Functional properties of protein isolates,globulin and albumin extracted from Ginkgo biloba seeds

In this study, the functional properties of Ginkgo seed protein isolate (GPI), Ginkgo seed globulin protein (GGP) and Ginkgo seed albumin protein (GAP) extracted from Ginkgo biloba seeds were investigated. The protein contents of GPI, GGP and GAP were 91.0%, 93.4% and 87.8%, respectively in the samples in which the sugar, polyphenol and crude fibre were removed by the preparation procedure. For functional properties of Ginkgo seed proteins in the natural state, GAP showed the highest oil-absorption capacity (9.3 ml/g), foaming capacity (67.8%), emulsifying capacity (65.4%) and emulsion stability (90.6%); while GPI showed the highest water absorption capacity (1.93 ml/g), and GGP showed the highest foam stability (55.5%). The differences of the chemical components, surface hydrophobicity, disulphide bond (SS) and sulfhydryl group (SH) contents of GPI, GGP and GAP, which were correlated significantly with functional properties of Ginkgo seed proteins, were also investigated. The improved functional properties, such as water absorption capacity, solubility, foaming properties and emulsifying properties of Ginkgo seed proteins were observed in a pH range of 8.0–10.0 or sodium chloride concentration of 0.5–0.75 M.     

Functional properties of protein concentrates and isolates produced from cashew (Anacardium occidentale L.) nut

Protein isolates and concentrates were obtained from defatted cashew nut powder by two methods: alkaline extraction-isoelectric precipitation (IP) and alkaline extraction-methanol precipitation (MP). The functional properties of cashew nut protein isolates, concentrates and powder were significantly different (p < 0.05). Cashew nut protein isolate (CNPI) had higher water and oil absorption capacities (2.20 ml/g and 4.42 ml/g, respectively), emulsifying stability index (447%), foam capacity and stability (45% and 55%, respectively), and least gelation capacity (13.5%) than cashew nut protein concentrate (CNPC), which was also higher than that of defatted cashew nut powder (DCNP). However, emulsifying activity index (12.45%) and bulk density (0.31) of CNPI were lower than that of CNPC, which were also lower than that of DCNP. The water solubility of CNPI (95%) and CNPC (95%) was not significantly different (p > 0.05) among the samples, but was significantly different (p < 0.05) from that of DCNP (75%). The CNPI, CNPC and DCNP showed decreasing solubility with decreasing pH, with the minimum solubility being observed at a pH range of 4.0–4.5, confirming the isoelectric point of cashew proteins. However, higher water solubility, emulsifying activity, and foaming property were observed at an alkaline pH than at an acidic pH in all samples.     

Protein extraction optimisation,characterisation, and functionalities of protein isolate from bitter melon (Momordica charantia) seed

Bitter melon seeds are a rich source of protein. Optimum conditions for protein extraction from the seeds, determined using a response surface design, were at a pH 9.0 and 1.3 M NaCl. Soy protein isolate (SPI) was included for comparison. Surface hydrophobicity of bitter melon seed protein isolate (BMSPI) (690) was significantly higher than that of SPI (399). Electrophoretograms of BMSPI showed bands at 40 and 55 kDa, and at 22, 25, and 35 kDa in non-reducing and reducing buffers, respectively. BMSPI had most of the essential amino acids and hence could be considered as a high quality protein. BMSPI had a single denaturation temperature (113.1 °C) while SPI had two denaturation temperatures (78.0 and 94.8 °C). The proteins exhibited U-shaped curves with solubilities ranging from 62.0% to 67.5% for BMSPI and 86.7% to 90.1% for SPI at pH ? 7.0. BMSPI had lower emulsifying activity (0.36 vs. 0.73), foaming capacity (39.6 vs. 61.0 ml), and foaming stability (21.5 vs. 25.5 min) than had SPI.     

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.     

Improvement of functional properties of chickpea proteins by hydrolysis with immobilised Alcalase

Limited chickpea protein hydrolysates ranging from 1% to 10% degree of hydrolysis were produced from chickpea protein isolate (CPI) using Alcalase immobilised on glyoxyl-agarose gels. Alcalase-glyoxyl derivative produced after 24 h of immobilisation at room temperature was 24 times more stable than soluble enzyme and presented approximately 51% of the activity of Alcalase. The chemical composition of chickpea hydrolysates were very close to that of CPI. Solubility, oil absorption, emulsifying activity and stability, and foaming capacity and stability were determined. All protein hydrolysates showed higher solubility than intact proteins, especially at pHs near isoelectric point of native chickpea proteins. Moreover, all hydrolysates had better functional properties, except emulsifying activity, than the original protein isolate.     

Heat-induced modifications in the functional and structural properties of vicilin-rich protein isolate from kidney (Phaseolus vulgaris L.) bean

Heat-induced changes in the physico-chemical (and/or functional) and structural properties of protein isolate from kidney beans (KPI) were characterised. The extent of protein denaturation, free sulphydryl contents, surface hydrophobicity, as well as structural characteristics of the proteins were evaluated. Analyses of size-exclusion chromatography combined with laser scattering showed that the heating at 95 °C led to transformation of 7S-form vicilin to its 11S-form, and even higher molar mass (MW) oligomers or polymers. Moderate heating (for 15–30 min) significantly improved protein solubility, emulsifying and foaming activities (at neutral pH), whilst extensive heating (for 60–120 min) on the contrary decreased these properties. Spectral analyses of fluorescence and/or Raman spectroscopy showed that tertiary and secondary conformations of protein in KPI were remarkably affected to a varying extent by the heating. The results suggested a close relationship between functional properties of the vicilin from kidney bean and its conformational characteristics.     

Interfacial and emulsifying properties of lentil protein isolate

The dynamic interfacial tension (DIFT) at oil–water interface, diffusion coefficients, surface hydrophobicity, zeta potential and emulsifying properties, including emulsion activity index (EAI), emulsion stability index (ESI) and droplet size of lentil protein isolate (LPI), were measured at different pH and LPI concentration, in order to elucidate its emulsifying behaviour. Sodium caseinate (NaCas), whey protein isolate (WPI), bovine serum albumin (BSA) and lysozyme (Lys) were used as benchmark proteins and their emulsifying property was compared with that of LPI. The speed of diffusion-controlled migration of these proteins to the oil/water interface, was in the following order: NaCas > LPI > WPI > BSA > Lys, while their surface hydrophobicity was in the following order: BSA > LPI > NaCas > WPI > Lys. The EAI of emulsions stabilised by the above proteins ranged from 90.3 to 123.3 m²/g and it was 93.3 ± 0.2 m²/g in LPI-stabilised emulsion. However, the stability of LPI-stabilised emulsions was slightly lower compared to that of WPI and NaCas-stabilised emulsions at the same protein concentration at pH 7.0. The ESI of LPI emulsions improved substantially with decrease in droplet size when protein concentration was increased (20–30 mg/ml). Reduction of disulphide bonds enhanced both the EAI and ESI compared to untreated samples. Heat treatment of LPI dispersions resulted in poor emulsion stability due to molecular aggregation. The stability of LPI-stabilised emulsions was found to decrease in the presence of NaCl. This study showed that LPI can be as effective emulsifiers of oil-in-water emulsions as are WPI and NaCas at ?20 mg/ml concentrations both at low and neutral pH. The emulsifying property of LPI can be improved by reducing the intra and inter-disulphide bond by using appropriate reducing agents.     

木瓜蛋白酶控制水解蚕豆水溶性蛋白及水解度对蚕豆蛋白功能性质的影响

针对蚕豆蛋白在pH较低的体系中溶解性差、乳化能力低,制约其在食品工业中应用等问题,应用808Titrando瑞士万通全自动滴定仪控制木瓜蛋白酶水解蚕豆蛋白,实现蚕豆蛋白的有限水解,探讨水解度对蚕豆蛋白水解物的溶解性、乳化能力及持水性等功能性质的影响。通过木瓜蛋白酶的控制水解获得水解度为2%～4%的蚕豆蛋白水解物;与蚕豆蛋白相比,在pH4.0～6.0体系、水解度为4%的蚕豆蛋白水解物的溶解度提高2～3倍;pH6.0、水解度为2%的蚕豆蛋白水解物的乳化能力是蚕豆蛋白的2.3倍,持水力是蚕豆蛋白的1.6倍。     

Emulsifying and foaming properties of Phaseolus vulgaris and coccineus proteins

Protein isolates from two Phaseolus cultivars, common bean (Phaseolus vulgaris L.) and scarlet runner bean (Phaseolus coccineus L.), were prepared by wet extraction methods (isoelectric precipitation – 4000 rpm, ultrafiltration, extraction with NaCl 2%, and isoelectric precipitation – 9900 rpm). The protein isolates were characterized by sodium dodecyl sulfate–polyacrylamide gel electrophoresis and then evaluated for their solubility. The emulsion stability of emulsions produced at pH 7.0 and 5.5 with 1% or 2% or 3% w/v protein isolate was evaluated by average droplet size diameter, viscosity and creaming measurements. Emulsions with 1% protein content were unstable through storage. Emulsions with 3% w/v protein isolate concentration, extracted by ultrafiltration at pH 5.5 from both cultivars, were flocculated; this was more pronounced for coccineus isolates. The foaming properties, for the respective foams, were investigated. Foams with 1% w/v protein showed little foaming ability Ultrafiltration isolates produced more foam, which was especially stable at pH 5.5.     

Functional properties of fish protein hydrolysates from Pacific whiting(Merluccius productus) muscle produced by a commercial protease

Pacific whiting (Merluccius productus) muscle was used to produce hydrolysates with 10%, 15% and 20% degree of hydrolysis (DH) using the commercial protease Alcalase^® and were characterized at pH 4.0, 7.0 and 10 according their solubility, emulsifying and foaming properties. Protein recovered in soluble fractions increased proportionally with the hydrolytic process, yielded 48.6 ± 1.9, 58.6 ± 4.1 and 67.8 ± 1.4 of total protein after 10%, 15% and 20% DH, respectively. Freeze-dried hydrolysates presented almost 100% solubility (p > 0.05) at the different pHs evaluated. Emulsifying properties (EC, EAI and ESI) were not affected by DH as most samples showed similar (p > 0.05) results. Higher EC (p ? 0.05) than sodium caseinate, used as control, were obtained at pH 4 for most hydrolysates. Hydrolysates showed very low foaming capacity not affected by pH; but foam stability was equal or even better (p > 0.05) than bovine serum albumin (BSA), except at pH 4.0. Results suggest that hydrolysates from Pacific whiting muscle can be produced with similar or better functional properties than the food ingredients used as standards.     

Enzymatic preparation and functional properties of wheat gluten hydrolysates

The water-insolublity of wheat gluten is one of the major limitations for its more extensive use in food processing. Wheat gluten was enzymatically hydrolyzed by several commercially available proteases (Pancreatin Trypsin 6.0S, Porcine pepsin, Pancreatin and Alcalase 2.4L) with protein recovery varying from 42.5 ± 0.7% to 81.3 ± 0.1%. The hydrolytic efficiency of these proteases on wheat gluten was also compared. Alcalase served best for the preparation of wheat gluten hydrolysates (WGHs). Thus, Alcalase-assisted hydrolysates of wheat gluten (AWGHs) with different degrees of hydrolysis (DH 5.0, 10.0 and 15.0%) were further assessed for their functionalities. All the AWGHs had excellent solubility (>60%) over a pH range of 2–12. The emulsifying and foaming properties of AWGH with relatively low DH (5.0%) were remarkably higher compared to the original gluten. However, extensive hydrolysis of gluten resulted in remarkable reduction in emulsifying and foaming properties.     

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.     

Physicochemical,nutritional and functional properties of marama bean flour

Marama bean is a protein-rich, underutilised, drought-tolerant legume in sub-Saharan Africa. Its utilisation may be increased through value addition into protein-rich flours. Defatted flour from unheated and dry-heated (150 °C/20 min) whole marama beans (UMF and HMF) were analysed for physicochemical and protein-based functional properties. Heating significantly increased in vitro protein digestibility of marama bean flour. Of functional importance are the high levels of tyrosine present in marama bean flours. Heating significantly reduced protein solubility and emulsifying capacity of marama bean flours whilst water absorption capacity was improved. Foaming capacity was not affected by heating. UMF could be useful in food systems requiring high emulsifying capacity, but would not be suitable for applications requiring high water absorption and foaming capacity. Due to its high protein contents, marama bean flour could be used to increase the protein quality of cereal-based foods to help alleviate protein-energy nutrition in the region.     

Functional properties of raw and heat processed cashew nut (Anacardium occidentale, L.) kernel protein isolates

The functional properties viz. solubility, water and oil absorption, emulsifying and foaming capacities of the protein isolates prepared from raw and heat processed cashew nut kernels were evaluated. Protein solubility vs. pH profile showed the isoelectric point at pH 5 for both isolates. The isolate prepared from raw cashew nuts showed superior solubility at and above isoelectric point pH. The water and oil absorption capacities of the proteins were slightly improved by heat treatment of cashew nut kernels. The emulsifying capacity of the isolates showed solubility dependent behavior and was better for raw cashew nut protein isolate at pH 5 and above. However, heat treated cashew nut protein isolate presented better foaming capacity at pH 7 and 8 but both isolates showed extremely low foam stability as compared to that of egg albumin.     

Amino acid composition and functional properties of collagen polypeptide from Yak (Bos grunniens) bone

Collagen polypeptide was prepared from Yak bone by applying papain as a catalyst. Its relative molecular weight distribution and amino acid composition were determined. Moreover, its main functional properties including water and oil absorption, water-holding capacity, emulsifying ability and stability, foaming ability and foam stability were investigated. The polypeptide had a molecular weight distribution of 11.7-43 kDa, in which most distributed at 11.7-25.3 kDa. It was high in glycine, alanine, proline, hydroxyproline and glutamic acid but low in methionine, tyrosine and histidine, the total amino acid amount being 88.06 g/100 g. The polypeptide showed good water adsorption, water-holding capacity, oil absorption, emulsifying and foaming properties. It is hoped to be applied in food and cosmetic.     

Some physicochemical and functional properties of alfalfa soluble leaf proteins

Important physicochemical and functional properties of soluble leaf proteins (SLPs) from alfalfa herbage are presented. Subunits molecular weight (MW) distribution, denaturation temperature, and functional properties like, emulsification, foaming, and solubility are discussed. SLP concentrates were prepared by acid precipitation, and ultrafiltration of clarified alfalfa juice. The MW of major soluble protein component ribulose 1,5, bisphosphate carboxylase/oxygenase was estimated to be around 490 kDa. Denaturation temperature of soluble proteins was observed to be around 70-75 °C. Most of the functional properties were affected by concentrate preparation. Acid-precipitated SLP concentrate showed lowest emulsifying properties and nitrogen solubility. Heat stability of emulsions was good. Foam overrun for SLP concentrate depended on pH and was stable around protein's isoelectric point. Stress relaxation tests on 7/100 g SLP gels indicated that they were softer gels and relaxed faster compared to 13/100 g WPI gels. SLP preparations showed encouraging functional properties.     

Isolation and characterization of protein isolated from defatted cashew nut shell: Influence of pH and NaCl on solubility and functional properties

This work reports the isolation of protein from defatted cashew nut shell (CNS), with the crude protein product containing 91.07% protein. Under its natural conditions, the solubility of this protein isolate is comparable (74.02%) to that of mustard green meal protein. The solubility of the protein isolate decreases with decreasing pH, with the minimum solubility observed at its isoelectric point (pH 3). The water holding capacity, oil holding capacity, foaming capacity, foam stability, emulsifying capacity and emulsion stability were found to be 2.56 cm³ H₂O/g protein, 4.28 cm³ oil/g protein, 76.88%, 70.98%, 62.0% and 79.0%, respectively. The profiles of these functional properties were determined with varying pH values and NaCl concentrations, and improved properties were observed in the alkaline pH range and in the presence of NaCl. Electrophoretic analysis showed that the high molecular weight protein globulin was the major protein in the protein isolate.     

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 lentil protein isolates prepared by different drying methods

Lentil protein isolate (LPI) extract was converted into powder by freeze drying, spray drying and vacuum drying. Differences in particle size distribution, protein subunit composition and colour and surface morphology were observed amongst the three drying methods. Spray and freeze-dried LPI powders exhibited higher solubility (81% and 78%, respectively) compared to vacuum dried powders (50%). The spray dried powders showed a low water absorption capacity (0.43 ± 0.02 g/g) compared to freeze (0.48 ± 0.02 g/g) and vacuum-dried (0.47 ± 0.01 g/g) LPI powders. Spray and freeze-dried powders displayed better gelation ability and higher gel strength, compared to vacuum-dried powder. Both spray and freeze-dried gels showed typical viscoelastic gel characteristics, with G′ dominating over G″ and very low loss tangent. The holding time required for gelation of vacuum dried powder at 90 °C was significantly longer, compared to spray and freeze dried powders. Hence, drying methods used for preparation of lentil protein isolate powders can affect physicochemical and associated functional properties.     

绿豆清蛋白功能特性及热特性研究

对水浸提法制备的绿豆清蛋白进行不同温度、不同pH、不同浓度对其功能特性的影响测试,并测试清蛋白的热变性温度。结果表明,在室温时,在等电点附近(pH4.6)绿豆清蛋白的溶解性、持水性最差,在偏离等电点时其溶解性、持水性显著提升;在中性条件下,在40℃时,溶解性、持水性最好;清蛋白吸油性随着温度升高而减弱;乳化性及乳化稳定性、起泡性及起泡稳定性随清蛋白浓度增加而增强,但增幅趋缓。热变性测试结果显示,绿豆清蛋白的初始变性温度100.1℃及焓变值ΔH(3.382J/g),说明清蛋白热稳定性较好。