermal induction. The presence of phenolic compounds not only conferred antioxidant activity and changed the color of protein products, but also reduced the water imbibing capacity of sunflower protein concentrates, the stability of the emulsions obtained, and the hardness of protein gels. In contrast, phenolic compounds did not modify the water holding capacity, their water solubility or their foaming properties. These results suggest that these protein products may be used as functional ingredients in the food industry.     

Toxic Compound, Anti-Nutritional Factors and Functional Properties of Protein Isolated from Detoxified Jatropha curcas Seed Cake

Jatropha curcas is a multipurpose tree, which has potential as an alternative source for biodiesel. All of its parts can also be used for human food, animal feed, fertilizer, fuel and traditional medicine. J. curcas seed cake is a low-value by-product obtained from biodiesel production. The seed cake, however, has a high amount of protein, with the presence of a main toxic compound: phorbol esters as well as anti-nutritional factors: trypsin inhibitors, phytic acid, lectin and saponin. The objective of this work was to detoxify J. curcas seed cake and study the toxin, anti-nutritional factors and also functional properties of the protein isolated from the detoxified seed cake. The yield of protein isolate was approximately 70.9%. The protein isolate was obtained without a detectable level of phorbol esters. The solubility of the protein isolate was maximal at pH 12.0 and minimal at pH 4.0. The water and oil binding capacities of the protein isolate were 1.76 g water/g protein and 1.07 mL oil/g protein, respectively. The foam capacity and stability, including emulsion activity and stability of protein isolate, had higher values in a range of basic pHs, while foam and emulsion stabilities decreased with increasing time. The results suggest that the detoxified J. curcas seed cake has potential to be exploited as a novel source of functional protein for food applications.     

Enzymatic hydrolysis of extruded-expelled soy flour and resulting functional properties

Limited hydrolysis (4% degree of hydrolysis) of extruded-expelled soy flour protein (protein dispersibility index=21) that was poor in solubility and other functional properties was evaluated at pilot-plant scale (5 kg of flour) with two endopeptidases and one exopeptidase. Some hydrolysates were merely spray-dried whereas others were jet-cooked at 104°C for 19 s before spray-drying. Solubility, emulsification capacity and stability, foaming capacity and stability, apparent viscosity, and sensory attributes were then characterized. The type of protease used and hydrothermal cooking affected functional and sensory properties. Protein solubility modestly increased with hydrolysis and jet cooking, but emulsification capacity decreased on hydrolysis and was not restored with hydrothermal cooking. Emulsion stability improved in the endopeptidase hydrolysates, but not in the exopeptidase hydrolysates. The foaming capacities of the hydrolysates for both types of enzymes were better than for the unhydrolyzed control. Highly stable foams were obtained after hydrolyzing with exopeptidase and hydrothermal cooking. Ten percent protein hydrolysate dispersions showed large losses in consistency coefficient apparent viscosity, which increased significantly with hydrothermal cooking only for the unhydrolyzed control. Difference-from-control sensory evaluation indicated that both jet-cooked and non-jet-cooked enzyme hydrolysates were different from unhydrolyzed controls.     

Enzymatic modification of proteins of commercial sesame meals (Sesamum indicum, L.)

Sesame (Sesamum indicum, L.) is one of the most important oilseed crops in Venezuela. However, the low solubility of the flour made of commercial meals does not allow its use in the preparation of fluid foods. To solve this situation, the alternative of solubilizing the sesame proteins by an enzymatic method, using commercial proteases, was studied. Hydrolysis was carried out with two types of bacterial proteases: neutrasa 0.5L, and alcalase 0.6L. Basically, the process consisted of milling and sieving the sesame cake (60 mesh), concentrating the proteins by solubilizing them at a pH of 9.5, and then precipitating at a pH of 4.5. Proteins were hydrolyzed by an enzymatic method, and the hydrolysates freeze-dried and spray-dried. Optimal conditions of hydrolysis using neutrase 0.5L at a pH of 7 were: 6% substrate concentration, 3% enzyme:substrate ratio, temperature 50 degrees +/- 1 degree C, and hydrolysis degree of 8%. When alcalase 0.6L was used at a pH of 8, optimal conditions were: 8% substrate concentration, 2.3% enzyme:substrate ratio, temperature 58 degrees +/- 1 degree C, and hydrolysis degree of 10%. The enzyme affinity (Km) was best at temperatures near the optimal temperature for the hydrolysates. Dried hydrolysates had protein values which ranged between 66.3% and 66.9% and a nitrogen solubility in water, of approximately 85%. Hydrolysis yields referred to the concentrate dried mass were 42% for the atomized hydrolysate, and 56% for the freeze-dried one. In conclusion, the enzymatic hydrolysis process improved the nitrogen solubility in water of the sesame proteins.     

Toxic Compound,Anti-Nutritional Factors and Functional Properties of Protein Isolated from Detoxified Jatropha curcas Seed Cake

Jatropha curcas is a multipurpose tree, which has potential as an alternative source for biodiesel. All of its parts can also be used for human food, animal feed, fertilizer, fuel and traditional medicine. J. curcas seed cake is a low-value by-product obtained from biodiesel production. The seed cake, however, has a high amount of protein, with the presence of a main toxic compound: phorbol esters as well as anti-nutritional factors: trypsin inhibitors, phytic acid, lectin and saponin. The objective of this work was to detoxify J. curcas seed cake and study the toxin, anti-nutritional factors and also functional properties of the protein isolated from the detoxified seed cake. The yield of protein isolate was approximately 70.9%. The protein isolate was obtained without a detectable level of phorbol esters. The solubility of the protein isolate was maximal at pH 12.0 and minimal at pH 4.0. The water and oil binding capacities of the protein isolate were 1.76 g water/g protein and 1.07 mL oil/g protein, respectively. The foam capacity and stability, including emulsion activity and stability of protein isolate, had higher values in a range of basic pHs, while foam and emulsion stabilities decreased with increasing time. The results suggest that the detoxified J. curcas seed cake has potential to be exploited as a novel source of functional protein for food applications.     

Hydrophobicity, solubility, and emulsifying properties of soy protein peptides prepared by papain modification and ultrafiltration

Peptide size control is important for obtaining desirable functional properties so that these peptides can be better utilized. Proteolytic enzymatic modification of soy protein isolates (SPI), followed by ultrafiltration, is an effective way to fractionate these proteins into peptides with controlled molecular size. SPI was predenatured by mild alkali at pH 10 and heated at 50°C for 1 h prior to partial hydrolysis by papain at pH 7.0 and 38°C for 10, 30, and 60 min (PMSPI10, PMSPI30, and PMSPI60). The hydrolysate PMSPI60 was further fractionated by ultrafiltration with a stirred cell and disc membranes (100-, 50-, and 20-kDa molecular weight cut-off) into one retentate (R100) and three permeates (P100, P50, and P20). Molecular weight distribution, surface hydrophobicity (S ₀), protein solubility (PS), emulsifying activity index (EAI), and emulsion stability index (ESI) of the control SPI (without added papain), hydrolysates, and ultrafiltrates were investigated. Significant increases (P<0.001) in S ₀, PS, EAI, and ESI were observed in the hydrolysates. Peptides in the permeates had higher PS and EAI but lower S ₀ than the peptides in the retentate and hydrolysate. Soy protein peptides that were prepared from SPI by papain modification and ultrafiltration had lower molecular weight, higher solubility, and higher emulsifying properties. They could find use in products that require these properties, especially in the cosmetic and health food industries.     

Enzymatic modification of soy protein concentrates by fungal and bacterial proteases

Solubility, foaming capacity and foam stability of denatured soy protein concentrate obtained from toasted flour were improved by proteolysis with fungal or bacterial proteases. Emulsifying capacity was unchanged, but emulsion stability decreased; bacterial protease highly improved oil absorption. Also, the bacterial protease was able to solubilize more protein and gave products which foamed more than those obtained with the fungal enzyme. However, the stabilizing properties of the bacterial modified soy protein concentrate at the air/water or oil/water interface were inferior. By limited hydrolysis up to degree of hydrolysis 10% most functional properties were improved without greatly reducing emulsion stability and water absorption.     

Antioxidative and Functional Properties of Pumpkin Oil Cake Globulin Hydrolysates

Cucurbitin extracted from pumpkin (Cucurbita pepo) oil cake was enzymatically hydrolysed with three different enzymes viz. alcalase, flavourzyme and pepsin. Antioxidative and functional properties of cucurbitin hydrolysates with different degrees of hydrolysis (DH) were investigated. The antioxidant activity of the hydrolysates was strongly dependent on the enzyme used. The hydrolysates obtained by alcalase and pepsin showed antioxidative potential whereas flavourzyme hydrolysates did not demonstrate these activities. Reducing power and 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) scavenging activity of cucurbitin hydrolysate were positively related to DH. The highest antioxidant activity was found in the hydrolysate obtained by alcalase at DH 25.6 % [reducing power of 0.25 ± 0.01 A700 nm and ABTS scavenging activity of 3.34 ± 0.02 mmol/L Trolox equivalent antioxidant coefficients (TEAC)]. Hydrolysis by all enzymes increased the protein solubility within the studied pH range. The best emulsion activity and stability index (EAI = 143.28 ± 3.05 m²/g and ESI = 87.5 ± 1.96 min) have hydrolysates produced by flavourzyme (DH 9.2 %) whereas alcalase produced hydrolysates with the best foaming capacity (FC = 242 ± 3.21). The results demonstrate that hydrolysates produced in the present study have good functional properties as well as antioxidant activity indicating their possible use in different food systems.     

Functional properties and protein concentrate of Pigeon pea (Cajanus cajan (I.) Millsp) flour

The objective of this investigation was to study the functional properties of Pigeon pea (Cajanus cajan (L.) Millsp) flour and protein concentrate. The solubility of both samples were superior than 70% at pH above 6.7 and below 3.5. The water and oil absorption were 1.2 and 1.07 ml/g of sample and 0.87 and 1.73 ml/g of flour and protein concentrate samples, respectively. The minimum concentration of flour and protein concentrate needed for gelation was 20% and 12%, respectively. The emulsifying capacity of flour and concentrate was 129.35 g and 191.66 g oil/g of protein and the emulsion stability 87.50 and 97.97%, respectively, after 780 minutes. The foam capacity and stability of flour foam were 36.0% and 18.61, while of the concentrate were 44.70% and 78.97% after 90 minutes. These properties indicate that the flour as well as the concentrate could have application in various food systems.     

Enzyme-assisted extraction of chicken skin protein hydrolysates and fat: Degree of hydrolysis affects the physicochemical and functional properties

Enzyme-assisted extraction (EAE) of oils/fats involves the disruption of the cell wall of source material using enzymes to facilitate the release of oil. When proteases are used as the enzyme, EAE ends in the extracted oil as well as the protein hydrolysates. Herein, the EAE (using a commercial protease, Alcalase) was exploited to obtain fat and protein hydrolysates from chicken skin. Degree of hydrolysis (DH, the percentage ratio of cleaved peptide bonds), which showed a logarithmic correlation with the reaction time, was found to affect the properties of the products. As the DH increased, the peptide chain length of protein hydrolysates decreased which was confirmed by SDS-PAGE analysis. With the increase of DH, the emulsifying activity index, foaming capacity, and oil holding capacity of the hydrolysates decreased but the solubility and emulsion stability index increased (p < 0.05). The DPPH free radical scavenging activity of the hydrolysates increased with the DH up to DH = 39.62% but decreased thereafter (p < 0.05). EAE resulted in a rise in fat yield and the fat contained a higher amount of unsaponifiables and lower free fatty acids (FFA) content, as compared to the control treatment (No enzyme, 80°C, 2 h, p < 0.05). DH affected the fat yield and the unsaponifiables content of the fat, positively (p < 0.05). However, it did not affect the fat FFA content and iodine value (p > 0.05). Results obtained here showed DH can be used as an effective measure for controlling the physicochemical and functional properties of chicken skin protein hydrolysates and fat in the EAE process.     

Preparation and properties of sodium alkyl sulfoacetates

The preparation and properties for a homologous series of sodium salts of alkyl sulfoacetates, containing 10, 12, 14 and 16 carbon atoms are described. The sodium salts of alkyl sulfoacetates were prepared from monochloroacetic acid, sodium sulfite and corresponding higher alcohol. The Krafft point, c.m.c. value, surface tension, solubilizing power, emulsifying power, foaming power, and calcium ion stability and resistance to acid hydrolysis were measured as the properties of these compounds. The c.m.c. values at 40 C obtained by electrical conductivity were related to the alkyl carbon number (N) of the compounds by log c.m.c.=4.852–0.301 N. Solubilizing power, emulsifying power and foaming power increased with the number of carbon atoms of alkyl chain in the surfactant. But the calcium ion stability and resistance to the acid hydrolysis decreased with an increase in the length of the hydrophobic portion.     

Effects of Conjugation between Proteins and Polysaccharides on the Physical Properties of Emulsion-Based Edible Films

The effects of conjugation between protein (soybean or peanut protein isolates) and polysaccharides (dextran or gum acacia) with different glycation time (0–32 hours) on the physical properties of emulsion-based edible films containing beeswax as dispersed phase were studied. Both the reaction time and type of polymers significantly (P < 0.05) affected the emulsifying properties of conjugates. Pearson's correlation analysis showed that the emulsifying activity index (EAI), emulsifying stability index (ESI), and droplet size of emulsions were in strong correlation with the physical properties of films, such as whiteness index, transparency, water vapor permeability, surface hydrophobicity, thermal stability, and mechanical properties. Furthermore, even though glycation could significantly (P < 0.05) affect intermolecular interactions between polymers in films, there was no strong correlation between the intermolecular interactions and the physical properties of films. Therefore, the emulsifying properties of conjugates are essential for preparing emulsion-based edible films.