Relationship between protein characteristics and film‐forming properties of kidney bean,field pea and amaranth protein isolates

This study was undertaken to evaluate physicochemical (colour, protein content, ash content and zeta potential), structural (size exclusion chromatography and thermal properties) and film‐forming properties of kidney bean, field pea and amaranth protein isolates (KBPI, FPPI and AMPI, respectively). Protein content, ash content, zeta potential and denaturation temperature of the isolates ranged from 83.9 to 91.4%, 2.9 to 4.5%, ?37.3 to ?44.2 mV and 85.5 to 96.2 °C, respectively. Size exclusion chromatography revealed that globulins were prominent proteins in KBPI and FPPI, while AMPI contained both globulins and albumins as major fractions. FPPI showed the highest L* value (88.1), surface charge (zeta potential = –44.2 mV) and protein solubility (80.0–94.2%). Films were prepared from heated (90 °C for 20 min) and unheated protein dispersions of pH 7.0, 8.0 and 9.0 and evaluated for colour, opacity, tensile strength (TS), water‐solubilised matter (WSM) and water vapour permeability (WVP). FPPI films showed the most desirable properties in terms of the highest L* (87.5–90.5), TS (12.6–37.2 MPa) and the lowest opacity (7.1–8.4 A₆₀₀/mm). FT‐IR spectroscopic analysis of the films revealed that alkaline pH and heat treatment unfolded protein molecules. Alkaline pH reduced opacity, while heat treatment improved TS and water resistance (decreased WSM and WVP) of protein films, which varied with the protein isolates.     

Interfacial and emulsifying properties of amaranth (Amaranthus hypochondriacus) protein isolates under different conditions of pH

Amaranth proteins have adequate amino acid balance for substituting either partly or completely animal proteins in human nutrition. However, they present poor emulsifying properties in basic conditions corresponding to their extraction medium. Consequently their use in acidic conditions could be envisaged to better exploit their potentialities. To better understand their emulsifying properties we have studied their interfacial activities at pHs 2.0 and 8.0 and tried to make the link between 2D and 3D properties.Our results clearly demonstrate the better properties of AI at pH 2.0 than at pH 8 in terms of protein solubility, spreading, adsorption, viscoelastic properties of interfaces and emulsion stability. These results are in relation with the denaturated state of proteins at pH 2.0 where proteins form a harder interfacial film, as compared to pH 8.0. Thus the potential use of amaranth proteins in emulsifying applications should be oriented towards acidic applications.     

Polypeptide profile and functional properties of defatted meals and protein isolates of canola seeds

Laboratory‐defatted meals from four types of canola seeds were analysed for protein profile by reducing and non‐reducing forms of sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS‐PAGE). In the absence of a reducing agent (2‐mercaptoethanol), four major polypeptide bands (16, 18, 30 and 53 kDa) were prominent in similar ratios in all varieties. In the presence of mercaptoethanol, significant reductions in intensity of the major bands occurred, suggesting that the major polypeptides contained smaller units which were held together by disulphide bonds. Meals from Brassica napus seeds had higher protein solubilities than meals from Brassica rapa seeds. Meals with higher protein solubility values also had higher foaming capacity (FC) values. Generally, the acid‐precipitated (pH 4.0) protein isolates (APPIs) had higher FC values than the calcium‐precipitated isolates (CPPIs). On the other hand, the CPPIs formed emulsions with higher values of emulsifying activity index (EAI) when compared to the APPIs. The results indicate that variations in functional properties of protein isolates and meals between the four seed types were probably due to differences in protein conformation in aqueous solutions rather than differences in polypeptide composition. © 2001 Society of Chemical Industry     

Effects of high hydrostatic pressure on physicochemical and functional properties of walnut (Juglans regia L.) protein isolate

BACKGROUND: Walnut (Juglans regia L.) is a good source of protein that has potential application in new product formation and fortification. The main objectives of this study were to investigate the effects of high hydrostatic pressure (HHP) treatment (300–600 MPa 20 min) on physicochemical and functional properties of walnut protein isolate (WPI) using various analytical techniques at room temperature. RESULTS: The results showed significant modification of solubility, free sulfhydryl content and surface hydrophobicity with increased levels of HHP treatment, indicating partial denaturation and aggregation of proteins. Differential scanning calorimetry and fluorescence spectrum analyses demonstrated that HHP treatment resulted in gradual unfolding of protein structure. Emulsifying activity index was significantly (P < 0.05) increased after HHP treatment at 400 MPa, but significantly decreased (P < 0.05) relative to the untreated WPI with further increase in pressure. HHP treatment at 300–600 MPa significantly decreased emulsion stability index. Additionally, HHP‐treated walnut proteins showed better foaming properties and in vitro digestibility. CONCLUSION: These results suggest that HHP treatment could be applied to modify the properties of walnut proteins by appropriate of pressure levels, which will help in using walnut protein as a potential food ingredient. © 2012 Society of Chemical Industry     

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.     

Physicochemical, functional and angiotensin converting enzyme inhibitory properties of amaranth (Amaranthus hypochondriacus) 7S globulin

BACKGROUND: Amaranth 7S globulin is a minor globulin component and its impact on the properties of an amaranth protein ingredient depends on its proportion in the variety of amaranth being considered. Some physicochemical, functional and angiotesin I‐converting enzyme (ACE) inhibitory properties of amaranth vicilin were studied in this work and compared with the 11S globulin. RESULTS: Fluorescence spectroscopy results indicated that 7S globulin tryptophans were more exposed to the solvent and, by calorimetry, the 7S globulin denaturation temperature (T_d) was found lower than the 11S globulin T_d, suggesting a more flexible structure. The 7S globulin surface hydrophobicity was higher than that of the 11S globulin, which is in agreement with the better emulsifying properties of the 7S globulin. The solubility in neutral buffer of the 7S globulin (851 ± 25 g kg^?1) was also higher than that of the 11S globulin (195 ± 6 g kg^?1). Bioinformatic analyses showed the presence of ACE inhibitory peptides encrypted in 7S tryptic sequences and peptides released after in vitro gastrointestinal digestion showed a high ACE‐inhibitory capacity (IC₅₀ = 0.17 g L^?1), similar to that of 11S globulin peptides. CONCLUSION: Compared with the 11S globulin, the 7S globulin presents similar ACE inhibitory activity and some functional advantages, better solubility and emulsifying activity, which suits some food requirements. The functional behavior has been related with the structural properties. Copyright © 2011 Society of Chemical Industry     

Popping of amaranth grain (Amaranthus caudatus) and its effect on the functional,nutritional and sensory properties

The popping of amarunth grain (Amaranthus caudatus var INIAP‐Alegría) by hot air processing was studied. A household corn popper adapted to control heating and airflow was used. The effects of temperature, load, airflow and moisture on the popping capacity and on the functional properties, nutritional quality, crude protein content, lysine content and sensory texture of the poppei grain were investigate. The yield, expansion volume and density of popped grain showed that the optimal conditions for the popping process were 240 °C, 22 g load, 0.013 m³ s^?1 airflow and 12% grain moisture. The proportion of popped grain with butterfly shape was highest (p < 0.05) at 220 °C, 22 g load, 0.014 m³ s^?1 airflow and 14% grain moisture. The functional and physic‐chemical properties of popped grain obtained by various treatments showed completely gelatinised starch. The total, available and resistant starch contents were similar among the different treatments. The enzymatic degradation of starch was 65% within 5–15 min of incubation with α‐amylase. The crude protein content was almost 15% for all the treatments, while the total lysine content was 45.2–48.0 mg g^?1 protein. The in vitro availability of protein of popped grain obtained at 0.013 m³ s^?1 airflow and 14% grain moisture was above 84%. The highest available lysine value was found for popped grain obtained at 0.014 m³ s^?1 airflow, 18–22 g load and 12–14% grain moisture. However, six of the eight treatments had available lysine contents that varied between 41.2 and 47.4 mg g^?1 protein. Sensory analyses showed that the treatments with the highest popping capacity produced grains with high crunch and expansion capacities. © 2002 Society of Chemical Industry     

Application of ultrasound treatment for modulating the structural,functional and rheological properties of black bean protein isolates

The modulating effect of ultrasound treatments at varying powers and times on the structural and functional properties of black bean protein isolate (BBPI) was investigated. Compared with native BBPI, low-power (150 W) and medium-power (300 W) ultrasound treatments increased the solubility, foaming and emulsifying properties of BBPI, especially at 300 W, 24 min. This effect arises predominantly due to increased exposure of hydrophobic groups, which serve to increase the interactions between the protein and water molecules. Additionally, an increase in the protein surface activity improved the absorption of protein molecules at the oil–water and air–water interfaces. Rheology data showed that increased hydrophobic and hydrogen-bonding interactions improved the water-holding capacity of BBPI gels following ultrasound treatment. However, high-power (450 W) ultrasound treatment weakened the functional properties of BBPI, and this was likely due to the formation of macromolecular BBPI aggregates. Overall, this study indicates that ultrasound treatment could be a promising approach for modulating other plant protein resources as well as expanding the application of black bean protein.     

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.     

Effect of acid treatment on structural and foaming properties of soy amaranth protein mixtures

To obtain a food ingredient composed of soybean and amaranth proteins with better functionality, the proteins were subjected to an acid treatment followed by neutralization. The native and treated proteins, amaranth (A and TA), soybean (S and TS) and the 1:1 mixture (M and TM) were studied. The structural characteristics and surface tension and foaming properties of the proteins were analyzed.     

菜籽蛋白氨基酸组成分析及与功能特性的相关性研究

选用长江上游、中游和下游的30个菜籽品种的饼提取蛋白质,对蛋白质进行氨基酸组成和功能特性的研究.结果表明:菜籽蛋白中总氨基酸含量为68.67％～84.90％,其中中双11号(湖南)氨基酸总量最高,而丰油730号最低;30个菜籽蛋白中的氨基酸种类齐全,必需氨基酸占氨基酸总量的37％～38％,绝大部分样品的第一限制氨基酸是蛋氨酸,氨基酸比值系数分(SRC)为77.66～91.53.在营养分析的基础上,建立氨基酸组成与功能特性的相关性分析,分析结果为:亲水性氨基酸含量与乳化稳定性呈显著负相关,乳化性与乳化稳定性呈极显著负相关,可溶性蛋白含量与吸油性、吸水性、起泡性呈正相关.菜籽蛋白是营养价值很高的植物蛋白,可广泛应用于食品工业.     

紫苏分离蛋白的制备工艺研究

以脱脂紫苏粕为原料,采用碱溶酸沉法制备紫苏分离蛋白.研究了紫苏分离蛋白制备工艺条件,同时测定了产品的功能性质.通过单因素实验和正交实验得出紫苏分离蛋白制备的最佳工艺条件为:碱溶温度55℃,料液比1∶10,碱溶pH 10,碱溶时间60min/次(2次),酸沉pH 4.4.在此工艺条件下紫苏分离蛋白产品得率为24.5%,产品蛋白质含量为91.52%(N×6.25,干基).该产品的氮溶解指数为54.7%,持水性为3.57g/g,吸油性为1.67mL/g,乳化性为42%,乳化稳定性为95.24%.     

Physicochemical, thermal and functional characterisation of protein isolates from Kabuli and Desi chickpea (Cicer arietinum L.): a comparative study with soy (Glycine max) and pea (Pisum sativum L.)

BACKGROUND: Chickpea (Cicer arietinum L.) seeds are a good source of protein that has potential applications in new product formulation and fortification. The main objectives of this study were to analyse the physicochemical, thermal and functional properties of chickpea protein isolates (CPIs) and compare them with those of soy (SPI) and pea (PPI) protein isolates. RESULTS: Extracted CPIs had mean protein contents of 728–853 g kg^?1 (dry weight basis). Analysis of their deconvoluted Fourier transform infrared spectra gave secondary structure estimates of 25.6–32.7% α‐helices, 32.5–40.4% β‐sheets, 13.8–18.9% turns and 16.3–19.2% disordered structures. CPIs from CDC Xena, among Kabuli varieties, and Myles, among Desi varieties, as well as SPI had the highest water‐holding and oil absorption capacities. The emulsifying properties of Kabuli CPIs were superior to those of PPI and Desi CPIs and as good as those of SPI. The heat‐induced gelation properties of CPIs showed a minimum protein concentration required to form a gel structure ranging from 100 to 140 g L^?1. Denaturation temperatures and enthalpies of CPIs ranged from 89.0 to 92.0 °C and from 2.4 to 4.0 J g^?1 respectively. CONCLUSION: The results suggest that most physicochemical, thermal and functional properties of CPIs compare favourably with those of SPI and are better than those of PPI. Hence CPI may be suitable as a high‐quality substitute for SPI in food applications. Copyright © 2011 Society of Chemical Industry     

Relationship of hydrophobicity and solubility with some functional properties of cowpea (Vigna unguiculata) protein isolate

The relationship of hydrophobicity and solubility with some functional properties of cowpea protein isolate was determined. Cowpea protein isolate was prepared by alkali extraction followed by precipitation at pH 4.5. The precipitated proteins were then neutralized to pH 7. Heating of the protein isolate to 100°C for 10 min followed by cooling to room temperature resulted in a significant (P ≦ 0.05) decrease in aromatic hydrophobicity (ARH) when compared to the native protein isolate. The inclusion of sodium dodecyl sulfate (SDS) during heating gave a significant (P ≦ 0-05) 1.7-fold increase while inclusion of mercaptoethanol (ME) gave a significant (P ≦ 0.05) 2.5-fold increase in ARH of the cooled protein solution. Protein solubility (PS), foam expansion (FE) and emulsification activity index (EAI) of the isolate generally increased significantly (P ≦ 0.05) upon heating or treatment with urea or SDS or a combination of SDS and ME. Backward stepwise multiple regression was used to obtain equations for predicting emulsifying and foaming properties of the protein isolate from solubility and hydrophobicity parameters. PS, ARH and aliphatic hydrophobicity (ALH) were important in predicting foam stability and emulsion stability, while PS and ALH were important for predicting FE. ALH alone was important for predicting EAI.     

Some physicochemical and antinutritional properties of raw flours and protein isolates from Mucuna pruriens (velvet bean) and Canavalia ensiformis (jack bean)

The legumes Canavalia ensiformis and Mucuna pruriens are underexploited in tropical Mexico. Their seeds have good nutritional potential, but contain antinutritional factors. Physicochemical and antinutritional properties were determined for raw flours (RF) and protein isolates (PI) produced from these legumes. Protein content in the PI was 737 g kg^–1 for C. ensiformis and 666 g kg^–1 for M. pruriens. Protein isolation improved in vitro digestibility, while maintaining high lysine levels and adequate sulphur amino acids content. Antinutritional factors such as cyanogenic glucosides, cyanide precursors from hydrolysis, tannins and trypsin inhibitors were lower in the PIs than in the RFs. The reduction in canavanine levels, a structural analogue of arginine, in the C. ensiformis PI was noteworthy. These PIs thus have potential applications in the development of new food ingredients in tropical regions using processes that improve nutritional value.     

Functional properties of safflower protein isolates: Water absorption,whipping and emulsifying characteristics

Safflower meal defatted at the laboratory (SML) and safflower cake provided by an industrial plant (SMI) were used for protein isolation. Isolates were obtained by micellisation (MP) and isoelectric precipitation (IP) techniques. The functional properties studied with these isolates were water and fat absorption, foam expansion and stability, and emulsion activity and stability. Within the experimental conditions of this research, it was observed that the various treatments received previously by the safflower meal, for oil extraction, seemed to have comparatively minor effects on the functional performance of the protein isolates. Only in the case of SML, did the MP isolates have a higher water and fat absorption, and foam expansion than IP samples. For both SML and SMI, the emulsion stability of MP was higher than that of IP.     

改性大豆分离蛋白与肌原纤维蛋白共混体系乳化性及凝胶性研究

采用热改性、碱改性、超声改性及辐照改性4种方法将大豆分离蛋白进行改性处理,并建立改性大豆分离蛋白与肌原纤维蛋白共混体系,对其乳化性及凝胶性进行研究。结果表明经热改性的大豆分离蛋白与肌原纤维蛋白共混体系的乳化性及凝胶性有显著提高,其中乳化活性提高了12.6 m2/g,硬度和弹性分别增加了18.58 g和0.16 mm,持水性增加了22.14%。经碱改性的SPI对混合体系的乳化性和凝胶性影响次之,而经超声和辐照改性的大豆分离蛋白,只对共混体系的持水性和乳化稳定性有影响,对质构性和乳化活性影响不显著。     

Effects of microwave heating,steaming, boiling and baking on the structure and functional properties of quinoa (Chenopodium quinoa Willd.) protein isolates

The effects of microwave heating (MW), steaming (SM), boiling (BL) and baking (BK) on the structure and functional properties of quinoa protein isolates (QPI) were investigated. SDS-PAGE showed the 20–30 kDa band strength of QPI-BL was enhanced, which indicated the disulphide bond was broken and protein molecules dissociated. Due to the recombination of subunits, some large molecular weight or insoluble polymer components of QPI-SM and QPI-BK did not pass through the gel. Microwave heating and boiling showed negative effects for α-helix and positive effects for β-sheet, which implied the molecular structure was transformed from ordered to disordered, the secondary structure became loose. The reduction of free SH (sulfhydryl) and surface hydrophobicity implied that aggregation and cross-linking of protein molecules for QPI-SM and QPI-BK. QPI, QPI-MW and QPI-BL exhibited better solubility, which was related to the water holding capacity (WHC) and emulsification. For QPI-SM and QPI-BK, functional properties (including solubility, WHC and gel-forming ability) decreased due to molecular aggregation. Heat treatments significantly affect the structure and functional properties of QPI, the current research showed that microwave heating and boiling might be better heat treatment methods for QPI and would help the development of quinoa protein products.     

Composition and functional properties of hemp seed protein isolates from various hemp cultivars

Hemp seed protein isolates (HPI) were extracted from seven commercial hemp cultivars, a Cornell breeding line, and a commercial hemp heart product, and their composition and functional properties were investigated. HPI contained different ratios of edestin, vicilin, and albumin proteins, which affected protein solubility and functionality. Higher protein solubility was associated with cultivars that contained more vicilin and albumin, which influenced the subsequent functional properties of HPI. Significant differences in water holding capacity (0.83–1.05 g water/g protein isolate), oil holding capacity (1.28–1.81 g oil/g protein isolate), foam capacity (52.9%–84.9%), and foam stability (68.1%–89.4%) were observed across HPI. The Cornell hemp breeding line exhibited the highest protein solubility at pH 7.0 and was uniquely capable of forming an emulsion. The relationship identified between hemp seed protein composition and functionality, in conjunction with the demonstration of an on-going hemp breeding line, suggest that continued, targeted development of hemp cultivars can improve its seed protein functional properties for ingredient utilization in plant-based foods.