Physicochemical Properties Of Proteins Research Articles

Post-Translational Protein Modifications of Rare and Unconventional Types: Implications in Functions and Diseases.

Protein post-translational modification (PTM) occurs following their biosynthesis and is a key cellular event that defines their ultimate functional properties. It is an important control mechanism for display of biological functions of proteins often in a profound manner. It may switch on or off a protein's function. Several studies have been conducted to understand their mechanisms, physiological pathways and functional properties. PTMs have been shown to alter structural, conformational and physicochemical properties of proteins. So far a variety of protein modifications have been detected in physiological systems. These involve covalent modifications of amino acids via their side chains, backbone peptide bonds and terminal moieties. Following PTM, proteins may become (a) pathologically toxic, (b) biologically active or inactive, (c) more or less susceptible to proteolytic processing, (d) increasingly/decreasingly bound to its partner protein/s, or (e) modified with altered protease activities. These changes may affect pathways linked to cell signaling/transduction, trafficking, storing, expression, binding and/or affinity. Any of these events may be linked to metabolic, growth and/or chronic dysfunctions with serious health consequences that may include cancer, cardiovascular disease, stroke, viral/bacterial/parasite infections, inflammation, thrombosis, diabetes; central nervous system related conditions. Some of the modifications are more prevalent physiologically and widely studied. However, in recent years additional PTMs have been described that are less common. These include glypiation, neddylayion, siderophorylation, sumoylation, AMPylation, Cholesteroylation and others which are also important. This manuscript provides a comprehensive review of these rare and unconventional types of protein modifications and their functional implications to health, metabolism and disease conditions.

Sample Preparation Approaches for iTRAQ Labeling and Quantitative Proteomic Analyses in Systems Biology.

Among a variety of global quantification strategies utilized in mass spectrometry (MS)-based proteomics, isobaric tags for relative and absolute quantitation (iTRAQ) are an attractive option for examining the relative amounts of proteins in different samples. The inherent complexity of mammalian proteomes and the diversity of protein physicochemical properties mean that complete proteome coverage is still unlikely from a single analytical method. Numerous options exist for reducing protein sample complexity and resolving digested peptides prior to MS analysis. Indeed, the reliability and efficiency of protein identification and quantitation from an iTRAQ workflow strongly depend on sample preparation upstream of MS. Here we describe our methods for: (1) total protein extraction from immortalized cells; (2) subcellular fractionation of murine tissue; (3) protein sample desalting, digestion, and iTRAQ labeling; (4) peptide separation by strong cation-exchange high-performance liquid chromatography; and (5) peptide separation by isoelectric focusing.

Concentrated protein body product derived from rice endosperm as an oral tolerogen for allergen-specific immunotherapy--a new mucosal vaccine formulation against Japanese cedar pollen allergy.

The endoplasmic reticulum-derived type-I protein body (PB-I) from rice endosperm cells is an ideal candidate formulation for the oral delivery of bioencapsulated peptides as tolerogens for allergen-specific immunotherapy. In the present study, PBs containing the deconstructed Japanese cedar pollen allergens Cryptomeria japonica 1 (Cry j 1) and Cry j 2 were concentrated by treatment with thermostable α-amylase at 90°C to remove the starch from milled rice powder, which resulted in a 12.5-fold reduction of dry weight compared to the starting material. The modified Cry j 1 and Cry j 2 antigens in this concentrated PB product were more resistant to enzymatic digestion than those in the milled seed powder despite the absence of intact cell wall and starch, and remained stable for at least 10 months at room temperature without detectable loss or degradation. The high resistance of these allergens could be attributed to changes in protein physicochemical properties induced by the high temperature concentration process, as suggested by the decreased solubility of the antigens and seed proteins in PBs in step-wise-extraction experiments. Confocal microscopy showed that the morphology of antigen-containing PB-Is was preserved in the concentrated PB product. The concentrated PB product induced specific immune tolerance against Cry j 1 and Cry j 2 in mice when orally administered, supporting its potential use as a novel oral tolerogen formulation.

Dissociation and reduction of covalent β-lactoglobulin–quinone adducts by dithiothreitol, tris(2-carboxyethyl)phosphine, or sodium sulfite

Covalent protein–phenol adducts, generated by reaction of protein nucleophiles with quinones, have recently attracted increased attention because the interactions change the functionality and physicochemical properties of proteins in biological and food systems. The formation of such covalent adducts between β-lactoglobulin (β-LG) and the quinone of 4-methylcatechol, 4-methylbenzoquinone (4MBQ), and subsequent reduction by dithiothreitol (DTT), tris(2-carboxyethyl)phosphine (TCEP), or sodium sulfite was investigated by mass spectrometry. The results showed that 19.0±8.8% of β-LG reacted with 4MBQ when present in equimolar ratio at 20°C (pH 8.0) to yield the protein–phenol adduct (β-LG-Q). Following treatment with sulfite, DTT, or TCEP, 75, 68, or 36%, respectively, of the formed β-LG-Q adduct dissociated. Different reaction mechanisms were proposed for the reduction of β-LG and β-LG-Q by each of the reducing agents. These results show that on reductive sample preparation for analysis of protein samples, not only are protein polymers formed through oxidative disulfide bonds reduced into the individual protein constituents but also a large part of any protein–phenol adducts present will dissociate and, thus, give a false picture of the level of protein–protein interactions that have occurred in the sample.

Head to Head Comparison of the Formulation and Stability of Concentrated Solutions of HESylated versus PEGylated Anakinra

Although PEGylation of biologics is currently the gold standard for half-life extension, the technology has a number of limitations, most importantly the non-biodegradability of PEG and the extremely high viscosity at high concentrations. HESylation is a promising alternative based on coupling to the biodegradable polymer hydroxyethyl starch (HES). In this study, we are comparing HESylation with PEGylation regarding the effect on the protein's physicochemical properties, as well as on formulation at high concentrations, where protein stability and viscosity can be compromised. For this purpose, the model protein anakinra is coupled to HES or PEG by reductive amination. Results show that coupling of HES or PEG had practically no effect on the protein's secondary structure, and that it reduced protein affinity by one order of magnitude, with HESylated anakinra more affine than the PEGylated protein. The viscosity of HESylated anakinra at protein concentrations up to 75 mg/mL was approximately 40% lower than that of PEG-anakinra. Both conjugates increased the apparent melting temperature of anakinra in concentrated solutions. Finally, HESylated anakinra was superior to PEG-anakinra regarding monomer recovery after 8 weeks of storage at 40°C. These results show that HESylating anakinra offers formulation advantages compared with PEGylation, especially for concentrated protein solutions.

Protein Tertiary Structure Classification based on its Physicochemical property using Neural Network and KPCA-SVM: A Comparative Study

Proteins are one of the most important molecules in living organisms so they play a vital structural role in the cells of living organism. They are constructed of several polypeptide chains of amino acids, which fold into complex tertiary Structure. The knowledge of the protein function is directly dependent on its three dimensional (tertiary) structure. The Physicochemical properties of proteins always guide to determine the quality of the protein tertiary structure. Therefore it has been rigorously used to distinguish native or native like structure from other predicted structure. The experiments were conducted on the CASP dataset to classify RMSD (target class) near to native protein tertiary structure or not. Kernel principal component analysis (KPCA) is used for feature extraction since it performs better than PCA on protein tertiary structure dataset due to their nonlinear structures. The proposed model compare with neural network classification method. The experiments conducted shows that support vector machine combined with KPCA feature extraction performs better than neural network classifier. More than our results show better performance in Gaussian KPCA feature extraction with respect to other kernels.

An Interpretation of the Ancestral Codon from Miller's Amino Acids and Nucleotide Correlations in Modern Coding Sequences.

Purine bias, which is usually referred to as an “ancestral codon”, is known to result in short-range correlations between nucleotides in coding sequences, and it is common in all species. We demonstrate that RWY is a more appropriate pattern than the classical RNY, and purine bias (Rrr) is the product of a network of nucleotide compensations induced by functional constraints on the physicochemical properties of proteins. Through deductions from universal correlation properties, we also demonstrate that amino acids from Miller’s spark discharge experiment are compatible with functional primeval proteins at the dawn of living cell radiation on earth. These amino acids match the hydropathy and secondary structures of modern proteins.

AFM-based technologies as the way towards the reverse Avogadro number

Achievement of the concentration detection limit for proteins at the level of the reverse Avogadro number determines the modern development of proteomics. In this review, the possibility of approximating the reverse Avogadro number by using nanotechnological methods (AFM-based fishing with mechanical and electrical stimulation, nanowire detectors, and other methods) are discussed. The ability of AFM to detect, count, visualize and characterize physico-chemical properties of proteins at concentrations up to 10(-17)-10(-18) M is demonstrated. The combination of AFM-fishing with mass-spectrometry allows the identification of proteins not only in pure solutions, but also in multi-component biological fluids (serum). The possibilities to improve the biospecific fishing efficiency by use of SOMAmers in both AFM and nanowire systems are discussed. The paper also provides criteria for evaluation of the sensitivity of fishing-based detection systems. The fishing efficiency depending on the detection system parameters is estimated. The practical implementation of protein fishing depending on the ratio of the sample solution volume and the surface of the detection system is discussed. The advantages and disadvantages of today's promising nanotechnological protein detection methods implemented on the basis of these schemes.

Understanding without Reading: Analogue Encoding of Physicochemical Properties of Proteins in their Cognate Messenger RNA

Being related by the genetic code, messenger RNAs (mRNAs) and cognate proteins are polymers with mutually interdependent compositions, which further implies the possibility of a direct connection between their general physicochemical properties. How efficiently do different characteristics of mRNA coding regions reflect the features of cognate proteins and is it possible for the cell to obtain information about proteins from their mRNAs without first reading them on the ribosome? We address these issues in a theoretical proteome-wide analysis and show that average protein hydrophobicity, calculated from either sequences or 3D structures, can be encoded in an analogue fashion by many different mRNA sequence properties with the only constraint being that pyrimidine and purine bases be clearly distinguishable on average [1]. Moreover, average characteristics of mRNA sequences allow for a reasonable discrimination between human proteins with different cellular localization and, in particular, cytosolic and membrane proteins, even in the absence of topogenic signal-based mechanisms. We discuss our findings in the context of protein and mRNA localization and propose that this cellular process may be partly determined by basic physicochemical rationales and interdependencies between the two biomolecules. [1] Polyansky AA, Hlevnjak M, Zagrovic B. (2013) Nat. Commun. 4, 2784.

Citrullination – small change with a great consequence

Citrullination is one of the possible post-translational modifications of proteins. It is based on a conversion of L-arginine residue (L-Arg) to L-citrulline residue (L-Cit). The reaction is catalyzed by peptidylarginine deiminases (PAD). The change of L-Arg imino moiety results in a loss of a positive charge. This slight modification can contribute to significant changes in physicochemical properties of proteins, which may also cause a change of their functions. Citrullination is the modification observed in physiological processes such as epidermal keratinization, regulation of gene expression and the reorganization of myelin sheaths. The changes in the efficacy of citrullination may contribute to the pathogenesis of many different diseases including: psoriasis, multiple sclerosis, rheumatoid arthritis and cancer.

Extraction and physicochemical properties of soya bean protein and oil by a new reverse micelle system compared with other extraction methods

SummaryReverse micelle extraction is a novel technology for the separation of plant components such as proteins and oil. In this study, sodium bis(2‐ethylhexyl) sulphosuccinate (AOT) reverse micelle system and AOT/Tween 85 reverse micelle system were used to extract soya bean protein and oil from soya bean flour. The physicochemical properties of the protein and oil extracted were investigated and compared with traditional extraction methods. The results showed that the efficiency of forward extraction of soya bean protein using an AOT/Tween 85 reverse micelle system was superior to that using an AOT reverse micelle system at the optimal extraction conditions. In addition, soya bean proteins extracted using reverse micelle extraction had no unordered structure under Fourier transform infrared spectroscopy. The acid and peroxide values of oil products from two reverse micelle extractions were lower than that from immersion. The results indicated that AOT/Tween 85 reverse micelle system is effective in extracting soya bean protein and oil.

Identification and characterization of plastid-type proteins from sequence-attributed features using machine learning

BackgroundPlastids are an important component of plant cells, being the site of manufacture and storage of chemical compounds used by the cell, and contain pigments such as those used in photosynthesis, starch synthesis/storage, cell color etc. They are essential organelles of the plant cell, also present in algae. Recent advances in genomic technology and sequencing efforts is generating a huge amount of DNA sequence data every day. The predicted proteome of these genomes needs annotation at a faster pace. In view of this, one such annotation need is to develop an automated system that can distinguish between plastid and non-plastid proteins accurately, and further classify plastid-types based on their functionality. We compared the amino acid compositions of plastid proteins with those of non-plastid ones and found significant differences, which were used as a basis to develop various feature-based prediction models using similarity-search and machine learning.ResultsIn this study, we developed separate Support Vector Machine (SVM) trained classifiers for characterizing the plastids in two steps: first distinguishing the plastid vs. non-plastid proteins, and then classifying the identified plastids into their various types based on their function (chloroplast, chromoplast, etioplast, and amyloplast). Five diverse protein features: amino acid composition, dipeptide composition, the pseudo amino acid composition, Nterminal-Center-Cterminal composition and the protein physicochemical properties are used to develop SVM models. Overall, the dipeptide composition-based module shows the best performance with an accuracy of 86.80% and Matthews Correlation Coefficient (MCC) of 0.74 in phase-I and 78.60% with a MCC of 0.44 in phase-II. On independent test data, this model also performs better with an overall accuracy of 76.58% and 74.97% in phase-I and phase-II, respectively. The similarity-based PSI-BLAST module shows very low performance with about 50% prediction accuracy for distinguishing plastid vs. non-plastids and only 20% in classifying various plastid-types, indicating the need and importance of machine learning algorithms.ConclusionThe current work is a first attempt to develop a methodology for classifying various plastid-type proteins. The prediction modules have also been made available as a web tool, PLpred available at http://bioinfo.okstate.edu/PLpred/ for real time identification/characterization. We believe this tool will be very useful in the functional annotation of various genomes.

The effects of low salt concentrations on the mechanism of adhesion between two pieces of pork semimembranosus muscle following tumbling and cooking

The aim of this research was to gain deeper insight into the effect of salt content on the adhesion between pieces of semimembranosus pork muscle bound by a tumbling exudate gel. Hydrophobic site number, free thiol and carbonyl content were measured in tumbling exudate and meat protein to evaluate the protein–protein interactions involved in the adhesion process. Proteins were far more oxidized in exudate than in meat, and under our experimental conditions, salt content increased protein bonding in the exudate but not in the meat. Breaking stress increased between non-salted meat and 0.8%-salted meat but did not depend on the protein physicochemical properties of the tumbling exudate. Modifying the meat surface by tumbling alone, tumbling and salting, or scarification had no effect on breaking stress. It is suggested that the break between the meat pieces occurred between the tumbling exudate and the meat surface due to weaker chemical bonds at this location.

Effect of pre-harvest sprouting on physicochemical changes of proteins in wheat

High moisture before harvest can cause sprouting of the wheat kernel, which is termed pre-harvest sprouting (PHS). The aim of this study was to examine the variation in physicochemical properties of proteins in PHS-damaged (sprouted) hard red and white spring wheat genotypes. Specifically, protein content, enzyme activity and degradation of proteins were evaluated in sound and PHS-damaged wheat. Protein contents of sprouted wheat samples were lower than that of non-sprouted samples; however, their differences were not significantly (P > 0.05) correlated with sprouting score. Sodium dodecyl sulfate (SDS) buffer extractable proteins (EXP) and unextractable proteins (UNP) were analyzed by high-performance size exclusion chromatography. PHS damage elevated endoprotease activity and consequently increased the degradation of polymeric UNP and free asparagine concentration in wheat samples. Free asparagine is known to be a precursor for formation of carcinogenic acrylamide during high heat treatment, such as baking bread. Free asparagine content had significant correlations (P < 0.01) with sprouting score, endoprotease activity and protein degradation. Genotypes with higher endoprotease activity tend to exhibit a larger degree of degradation of UNP and higher free asparagine concentration in sprouted wheat samples.

Application of Intelligent Techniques for Classification of Bacteria Using Protein Sequence-Derived Features

Standard molecular experimental methodologies and mathematical procedures often fail to answer many phylogeny and classification related issues. Modern artificial intelligent-based techniques, such as radial basis function, genetic algorithm, artificial neural network, and support vector machines are of ample potential in this regard. Reliance on a large number of essential parameters will aid in enhanced robustness, reliability, and better accuracy as opposed to single molecular parameter. This study was conducted with dataset of computed protein physicochemical properties belonging to 20 different bacterial genera. A total of 57 sequential and structural parameters derived from protein sequences were considered for the initial classification. Feature selection based techniques were employed to find out the most important features influencing the dataset. Various amino acids, hydrophobicity, relative sulfur percentage, and codon number were selected as important parameters during the study. Comparative analyses were performed applying RapidMiner data mining platform. Support vector machine proved to be the best method with maximum accuracy of more than 91%.

Improved classification of lung cancer tumors based on structural and physicochemical properties of proteins using data mining models.

Detecting divergence between oncogenic tumors plays a pivotal role in cancer diagnosis and therapy. This research work was focused on designing a computational strategy to predict the class of lung cancer tumors from the structural and physicochemical properties (1497 attributes) of protein sequences obtained from genes defined by microarray analysis. The proposed methodology involved the use of hybrid feature selection techniques (gain ratio and correlation based subset evaluators with Incremental Feature Selection) followed by Bayesian Network prediction to discriminate lung cancer tumors as Small Cell Lung Cancer (SCLC), Non-Small Cell Lung Cancer (NSCLC) and the COMMON classes. Moreover, this methodology eliminated the need for extensive data cleansing strategies on the protein properties and revealed the optimal and minimal set of features that contributed to lung cancer tumor classification with an improved accuracy compared to previous work. We also attempted to predict via supervised clustering the possible clusters in the lung tumor data. Our results revealed that supervised clustering algorithms exhibited poor performance in differentiating the lung tumor classes. Hybrid feature selection identified the distribution of solvent accessibility, polarizability and hydrophobicity as the highest ranked features with Incremental feature selection and Bayesian Network prediction generating the optimal Jack-knife cross validation accuracy of 87.6%. Precise categorization of oncogenic genes causing SCLC and NSCLC based on the structural and physicochemical properties of their protein sequences is expected to unravel the functionality of proteins that are essential in maintaining the genomic integrity of a cell and also act as an informative source for drug design, targeting essential protein properties and their composition that are found to exist in lung cancer tumors.

Changes in physicochemical properties of proteins in Kayserian Pastirma made from the M. semimembranosus muscle of cows during traditional processing

In the current study, we examined the effects of beef processing to produce pastirma on the physicochemical properties of proteins in M. semimembranosus (SEM) muscle. Protein concentrations significantly increased in pastirma muscles (P<0.01), as a result of the salting and curing process. The surface hydrophobicity values of processed samples were higher than those without processing at all guanidine-HCl concentrations, suggesting hydrophobicity increased, which may attribute to the new generated peptides during the traditional pastirma-making process. The metmyoglobin content greatly increased (by as much as 89%) in pastirma samples compared with the unprocessed samples. The images of histology also demonstrate that the pastirma processing had no negative impact on the structure of the muscle. The results from this study suggest that the traditional pastirma-making process catalyzed the enzymatic digestion of muscle proteins, and the differences in some physicochemical parameters between the control and pastirma samples were thus likely to be contributable to protein digestion. Thus, the traditional pastirma-making process results in the degradation of many proteins into peptides, which might then be obtainable as functional components to treat human diet- and lifestyle-related diseases such as hypertension, hyperglycemia syndromes or to be used as nutraceuticals.

Natural proteins: Sources, isolation, characterization and applications

Worldwide, plant protein contributes substantially as a food resource because it contains essential amino acids for meeting human physiological requirements. However, many versatile plant proteins are used as medicinal agents as they are produced by using molecular tools of biotechnology. Proteins can be obtained from plants, animals and microorganism cells. The abundant economical proteins can be obtained from plant seeds. These natural proteins are obtained by isolation procedures depending on the physicochemical properties of proteins. Isolation and purification of single protein from cells containing mixtures of unrelated proteins is achievable due to the physical and chemical attributes of proteins. The following characteristics are unique to each protein: Amino acid composition, sequence, subunit structures, size, shape, net charge, isoelectric point, solubility, heat stability and hydrophobicity. Based on these properties, various methods of isolation exist, like salting out and isoionic precipitation. Purification of proteins is quiet challenging and, therefore, several approaches like sodium dodecyl sulfate gel electrophoresis and chromatography are available. Characterization of proteins can be performed by mass spectrometry/liquid chromatography-mass spectrometry (LC-MS). The amino acid sequence of a protein can be detected by using tandem mass spectrometry. In this article, a review has been made on the sources, isolation, purification and characterization of natural proteins.

Controlled intra- and transdermal protein delivery using a minimally invasive Erbium:YAG fractional laser ablation technology

The aim of the study was (i) to investigate the feasibility of using fractional laser ablation to create micropore arrays in order to deliver proteins into and across the skin and (ii) to demonstrate how transport rates could be controlled by variation of poration and formulation conditions. Four proteins with very different structures and properties were investigated – equine heart cytochrome c (Cyt c; 12.4kDa), recombinant human growth hormone expressed in Escherichia coli (hGH; 22kDa), urinary follicle stimulating hormone (FSH; 30kDa) and FITC-labelled bovine serum albumin (FITC-BSA; 70kDa). The transport experiments were performed using a scanning Er:YAG diode pumped laser (P.L.E.A.S.E.®; Precise Laser Epidermal System). The distribution of FITC-BSA in the micropores following P.L.E.A.S.E.® poration was visualised by using confocal laser scanning microscopy (CLSM). Porcine skin was used for the device parameter and CLSM studies; its validity as a model was confirmed by subsequent comparison with transport of Cyt c and FITC-BSA across P.L.E.A.S.E.® porated human skin. No protein transport (deposition or permeation) was observed across intact skin; however, P.L.E.A.S.E.® poration enabled total delivery after 24h of 48.2±8.9, 8.1±4.2, 0.2±0.1 and 273.3±30.6μg/cm2 for Cyt c, hGH, FSH and FITC-BSA, respectively, using 900 pores/135.9cm2. Calculation of permeability coefficients showed that there was no linear dependence of transport on molecular weight ((1.6±0.3), (0.1±0.05), (0.08±0.03) and (0.9±0.1)×10−3cm/h, for Cyt c, hGH, FSH and FITC-BSA, respectively); indeed, a U-shaped curve was observed. This suggested that molecular weight was not a sufficiently sensitive descriptor and that transport was more likely to be determined by the surface properties of the respective proteins since these would govern interactions with the local microenvironment. Increasing pore density (i.e. the number of micropores per unit area) had a statistically significant effect on the cumulative permeation of both Cyt c (at 100, 150, 300 and 600pores/cm2, permeation was 11.2±2.4, 15.3±11.8, 33.8±10.5 and 51.2±15.8 4μg/cm2, respectively) and FITC-BSA (at 50, 100, 150 and 300pores/cm2, it was 58.5±15.3, 132.6±40.0, 192.7±24.4, 293.3±76.5μg/cm2, respectively). Linear relationships were established in both cases. However, only the delivery of FITC-BSA was improved upon increasing fluence (53.3±22.5, 293.3±76.5, 329.6±11.5 and 222.1±29.4μg/cm2 at 22.65, 45.3, 90.6 and 135.9J/cm2, respectively). The impact of fluence – and hence pore depth – on transport will depend on the relative diffusivities of the protein in the micropore and in the ‘bulk’ epidermis/dermis. Experiments with Cyt c and FSH confirmed that delivery was dependent upon concentration, and it was shown that therapeutic delivery of the latter was feasible. Cumulative permeation of Cyt c and FITC-BSA was also shown to be statistically equivalent across porcine and human skin. In conclusion, it was demonstrated that laser microporation enabled protein delivery into and across the skin and that this could be modulated via the poration parameters and was also dependent upon the concentration gradient in the pore. However, the role of protein physicochemical properties and their influence on transport rates remains to be elucidated and will be explored in future studies.

Composition of Proteins in Okara as a Byproduct in Hydrothermal Processing of Soy Milk

Protein quality, based on its subunit composition, in okara obtained as a byproduct during hydrothermal cooking of soy milk was assessed. The composition of 7S and 11S protein fractions was correlated with the physicochemical properties of protein in okara produced from six soybean varieties. The basic 7S globulin (Bg7S) and 11S protein were two main proteins in okara. Investigated soybean genotypes produced okara with mainly acidic A(5) and basic B(1,2,4) polypeptides of 11S proteins. Soybean 11S content was not an indicator of okara protein recovery or extractability. Of all tested relationships, extractable soluble protein content of okara was influenced only by soybean Bg7S (r = 0.86; p < 0.05) and its light subunit contents (r = 0.93; p < 0.05). Okara protein recovery depended on Bg7S heavy subunit content in soybeans (r = 0.81; p < 0.05). The high quantity of vegetable protein in okara (around 35%) and very high protein extractability (around 85%) qualify this byproduct for potential application in food preparation as a functional ingredient.