In situ examination of starch granule-soy protein and wheat protein interactions

The objective of this study was to evaluate the association between heat and pressure-treated soy proteins and wheat prime starch relative to the level of granule surface proteins present. Soy isolates were manufactured from defatted soy flour and from two types of textured soy flour. Conditions for binding between wheat starch and soy fractions were established by altering pH, protein and sucrose concentrations. Conformations of exogenous proteins bound to the wheat starch granule surface were evaluated using an amyloglucosidase assay. Proteins present on the granule surface were removed and soy protein binding was reevaluated. Thermal and pressure processing of soy protein significantly influenced binding kinetics. Textured soy proteins exhibited increased wheat starch granule adsorption characteristics compared to untreated soy protein. Removal of native wheat starch granule surface proteins decreased the binding of added proteins. This suggests that native granule proteins may mediate the binding of exogenous protein.     

DENATURATION OF PLANT PROTEINS RELATED TO FUNCTIONALITY AND FOOD APPLICATIONS. A Review

Proteins can be denatured by heat, changes in pH, organic solvents, detergents, urea, guanidine hydrochloride or other methods that modify the secondary, tertiary or quaternary structure, without breaking any covalent bonds. Physical-chemical measurements or functionality related to denaturation include solubility, viscosity, dissociation into subunits, sedimentation constant, optical rotation, association and ultraviolet spectra. The relationship between pH, temperature and rate of denaturation of wheat and soy proteins is complex. Optimum heat treatment of soy flakes, for example, inactivates nearly all biologically active components, but the protein retains most of its functionality. Knowledge about protein denaturation helps to produce food products with desirable functional properties.     

Electrophoresis studies for determining wheat–soy protein interactions in dough and bread

The interactions between soy and wheat proteins after dough mixing and bread baking were studied. Protein extractions from gluten and breadcrumbs elaborated with mixtures of wheat flour and enzyme-active full-fat, heat-treated full-fat, and enzyme-active defatted soy flours, and commercial isolated soy proteins were analyzed by electrophoresis. Different buffer systems with specific chemical action on proteins were used to investigate the types of forces between soy and wheat proteins in gluten and breadcrumbs. The presence of protein bands of similar molecular weight to soy proteins in gluten fractions after intensive dough washing indicated association between these proteins. Nonreduced wheat–soy gluten proteins had higher amount of sodium dodecyl sulfate soluble protein aggregates than wheat gluten. Soy and wheat proteins interacted by means of noncovalent and covalent (disulfide) bonds and the extent of the interactions depended on the soy protein state.     

Properties of Cysteine-Added Soy Protein-Wheat Gluten Films

Soy and wheat proteins as film ingredients are advantageous due to relative abundance, biodegradability, and their renewable nature. Research objectives were to evaluate effectiveness of gluten and cysteine addition in improving properties of soy protein-based films. Thickness, mechanical, and barrier properties were evaluated. Gluten addition and pH 3.0 lowered water vapor permeability and thickness. Mechanical properties were enhanced at pH 7.0 with cysteine addition. Cysteine increased tensile strength of some treatments due to increase in disulfide bond formation. Best compromise between barrier and mechanical properties was observed for the cysteine-added soy:gluten (4:1) film at pH 7.0. These films could find application as primary packaging for low moisture foods.     

PHYSICAL PROPERTIES OF SUGAR-SNAP COOKIES USING GRANULE SURFACE DEPROTEINATED WHEAT STARCH

The physical properties of soft wheat starch granule surface proteins and soy flours or isolates, which contribute to the texture of sugar‐snap cookies was studied. Soft wheat flour was deproteinated and cookies were produced containing 0, 10, 20 or 30% soy flour, or one of two types of ground, textured soy flour. Color, fracture force and spread ratio of cookies were determined. Cookies formulated with wheat starch stripped of the starch granule surface proteins exhibited significant alterations in diameter, fracture force, thickness and surface cracking. Cookies containing ground, textured soy flour and protein‐stripped starch granule wheat flour were larger, thinner and had more surface cracking than those produced with nontextured soy flour. Wheat starch granule surface proteins appear to partially mediate the interaction of proteins and starch in a sugar‐snap cookie system.     

THERMO-RHEOLOGY,QUALITY CHARACTERISTICS,AND MICROSTRUCTURE OF FRANKFURTERS PREPARED WITH SELECTED PLANT AND MILK ADDITIVES1

The purpose of this study was to evaluate substitution of nonmeat proteins for meat protein on the thermo-rheology, quality characteristics, and microstructure of frankfurters. Batters were formulated to contain either 2% sodium caseinate or soy protein isolate, or 3.5% whey protein concentrate or wheat germ flour. The storage modulus (G') of all treatments initially decreased during temperature ramping from 20–50C, then increased rapidly from 60–80C, with all-meat batter exhibiting the highest G' at 80C. Substitution with nonmeat proteins decreased G', shear force, compression force, and red color of meat compared with all-meat frankfurters. Increased protein content, cooking yield, and decreased fat content were obtained with nonmeat protein formulations. Electron micrographs showed that nonmeat proteins were able to bind to the meat protein and fat, forming a protein-fat matrix with less coalescence of fat droplets. Sodium caseinate, soy protein isolate, whey protein concentrate, and wheat germ flour can be used as protein additives in comminuted meat products without adversely affecting their physical characteristics.     

FUNCTIONAL PROPERTIES AND NUTRITIONAL QUALITY OF ALKALI- AND HEAT-TREATED SOY PROTEIN ISOLATE

Alkali and heat are increasingly utilized in food processing. This study was conducted to evaluate specific functional and nutritional properties of alkali- and heat-treated soy protein isolate (AHSPI) and the relationship between these properties. High pH (12.0) and temperature (100C) increased protein solubility of the isolate from 47 to 99.5% and emulsifying activity index from 74 to 184 m²/g. The values for in vitro protein digestibility (IVPD), computed-protein efficiency ratio, and IVPD-corrected amino acid score of AHSPI were not significantly (P>0.05) affected at pH 8.0 or 10.0, but were reduced At pH 12.0. At pH 12.0, lysinoalanine content significantly (p<0.05) increased from 0.39 to 1.22 g/100g protein as temperature was increased from 40 to 100C. Improvements in functional properties of soy proteins can be obtained through combined alkali and heat treatments. However, very high pH and temperature should be avoided to maintain nutritional quality of the proteins.     

Effect of soybean proteins on gluten depolymerization during mixing and resting

BACKGROUND: Gluten and soy proteins interact as a consequence of dough mixing; however, there is no evidence of the effect of soy protein on gluten depolymerization. The aim of this study was to assess the depolymerizing effect of soy protein on gluten network after mixing and resting of mixed doughs. Therefore, the changes in glutenin macropolymer (GMP) content, protein composition and free sulfhydryl content were evaluated. RESULTS: The protein profile from gluten–soybean blends, obtained by multistacking SDS‐PAGE, showed differences when compared to gluten profile. Soy and gluten proteins were extracted together with SDS buffer, which showed that soy proteins remained associated to insoluble wheat proteins even after hand‐washing the dough to obtain gluten. GMP content was determined to analyze the effect of soy protein on GMP gel formation. Protein content of GMP obtained from flour mixes and doughs was increased by inactive soy flour because soy proteins became insoluble and precipitated together with GMP. Active soy flour decreased GMP content due to gluten depolymerization. CONCLUSION: Soy proteins were associated to wheat protein through physical interaction and covalent and non‐covalent bonds during mixing and resting. These interactions produced large and medium‐size polymers. This fact increased SDS solubility of insoluble gluten proteins, producing a weakening of the gluten network. Physicochemical status of soy protein in the product had a great influence on how wheat–soy proteins interact. Copyright © 2007 Society of Chemical Industry     

Purification and identification of interacting components in a wheat starch–soy protein system

The objective of this research was to quantify the solubility, hydrophobicity and interaction characteristics of wheat–starch proteins (puroindoline, gliadin and glutenin) and protein-containing soy fractions (soy flour isolate [SFI], SFI 7S and 11S fractions, hexane-extracted textured soy flour [TVP] isolate, TVP 7S and 11S fractions, expelled, extruded soy flour [TSP] isolate, TSP 7S and11S fractions). Functional characteristics were assessed in aqueous sucrose solutions at pH 5.5 and 7.5 after heating to 25, 50, and 100 °C. Textured soy protein fractions were more soluble and had higher surface hydrophobicity profiles than their untextured counterparts. Sucrose addition decreased hydrophobicity in the textured proteins but increased it in untextured proteins. Characteristics of the isolate, as a whole, appear to be dictated by those of its 11S moiety. Dissociation constants (K_d values) for soy protein and starch-derived puroindoline were determined and indicated an extremely short association in all cases. The 11S fractions formed a complex with puroindoline in solution; however 7S fractions did not.     

Effects of Transglutaminase on SDS-PAGE Patterns of Wheat, Soy, and Barley Proteins and their Blends

Transglutaminase (TG) catalyzes the formation of nondisulfide covalent crosslinks between pep‐tide‐bound glutaminyl residues and ε‐amino groups of lysine residues in proteins. TG can be used for polymerizing proteins from 1 or more sources through formation of intermolecular crosslinks. This study investigated, by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis, polymers created by the action of TG on proteins of wheat, soy, barley, wheat‐soy, and wheat‐barley blends. Electrophoretic results showed that with increasing incubation time, the crosslinking reaction is substantially increased, with progressive decrease or disappearance of some protein monomers. Densitometric results showed that soy proteins were the best substrates of TG while barley and wheat proteins were similar in reactivity.     

Fractionating Soybean Storage Proteins Using Ca2+ and NaHSO3

ABSTRACT:  Individual soybean storage proteins have been identified as having nutraceutical properties, especially β-conglycinin. Several methods to fractionate soy proteins on industrial scales have been published, but there are no commercial products of fractionated soy proteins. The present study addresses this problem by using calcium salts to achieve glycinin-rich and β-conglycinin-rich fractions in high yields and purities. A well-known 3-step fractionation procedure that uses SO_2, NaCl, and pH adjustments was evaluated with CaCl₂ as a substitute for NaCl. Calcium was effective in precipitating residual glycinin, after precipitating a glycinin-rich fraction, into an intermediate fraction at 5 to 10 mM CaCl₂ and pH 6.4, eliminating the contaminant glycinin from the β-conglycinin-rich fraction. Purities of 100%β-conglycinin with unique subunit compositions were obtained after prior precipitation of the glycinin-rich and intermediate fractions. The use of 5 mM SO₂ in combination with 5 mM CaCl₂ in a 2-step fractionation procedure produced the highest purities in the glycinin-rich (85.2%) and β-conglycinin-rich (80.9%) fractions. The glycinin in the glycinin-rich fraction had a unique acidic (62.6%) to basic (37.4%) subunit distribution. The β-conglycinin-rich fraction was approximately evenly distributed among the β-conglycinin subunits (30.9%, 35.8%, and 33.3%, for α', α, and β subunits, respectively). Solids yields and protein yields, as well as purities and subunit compositions, were highly affected by pH and SO₂ and CaCl₂ concentrations.     

Effects of Soy Protein on Physical and Rheological Properties of Wheat Starch

It is necessary to understand the interaction phenomena between proteins and polysaccharides for the development of starch‐based products with better physical and sensory properties. A simplified model system was chosen to study the influence of soy protein on physical and rheological properties of wheat starch and the possible interactions between them. Thermal and pasting behaviors of the slurries and texture properties, water retention capacity and ultra structure of soy protein‐wheat starch gels were analyzed. While soy protein isolate increased the viscosity of starch suspension during and after heating, gels with soy protein presented a weaker structure than wheat starch gels. Results suggested association between leached out material and swollen granule surface of starch with soy protein. Scanning electron microscopy reflected these changes in the gel ultrastructure.     

Improvement of Functional Properties of Wheat Gluten and Blood Globin by Complex-Formation with Soy Lecithin

To improve the functional properties of wheat gluten or blood globin, a lecithin-protein complex was prepared by sonicating each protein solution with soy lecithin suspension at pH 3.0. The complex formation of each protein was demonstrated by gel filtration chromatography. Both solubility and emulsifying activities of each protein in the neutral pH region were much improved by complex-formation with soy lecithin. Soy lecithin-protein complexes were stable for 4 days storage at 24°C.     

双孢菇酱油双酿工艺研究

以双孢菇及豆粕、小麦、麸皮等为原料,通过米曲霉和鲁氏酵母的混合种曲在28℃～30℃发酵40d,将原料中蛋白质降解,从而酿制出双孢菇酱油。该产品具有红褐色、酱香浓郁、菇香味突出、口感鲜美、咸淡适口等特征,其理化指标均达到酿造酱油一级的标准,为双孢菇的利用提供了新的思路。     

Foaming Properties of Selected Plant and Animal Proteins

The foaming properties of proteins are important in predicting their fnnctionality in aerated foods. In model aqueous systems, foam expansion (FE) and foam stability (FS) of commercial plant proteins, wheat germ protein flour (WGPF), corn germ protein flour (CGPF), and soy flour (SF), were compared with those of nonfat dried milk (NFDM) and egg white powder (EWP) at 1, 2, 4, 6, and 8% using one- and two-way analyses of variance. The effects of pH 4, 5, 6, 7, and 8 on FE and FS of WGPF were also measured. The highest overall FE and FS were obtained for EWP. Among plant proteins, FE and FS were maximum for CGPF and SF, respectively. FS was lowest for NFDM. Except for SF, FE and FS increased with increasing protein concentration. The FE and FS of WGPF were highest at pH 8, lowest at pH 7, and intermediate at pH 4–6.     

大豆乳清蛋白功能特性的研究

对经过膜分离技术提取的大豆乳清蛋白的功能特性进行研究。主要研究了pH对大豆乳清蛋白的溶解特性、起泡性能及乳化性能的影响,并对大豆乳清蛋白的组成成分进行了电泳分析。结果表明,大豆乳清蛋白具有较好的溶解性及起泡性,但泡沫稳定性及乳化性不如大豆分离蛋白。大豆乳清蛋白主要包含6种成分。     

大豆高压短时蒸煮显著提高酱油二次沉淀蛋白降解率

酱油二次沉淀严重影响其外观质量和商品价值。本研究以大豆低压长时(0.24 MPa/18 min)蒸煮工艺为对照,采用十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(SDS-PAGE)和基质辅助激光解吸附电离串联飞行时间质谱(MALDI-TOF/TOF MS)等方法研究了大豆高压短时(0.54MPa/14min)蒸煮工艺对酱油二次沉淀蛋白和二次沉淀生成量的影响。实验结果表明大豆球蛋白G4中的B3亚基(20 ku)和G1中的A1a亚基(35 ku)是酱油二次沉淀蛋白的主要成分,采用大豆高压短时蒸煮工艺制备的酱油(样品)比其对照酱油中B3亚基减少65.38%,样品中A1a亚基被完全降解;样品中二次沉淀含量比其对照减少72.69%。同时,采用大豆高压短时蒸煮工艺可提高酱油原料蛋白质利用率9.37%、氨基酸态氮14.14%、总氮10.74%、总糖22.36%、还原糖27.87%和无盐固形物12.38%(p0.05)。因此,采用大豆高压短时蒸煮工艺可显著提高酱油二次沉淀蛋白降解率、减少酱油二次沉淀生成量和提高酱油滋味物质含量,同时改善酱油外观质量和滋味。     

Influence of soy protein on rheological properties and water retention capacity of wheat gluten

A better understanding of the physicochemical and rheological changes in soy/wheat composite dough may lead to overcome the problems caused by the incorporation of high levels of soy products on bread formulation. The effects of commercial soy protein isolate (SPI) on uniaxial extension and creep behavior, microstructure and free water of hydrated gluten were studied. Different solid:moisture ratios were used. Results showed that the substitution of wheat protein by soy protein negatively affected the gluten-SPI mixture rheological properties due to network weakening. It was demonstrated that gluten was weakened as a consequence of the interference effect of soy proteins on their structure, and the smaller availability of water to the build-up of the gluten network. A greater amount of moisture could partially improve the rheological performance of the gluten-SPI mixture.     

THERMAL BEHAVIOR, SOLUBILITY AND STRUCTURAL PROPERTIES OF SOY CONCENTRATE HYDROLYZED BY NEW PLANT PROTEASES

A soy concentrate prepared by alcoholic extraction of defatted soy flour was hydrolyzed with three plant proteases: hieronymin and macrodontin, cysteine proteases, and pomiferin, a serine protease. A commercial microbial protease (alcalase) was included for comparative purposes. Working at optimal conditions for each enzyme, 5–15% degree of hydrolysis (DH) values were obtained. Hydrolysates exhibited a characteristic SDS-PAGE pattern: the plant proteases attacked the polypeptides of 7S and 11S proteins with different intensity and selectivity, especially the A and B polypeptides of the 11S protein. Intermediate molecular weight peptides (24 and 60 kDa) were produced as the hydrolysis progressed. Differential Scanning Calorimetry (DSC) thermograms of flour. concentrate and hydrolysates were analyzed to evaluate the thermal stability and denaturation enthalpies of the major proteins. An increase in the degree of protein denaturation resulting from enzymatic action and a lower thermal stability at low pH were detected. The surface hydrophobicity of all hydrolysates, unlike expected, did not increase. Solubility at pH 7.0 is closely related to the DH, independent of the protease used. Solubility at pH 4.5 appeared to be related to the extent of hydrolysis of polypeptide A by each protease.     

Physicochemical and Functional Properties of Winged Bean Flour and Isolate Compared with Soy Isolate

The proximate composition, amino acid profile and functional properties of isolated winged bean proteins were determined and compared with soy protein isolate. Winged bean protein extracted at pH 10 and pH 12 had protein contents of about 90% and 80%, respectively. Alkali extraction of winged bean proteins at pH 10 and pH 12 did not affect the amino acid distribution of the isolated proteins. Oil and water absorption, emulsion, and foaming properties of winged bean isolated compared favorably with soy isolate. Least gelation concentration for winged bean isolate was 18% compared to 14% for soy isolate. Thus, winged bean protein isolate with its high protein content, high lysine and other essential amino acid content and good functionality has a good potential as an ingredient in food products.