不同干燥方法对花生蛋白功能特性的影响

以花生蛋白为原料,分别采用热风干燥、真空干燥、微波干燥和微波结合真空干燥对花生蛋白进行干燥处理,比较不同的干燥方式对花生蛋白功能特性(吸油性、持水性、乳化性、乳化稳定性、起泡性能和起泡稳定性)的影响。实验表明,微波结合真空干燥的花生蛋白不仅干燥时间短,而且具有较好的功能特性,微波结合真空干燥是一种干燥花生蛋白的适宜方法。     

不同干燥方法对花生蛋白功能特性的影响

以花生蛋白为原料，分别采用热风干燥、真空干燥、微波干燥和微波结合真空干燥对花生蛋白进行干燥处理，比较不同的干燥方式对花生蛋白功能特性（吸油性、持水性、乳化性、乳化稳定性、起泡胜能和起泡稳定性）的影响。实验表明，微波结合真空干燥的花生蛋白不仅干燥时间短，而且具有较好的功能特性，微波结合真空干燥是一种干燥花生蛋白的适宜方法。     

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 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.     

Effect of denaturation during extraction on the conformational and functional properties of peanut protein isolate

Peanut protein isolate (PPI) was extracted by alkali dissolution and acid precipitation from defatted peanut flour. The effects of extraction conditions on the denaturation and functional properties of PPI were investigated. In comparison with native peanut protein (NPP) which was extracted by ammonium sulfate, the PPI extracted by alkali dissolution and acid precipitation had a higher extent of denaturation. Arachin was affected more easily by the extraction process than conarachin and led to a noticeable decrease of thermal stability of PPI. PPI contained much lower sulfhydryl and disulfide bond contents than NPP. The analyses of intrinsic fluorescence spectra indicated a more compacted tertiary conformation of NPP than PPI. Extraction process influenced the functional properties of PPI, such as protein solubility, emulsifying activity index and foaming capacity. The relatively poor functional properties of PPI might be associated with protein denaturation/unfolding and subsequent protein aggregation.

Industrial relevance

Peanut is an important oilseed crop and a well-accepted food. After oil production through thermal treatment, the defatted peanut flour is the main byproduct, which possesses a large amount of proteins. However, due to the low extraction yield and poor functional properties of these proteins, they are not well utilised in industry till now. In this work, peanut proteins were extracted by two techniques. The results indicated that extraction technique could significantly modify the functional properties of peanut proteins. Therefore, this work is helpful for industrial utilisation of peanut proteins.     

Characterization of hyacinth bean (Lablab purpureus (L.) sweet) seeds from Indonesia and their protein isolate

Hyacinth bean (Lablab purpureus (L.) sweet) seeds from Indonesia were characterized for the purposes of usage as a protein source. Protein isolate was prepared from the seeds using an isoelectric method, which was also used to characterize the physicochemical and functional properties. Hyacinth bean seeds have a moderate concentration of protein (17.1 ± 1.5%), and low concentration of HCN (1.1 ± 0.1 mg/100 g). However, before using the seeds as food, some treatments are needed to reduce their anti-nutritional factors, since the contents of trypsin inhibitor and phytate are 0.15 ± 0.02 TIU/mg and 18.9 ± 0.2 mg/g, respectively. Using the isoelectric preparation, the yield of protein isolate was low (7.38 ± 0.2 g per 100 g of the seeds), but the protein isolate had good colour, neutral odour, high protein content (89.8 ± 0.82%), and low ash (2.97 ± 0.36%). The protein isolate also had good functional properties, such as solubility, foaming capacity, and emulsifying activity. However, the foaming and emulsifying stabilities were low.     

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.     

Effect of frozen storage on lipids and functional properties of proteins of dressed Indian oil sardine (Sardinella longiceps)

Changes occuring in lipids and functional properties of dressed oil sardine during storage at −20°C (±2°C) were investigated for 12 weeks. Significant (P 0.05) changes were observed in the lipids and functional properties of frozen stored oil sardine meat. The extent of lipid oxidation and hydrolysis was strongly associated with decreased protein solubility (P0.01). Decrease in protein solubility (PS) positively correlated (P0.05) with the decrease in emulsifying capacity (EC), relative viscosity (RV) of soluble protein extracts, water binding capacity and negatively correlated with the cook loss. A positive correlation (P0.001) was established between the PS and the ability of soluble proteins to emulsify and stabilise an emulsion. High positive correlation between SSP & EC (P0.001) and PS & EC (P0.001) revealed that myofibrillar proteins are the main protein that decide the emulsion properties.     

Influence of acetylation on physicochemical, functional and thermal properties of potato and cassava starches

Starches were isolated from cassava (Manihot esculenta) and potato (Solanum tuberosum) tubers. They were further modified by acetylation. The physicochemical, functional and thermal properties of native and modified starches, prepared using acetic anhydride at different times (10 and 20 min) were compared. Potato starch (Sipiera/20) showed higher acetyl percentage and degree of substitution values than cassava (2425/20) starch when acetylated for 20 min. Proximate analysis revealed that the acetylated starches retained more moisture than the native ones. Above 75 °C, acetylation improved the water binding capacity of the native cassava starch; the same trend was observed for potato starch from 60 to 90 °C after acetylation. The X-ray powder diffraction patterns derived from acetylated potato starches were similar to its native form, which was expected as B-type pattern; the same trend was observed for modified cassava starch. However the modified starches showed increased crystalline index.     

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.     

Effects of konjac glucomannan on physicochemical properties of myofibrillar protein and surimi gels from grass carp (Ctenopharyngodon idella)

The cryoprotective effect of konjac glucomannan (KGM) on myofibrillar protein from grass carp (Ctenopharyngodon idella) during frozen storage at −18 °C and the influence of five levels of KGM (0%, 0.5%, 1%, 1.5%, and 2%) on texture properties, water-holding capacity, and whiteness of grass carp surimi gels were investigated. KGM as a novel cryoprotectant could significantly mitigate the decrease in salt extractable protein (SEP), Ca²⁺-ATPase activity, and total sulphydryl and active sulphydryl contents of myofibrillar protein during frozen storage. KGM at the level of 1% showed the same good cryoprotective effect as a conventional cryoprotectant (10% sucrose–sorbitol, 1:1, w/w). As the levels of KGM increased, breaking force and deformation of grass carp surimi gels increased significantly. Water-holding properties of the surimi gels are improved with the increasing addition of KGM, but the whiteness decreased and the colour became darker. The optimum addition level of KGM was suggested to be 1%.     

Isolation and structural properties of the major protein fraction in Australian wattle seed (Acacia victoriae Bentham)

The major protein fraction of wattle (Acacia victoriae Bentham) seed was isolated by anion-exchange and gel permeation chromatography. The protein was then characterised by its amino acid composition, gel electrophoresis, fluorimetry and circular dichroism (CD) in order to elucidate its nature and structural properties. The major amino acids were found to be glutamate (14.4%), aspartate (11.1%) and lysine (9.13%) while the contents of sulphur-containing amino acids (cysteine and methionine) and tryptophan were very low. The native protein, with an isoelectric point of 6.85, was comprised of two subunits of molecular masses 62 and 125 kDa, the bigger unit being joined by at least one disulphide bond. Far-UV-CD spectra showed that the protein consisted mainly of equal amounts of β-sheets and random structures (39% each), about 19% β-turns and relatively little α-helix (3.6%). These structures were also found to be very stable to changes in pH (3–9), temperature and ionic strength. Based on the fluorescence emission and near-UV-CD data, however, the tertiary structure was more sensitive to pH, temperature and ionic strength.     

Effects of pulsed electric fields on physicochemical properties of soybean protein isolates

Effects of pulsed electric fields (PEF) treatment (0-547 μs and 0-40 kV/cm) on physicochemical properties of soybean protein isolates (SPI) were studied. Solubility, surface free sulfhydryls (SH_F) and hydrophobicity of SPI dispersions (20 mg/ml) increased with the increment of the PEF strength and treatment time at constant pulse width 2 μs, pulse frequency 500 pulse per second (pps) and sample flow rate (1 ml/s). When the PEF strength and treatment time were above 30 kV/cm and 288 μs, solubility, surface SH_F, and hydrophobicity of SPI decreased due to denaturation and aggregation of SPI by hydrophobic interactions and disulfide bonds. Size-exclusion chromatography and laser light scattering analyses demonstrated further that stronger PEF treatment-induced dissociation, denaturation and reaggregation of SPI. Circular dichroism analysis showed that PEF treatment did not produce significant secondary structure changes of SPI. These results suggested that controlled PEF could be applied to process liquid food including soybean protein ingredient and to modify their structure and function in order to get desired products.     

Influence of heating,protein and glycerol concentrations of film-forming solution on the film properties of Argentine anchovy (Engraulis anchoita) protein isolate

This study was conducted to evaluate the influence of thermal treatment (74, 82, and 90 °C), glycerol (30%, 35%, and 40%, w/w) and protein concentrations (3.0%, 3.5%, and 4.0% w/w) of film-forming solution on the properties of Argentine anchovy (Engraulis anchoita) protein isolate (API) films produced by casting. The API presented 88.8% of proteins, 5.5% moisture, 1.3% lipids, 1.0% ash and 53.3% of polar amino acids. The DSC of protein isolate was observed at maximum temperature of 62.2 °C and ΔH 6.4 J/g. The thickness, water vapor permeability, color difference and opacity of the films were not affected by the experimental variables studied (p > 0.05). The lowest solubility, elongation, and highest tensile strength of the films occurred at low temperature, low protein and glycerol concentrations (p < 0.05). Micrographs obtained by scanning electron microscopy of the films showed homogeneous surfaces at low temperature.     

Effect of thermal treatments on functional properties of cress seed (Lepidium sativum) and xanthan gums: A comparative study

Foods are generally subjected to thermal treatments during processing operations, which affect on the functional properties of hydrocolloid solutions. In this paper, the effect of different thermal conditions (60 °C-30 min, 80 °C-23 min, 100 °C-18 min and 121 °C-15 min) on functional properties (rheological, emulsifying and foaming properties) of cress seed gum and xanthan gum were investigated. The results demonstrated that cress seed gum solutions had desirable rheological, emulsifying and foaming properties. When the hydrocolloid samples were heated, an irreversible increase in viscosity of cress seed gum solutions was observed and as a result, the emulsification and foaming properties improved. Whereas, xanthan gum would not have the ability to stand against heat treatment and its viscosity decreased. Nevertheless, the viscosity values of xanthan gum solutions were always higher than cress seed gum in all conditions.     

Functional properties of fenugreek (Trigonella foenum graecum) protein concentrate

Proximate composition and physicochemical properties of a protein concentrate prepared from fenugreek seed were determined. The effects of pH and/or NaCl concentration on these properties were investigated. The protein content of fenugreek was found to be 28.4%. The crude fibre content was 9.3% and crude fat was 7.1%. The minimum protein solubility was observed at pH 4.5, which was 18.5%, while maximum protein solubility was observed at pH 11, which was 91.3%.     

Effect of some traditional processing operations on the functional properties of African breadfruit seed (Treculia africana) flour

The effect of germination, fermentation, roasting and defatting on the proximate composition, water absorption capacity (WAC), oil absorption capacity (OAC), foaming capacity (FC), foaming stability (FS), emulsion capacity (EC), emulsion stability (ES), packed bulk density (PBD), least gelation concentration (LGC) and protein solubility (PS) of breadfruit seed flour (BSF) was investigated. WAC, OAC, FC, EC, PBD and LGC obtained are 190-380%; 130.3-200.5%; 2.3-60.4%; 12.4-52.9%; 0.4-0.6 g/ml; 6-12% (w/v) and 200-420%; 176.4-320.6; 4.2-70.8%; 20.2-60.4%; 0.5-0.7 g/ml; 0.5-0.8% (w/v) in the full fat and defatted flours respectively. Foams were more stable in the untreated; least in fermented and roasted samples. Defatting improved the FC, FS and EC; roasting and fermentation reduced EC of full fat BSF; Processing and defatting had no effect on the PBD; roasting and germination increased LGC while defatting and fermentation reduced it. Full fat flours had the lowest PS at pH 4 and the highest at pH 8. Fermented full fat BS flour had the highest PS at pH 5 and 8. Defatted germinated, raw dried and roasted BSF had lowest PS at pH 4; PS of fermented BSF is lowest at pH 3 and highest at pH 2.     

Structure,physicochemical, and functional properties of protein isolates and major fractions from cumin (Cuminum cyminum) seeds

In this study, cumin protein isolates (CPI) and major protein fractions were extracted and separated from cumin seeds, their structure, physicochemical, and functional properties were investigated. Albumin (62.29%) and glutelin (25.16%) were the predominant protein fractions of cumin seeds. Glutamic acid (Glu) and aspartic acid (Asp) were the major amino acids of cumin proteins, whereas more hydrophobic and aromatic amino acids were predominantly found in chickpea protein isolates. Electrophoresis profiles indicated that CPI have more disulphide bonds than major protein fractions. The intrinsic fluorescence data revealed that glutelin displayed greater exposure of tyrosine (Tyr) and tryptophan (Trp) residues compared to albumin and CPI. Circular dichroism (CD) data showed CPI presented more α-helix (14.4%) and less β-strand (30.7%) than albumin and glutelin. The atomic force microscope (AFM) profile and hydrodynamic diameter (D_h) determination showed the presence of low particle size in albumin fractions. Differences in the hydrophobicity (H_o) and the zeta-potential (ζ) of CPI, albumin, and glutelin were also observed due to their difference in structure and amino acid composition. Compared with CPI and glutelin, albumin exhibited the highest emulsifying activity (103.67 m²/g) and stability (42.84 min) and the smallest emulsion particle size (4.29 μm). The CPI, albumin and glutelin presented typical U-shaped protein solubility–pH curves, with the lowest solubility at pH 4.0. Rheological investigation demonstrated that CPIs were efficient in forming a gel at 80.6°C, whereas glutelin could form the hardest gel at 92.6°C. The overall results suggested that the cumin proteins can be a promising protein source for the food industry.     

Effect of micronisation temperature (130 and 170 °C) on functional properties of cowpea flour

Functional properties of cowpea flour from seeds micronised at two different surface temperatures (130 and 170 °C) were studied. Micronisation (130 and 170 °C) significantly (P ? 0.05) increased the water absorption capacity and least gelation concentration of the flour. The treatment significantly (P ? 0.05) reduced the water solubility and swelling indices, gel strength and foaming capacity of the flour. The changes in cowpea flour functional properties, such as the loss of foaming capacity in flours from micronised (130 and 170 °C) seeds, were associated with significant (P ? 0.05) increase in the surface hydrophobicity and cross-linking of the cowpea protein. SDS–PAGE of the protein-rich fractions revealed changes in the protein subunit profile which included the formation of disulphide bonds and possibly Maillard cross-links. The flour from M-170 °C seeds was significantly (P ? 0.05) darker than was the flour from unmicronised and M-130 °C seeds.     

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.