Effects of ozone on functional properties of proteins

The present study investigates whether the ozone treatment could be an alternative to improve some functional properties of proteins. Ozone treatment was applied on whey protein isolate and egg white proteins which have been extensively used in food products to improve textural, functional and sensory attributes. Ozone treatment of proteins was performed either in aqueous solutions or as gas ozonation of pure protein powders. Foam formation and foam stability of proteins were enhanced extensively. The solubility of proteins were reduced as influenced from the aqueous and gas ozonation medium. The reduction was more pronounced in egg white proteins. Ozone treatment affected emulsion activity of whey protein isolate negatively and reduced the emulsion stability.     

Effects of succinylation and deamidation on functional properties of oat protein isolate

The effects of two different modification methods (deamidation and succinylation) on the functional properties (solubility, water- and oil-binding capacity, foaming capacity and stability, emulsion activity and stability) of oat protein isolates were evaluated. Protein isolates extracted from defatted oat flour at alkaline pH were acylated by 0.20 g/g of succinic anhydride. The protein isolate was also modified using a mild acidic treatment (HCl, 0.5 N). Succinylation and deamidation improved solubility and emulsifying activity of the native protein isolate. Foaming capacity of oat protein isolate increased after deamidation, whereas succinylation decreased it. The deamidated and succinylated proteins had lower foam and emulsion stabilities than had their native counterpart. Water- and oil-binding capacity, in both modified oat proteins, was higher than those of the native oat protein isolate.     

米糠蛋白的分离及其营养特性的研究

米糠中含有较高的蛋白质,其必需氨基酸组成近似于人体需要量模式,本文基于此原因,主要介绍了米糠蛋白的分离方法以及营养特性,相信米糠蛋白将成为食品工业的一种新型蛋白质。     

Effects of barley flour and barley protein isolate on chemical, functional, nutritional and biological properties of Pita bread

This study was carried out to investigate the effects of fortification of wheat flour with barley flour (BF) and barley protein isolate (BPI) at three levels; 5, 10 and 15% levels on the chemical composition, nutritional evaluation and biological properties of pita bread. Proteins fractions such as globulin, prolamin, glutelin-1 and glutelin-2 as well as protein isolates were extracted from barley flour and evaluated for protein yield, chemical composition and nutritional quality. Highest yield and essential amino acids contents were obtained in barley protein isolate. SDS-PAGE gels electrophoresis indicated that fortified wheat flour with BPI and BF consists of proteins coming from wheat flour and barley proteins. The contents of essential limiting amino acids in bread were increased from 1.38 to 3.10 g/100 g for lysine and from 0.86 to 1.73 g/100 g for methionine as the ratio of fortification with BF and BPI increased from 0 to 15%. The highest content of total phenolics, antioxidant activity, and inhibitory activity for both angiotensin converting enzyme (ACE) and α-amylase were found in fortified bread with BPI at 15%. Results indicated that bread made from fortification of wheat flour with BF and BPI at 15% showed superior chemical, physico-chemical, nutritional and biological properties.     

Chemical composition,functional properties,and bioactivities of rapeseed protein isolates

In order to utilize rapeseed protein from oil industry waste for food applications, rapeseeds were pretreated to remove the oil using hexane. Two protein isolates were prepared, one by precipitation at controlled pH and the other by ultrafiltration. The precipitated and ultrafiltered protein isolates, respectively, contained 70.8% and 98.7% protein. The ultrafiltered protein isolate had a better emulsification capacity than had whole egg. The ultrafiltered protein isolate had a protein solubility of 52.5–97.2% in the range pH 3–9, whilst the maximum protein solubility of the precipitated protein isolate was 26.4% in the pH range 7–9. There were no significant differences between the precipitated and ultrafiltered protein isolates regarding their angiotensin converting enzyme inhibition are their bile acid-binding capacity. Their bile acid-binding capacity and angiotensin converting enzyme inhibition capacities were lower than of those de-oiled soybean. They showed stronger DPPH radical-scavenging activity than did de-oiled soybean.     

Maleic anhydride derivatives of a protein isolate: preparation and functional evaluation

African locust bean protein isolate (NPI) was acylated with maleic anhydride at various concentrations. Addition of maleic anhydride at the levels of 0.1, 0.5 and 1.0 g/g of protein produced 36.4% (MP1), 43.7% (MP2) and 73.6% (MP3) of maleylated protein isolate, respectively. Water absorption capacity increased after maleylation but oil absorption capacity reduced progressively with increase in level of modification. Results also revealed that gelation capacities reduced after protein modifications. Emulsifying activity (EA) and emulsion stability (ES) increased following protein modification. In addition, corresponding increases in emulsifying properties were observed with increase in degree of modification of the proteins. Maleylation improved the foaming capacity of the native protein. Foaming capacity increased with increases in protein concentration for both native and maleylated protein derivatives while progressive decline in foam stability occurred with increases in level of protein modification.     

Effect of peanut protein isolate on functional properties of chicken salt-soluble proteins from breast and thigh muscles during heat-induced gelation

In this study, we investigated the impact of peanut protein isolate (PPI) on the functional properties of chicken salt-soluble protein (SSP) prepared from breast and thigh muscles during heat-induced gelation. The addition of PPI increased the water-holding capacity, gel strength and elasticity of heat-induced chicken SSP mixed gel. Breast and thigh SSP had the best gel properties at the addition of 2.5% and 3.5% PPI, respectively. Rheology indicated that thigh SSP showed higher storage modulus (G') than breast SSP. Differential scanning calorimetry showed that the addition of PPI changed transition temperatures (Tmax) and enthalpy of denaturation (ΔH) of chicken SSP. Scanning electron microscopy indicated that the PPI-treated SSP gels had more compact ultrastructures than controls. The results suggested that PPI may be a potential protein additive for improve the characteristics of SSP gelations.     

Influence of heat processing on functional properties of Australian wattle seed (Acacia victoriae Bentham) extracts

Whole wattle (Acacia victoriae Bentham) seed was extracted with water before or after a soaking/heat treatment regime designed to destroy its protease inhibitors. The yield, composition and physical properties of these extracts were measured and they were then subjected to an analysis of their functional properties, which included emulsion and foam formation and stabilization, solubility at different pH values and gelling ability. Processing of soaked wattle seed at 100 °C for 30 s led to a much reduced extract yield and viscosity at both pH 4 and 7, decreased its water-soluble carbohydrate content but increased its protein content, and solubility under alkaline conditions. Processing of wattle seed before extraction also led to increased emulsion droplet size and reduced emulsion stability, the differences being more pronounced in emulsions formed with 20% oil compared with 50% oil-in-water emulsions. Comparatively, the emulsions formed using extract from non-processed wattle seed were very stable at both 20% and 50% oil levels, especially at pH 7 where the enhanced viscosity of the extract predominated. All extracts had very low foaming capacity, and gelation did not occur in any of the samples even at 10% (w/v) extract concentration.     

Production and functional properties of beef lung protein concentrates

This work investigated the production and the properties of meat protein concentrates from beef lungs (BLPC) at pilot scale. Protein recovery and functional properties were compared to those of BLPC obtained using membrane technology in a previous work (Selmane, D., Vial, C., & Djelveh, G. (2008). Extraction of proteins from slaughterhouse by-products: Influence of operating conditions on functional properties. Meat Science, 79, 640–647). An alkaline solubilisation method was applied for protein extraction, followed by pI precipitation for concentration. The physicochemical properties of BLPC such as molecular mass, solubility, surface hydrophobicity, surface tension and interfacial tension, as well as technofunctional emulsifying and foaming properties were determined. These were compared to those of commercial protein ingredients, such as sodium caseinates, whey protein isolates, egg white proteins and soy protein isolates. Results showed that proteins from BLPC included a low-molecular-weight fraction and exhibited good solubility and high hydrophobicity with small surface and interfacial tensions. This explained their excellent emulsifying activity, better than sodium caseinates, and their good foaming properties.     

Effect of extraction and isolation on physicochemical and functional properties of an underutilized seed protein: Gingerbread plum (Neocarya macrophylla)

The effect of extraction and isolation on the physicochemical and functional properties of gingerbread plum seed protein isolate was studied. Gingerbread plum seed protein isolate was extracted from defatted gingerbread plum seed flour (DGPSF) by alkali solution along with isoelectric precipitation. The protein isolate was subjected to freeze or vacuum drying process. Freeze dried gingerbread plum seed protein isolate (FGPSPI) and vacuum dried gingerbread plum seed protein isolate (VGPSPI) were evaluated for their physicochemical and functional properties (protein solubility, water/oil binding capacity, emulsifying capacity, foaming capacity). Among physicochemical parameters, the proximate composition, amino acid composition, minerals, differential scanning calorimetry (DSC), SDS-PAGE and color attributes were studied. Both FGPSPI and VGPSPI contained over 90% protein versus DGPSF (56.72%) used as raw material. The method of drying had significant effect (p < 0.05) on the physicochemical characteristics of FGPSPI and VGPSPI except for amino acids composition. The functional properties were variable among samples. DGPSF had higher emulsifying, water holding and oil binding capacities compared with FGPSPI and VGPSPI. FGPSPI exhibited better emulsifying capacity and water holding capacity than VGPSPI. FGPSPI also showed comparable oil binding capacity and bulk density to commercial soy protein isolate (SPI). The results indicated that FGPSPI and VGPSPI could be a good source of protein fortification for a variety of food products for protein deficient consumers as well as a potential food ingredient.     

Physicochemical and functional properties of the protein isolate and major fractions prepared from Akebia trifoliata var. australis seed

The physicochemical and functional properties of protein isolate (API) and major protein fractions prepared from Akebia trifoliata var. australis seed were investigated. The seed contained 38.83% of oil and 17.23% of protein. Albumin (51.65%) and glutelin (46.40%) were the predominant fractions in the protein component of the seed. The major amino acids were found to be glutamic acid and aspartic acid, while the contents of sulphur-containing amino acids and threonine were very low. One to eight distinct bands with molecular weight (MW) ranging from 12.0 to 50.0 kDa were displayed by SDS–PAGE. The solubilities of API, albumin and glutelin from seeds of the A. trifoliata var. australis were the lowest at pH 4.0–5.0. The high surface hydrophobicity indices of these three proteins were observed at pH 7.0, while the excellent emulsifying properties were displayed at pH 9.0. Circular dichroism measurements indicated that API, albumin and glutelin were rich in β-strand and random coil structures.     

Comparative study of functional properties of commercial and membrane processed yellow pea protein isolates

Functional properties of commercial and membrane processed pea protein isolates (PPI) prepared from yellow peas were investigated. Four protein isolates were prepared from yellow pea flour using water and KCl extractions at 25 °C followed by ultrafiltration and diafiltration (UF and DF) at pHs of 7.5 and 7.5 or 6 respectively. Following assessment of compositional attributes; solubility, foaming, flow and dynamic rheology, emulsification ability and heat-induced textural and rheological properties of prepared PPIs and a commercially available PPI were tested and compared. Membrane purification of proteins resulted in 28% to 68% reduction in phytic acid and enhanced, comparatively, the tested functional properties. Solubility of membrane processed PPIs, at all tested pHs, was superior and the lowest foaming stability and apparent viscosity were associated with commercial PPI. Gelling temperatures of water and KCl extracted PPIs, DF treated at pH 6, trimmed down to 75.7 ± 0.63 °C and 81.6 ± 0.55 °C in contrast to that of commercial PPI at above 90 °C. Similarly, the formation of firm gels, after 1 h heating at 90 °C, was associated with membrane processed PPIs whereas commercial PPI did not develop any gel.     

Molecular characterization of Italian rice cultivars

Random amplified polymorphic DNA (RAPD) is an efficient tool to detect DNA polymorphisms and to distinguish different clones and cultivars. We have applied the RAPD technique to distinguish, starting from a single rice seed, among some Italian rice cultivars from market and from National Institute for research on food and nutrition, Italy. We also estimated the genomic similarity among the rice cultivars object of this study taking advantage of the amplification patterns. Despite the low genomic variability among Italian rice cultivars, RAPD technique allowed us to distinguish among them. This indicates that RAPD can be used routinely to verify the identity of Italian rice cultivars in order to prevent fraudulent commercial activity.     

Extraction of proteins from slaughterhouse by-products: Influence of operating conditions on functional properties

This study investigated the extraction and functional properties of proteins from slaughterhouse by-products: pork lungs, beef lungs and mechanically deboned chicken meat (MDCM). The extraction yield was investigated as a function of pH, temperature and time. Membrane technology was used for purification of proteins from pork and beef lungs, while for MDCM a method based on PI was applied. In the three cases, yields of protein recovery were between 48 and 55% (w/w). The functional properties of the protein concentrates were compared to those of some commercial ingredients. Proteins from pork lungs and MDCM exhibited better gelling properties than egg white and beef plasma, while beef and pork lungs displayed very good emulsifying properties, similar to Na-caseinates. As the methods developed are easy to scale-up, the use of by-product proteins at industrial scale appears to be an interesting opportunity to obtain added value slaughterhouse by-products.     

Protein isolates from two Mediterranean legumes: Lathyrus clymenum and Lathyrus annuus. Chemical composition,functional properties and protein characterisation

Protein isolates were analysed from two Mediterranean legumes, Lathyrus clymenum and L. annuus. Protein isolates were prepared by alkaline extraction, including sodium sulphite and acid precipitation of Lathyrus proteins at their isoelectric point (pH 4.5). The percentage of proteins recovered from L. annuus and L. clymenum flours during the preparation of the protein isolates was around 60%. Chemical composition, nutritional parameters, main functional properties and protein composition of Lathyrus protein isolates were studied. L. annuus and L. clymenum protein isolates contained 81.07% and 82.4% of proteins, respectively, and they have a balanced content of essential amino acids, except for sulphur amino acids, with respect to the FAO pattern. The in vitro protein digestibility increased in the protein isolates to 93% and 95% in L. annuus and L. clymenum, respectively. Functional properties were similar to those observed in other legumes protein isolates. These results confirm the interest of local crops as sources of high value protein products obtained after convenient protein extraction procedures and the removal of antinutritional components. These high added value protein isolates are of interest for the food industry and for the revalorisation of L. annuus and L. clymenum favouring the bioconservation of Lathyrus.     

Functional properties of the Maillard reaction products of rice protein with sugar

The glycation of rice proteins with reducing sugars was investigated in an attempt to improve their solubility and functionality. Rice proteins isolated from a Chinese milled medium-grain rice were glycated with glucose, lactose, maltodextrin, or dextran in 2% aqueous dispersions. The sugar that provided the most improvement of the solubility, emulsification activity (EA) and emulsification stability (ES) of the Maillard reaction products was glucose. The optimum reaction conditions were at pH 11, 100 °C, and reaction time 15 min, which increased the solubility, EA and ES of rice protein from 20%, 0.46 and 11.1 to 92%, 0.64 and 18.2, respectively. Extending the reaction time beyond 15 min continued the development of latter-stage Maillard browning products without improvements in the functional properties of the Maillard reaction products. SEC–HPLC analysis with light scattering detection showed a decrease of the weight-averaged molecular weight from 500 to 100 K during the initial 15 min.     

Antioxidative and functional properties of protein hydrolysate from defatted skipjack (Katsuwonous pelamis) roe

Antioxidative and functional properties of protein hydrolysate from defatted skipjack (Katsuwonous pelamis) roe, hydrolysed by Alcalase 2.4 L (RPH) with different degrees of hydrolysis (DH) at various concentrations were examined. As DH increased, the reduction of DPPH, ABTS radicals scavenging activities and reducing power were noticeable (p < 0.05). The increases in metal chelating activity and superoxide scavenging activity were attained with increasing DH (p < 0.05). However, chelating activity gradually decreased at DH above 30%. All activities except superoxide anion radical scavenging activity increased as the concentration of hydrolysate increased (p < 0.05). Hydrolysis using Alcalase could increase protein solubility to above 80% over a wide pH range (2–10). The highest emulsion ability index (EAI) and foam stability (FS) of hydrolysates were observed at low DH (5%) (p < 0.05). Concentrations of hydrolysates determined interfacial properties differently, depending on DH. The molecular weight distribution of RPH with 5%DH (RPH5) was determined using Sephadex G-75 column. Two major peaks with the molecular weight of 57.8 and 5.5 kDa were obtained. Fraction with MW of 5.5 had the strongest metal chelating activity and ABTS radical scavenging activity. The results reveal that protein hydrolysates from defatted skipjack roe could be used as food additives possessing both antioxidant activity and functional properties.     

Functional properties of Maillard reaction products of rice protein hydrolysates with mono-, oligo- and polysaccharides

The Maillard reaction was carried out under wet reaction conditions using rice protein product from limited hydrolysis to conjugate with various mono-, oligo- and polysaccharides. The Maillard reaction products (MRPs) prepared with rice protein hydrolysates at 5% degree (hydrolysed by Protease N) and dextran T20 (20 min at 100 °C) showed the greatest improvement in functionality. The solubility, emulsification activity (EA), and emulsification stability (ES) of the MRPs increased by factors of 3.5, 5.3 and 7.3 times, respectively as compared to MRPs formed with native rice proteins and dextran T20. Amino acid analysis indicated that lysine and arginine decreased significantly in the MRPs. Formation of MRPs reduced the surface hydrophobicity, which was in agreement with the change of solubility. However, further decreasing of the surface hydrophobicity resulted in lower EA and ES during the late stage of the reaction. Fluorescence analysis suggested that formation of late stage MRPs occurred after 20 min of the Maillard reaction. The molecular weight distributions showed that the functional properties of MRPs and the mechanisms of formation were affected by the peptide chain length.     

Enzymatic hydrolysis of rice dreg protein: Effects of enzyme type on the functional properties and antioxidant activities of recovered proteins

The effects of various proteases on the formation and characteristics of rice dreg protein hydrolysates (RDPHs) were investigated. Enzymatic hydrolysis of often under-utilised rice dreg protein (RDP) with different enzymes studied here was found to significantly improve protein content and solubility. RDPHs prepared by alkaline protease showed better protein recovery, producing higher protein content with much smaller peptides, while hydrolysates generated by Protamex showed the highest antioxidant activities with more than 80% solubility over a wide pH range. The results indicated that the type of protease greatly influenced the molecular weight and amino acid residue composition of RDPH. The enzyme type also determined the functional properties and antioxidant activity of the recovered proteins. It was found that an optimum allocation of alkaline protease in addition to the Neutrase enzyme could be an appropriate strategy to produce RDPH with desirable functionalities, antioxidant properties, and low salt content.     

Improvement of functional properties of peanut protein isolate by conjugation with dextran through Maillard reaction

Reaction mixtures containing peanut protein isolate (PPI) and dextran (1:1 weight ratio) were dry-heated at 60 °C and 79% relative humidity for 7 days. SDS-PAGE analysis indicated that PPI had become complexed with dextran to form conjugates of higher molecular weight. Arachin, accounting for 50% of peanut proteins, was hard to glycosylate with dextran, which might limit the extent of glycosylation of PPI. The thermal stability of PPI was remarkably improved by mixture/conjugation with dextran. Proteins in mixtures/conjugates might have a more compacted tertiary conformation than PPI. The protein solubility of conjugates at pH 4.5-6.0 was remarkably increased compared with the PPI/mixture. Mixture with dextran could significantly improve the emulsifying and foaming properties of PPI (p < 0.05). Conjugation with dextran could further enhance emulsifying and foaming properties of PPI.