Deamidation and Functional Properties of Food Proteins by the Treatment with Immobilized Chymotrypsin at Alkaline pH

Ovalbumin, lysozyme, 7S globulin, 11S globulin, and gluten were treated with immobilized chymotrypsin on controlled-pore glass at pH 10 at 20°C to improve their functional properties. Optimum pH of deamidation of ovalbumin by immobilized chymotrypsin was 10, where proteolysis was very limited. Deamidation percentages of ovalbumin, lysozyme, 7S globulin, 11S globulin, and gluten were 10.0, 8.4, 6.0, 5.0, and 8.0, respectively. SDS polyacrylamide gel electrophoretic patterns of ovalbumin and lysozyme showed no difference between untreated and treated proteins, while those of soy proteins and gluten showd that larger molecular weight fractions were dissociated into smaller molecular size fractions. Solubility of gluten was greatly improved at all pHs, 2-12. Both emulsifying and foaming properties of proteins were improved by treatment with immobilized chymotrypsin.     

Mechanical and Biochemical Characterisation of Wheat Gluten Films as a Function of pH and Co‐solvent

Dispersions of wheat gluten were prepared at different pHs (4, 6 and 11) in the presence or absence of ethanol. Films were obtained after casting suspensions followed by evaporation of the solvent. Films prepared at pH 11 were significantly stronger than the films prepared at pH 4 and 6 with tensile strengths of approximately 7 vs. 2 MPa. With increasing strength, the elongation at break was moderately reduced from approximately 300% to 190%. No significant variations of water vapour transfer rate properties were observed among the films. The solubility of gluten films in aqueous and 1.5% sodium dodecyl sulfate (SDS) solution decreased with increasing pH of films. Tricine sodium dodecyl sulfate‐polyacrylamide gel (SDS‐PAGE) patterns of wheat gluten and film showed the formation of high molecular weight fractions. The amount of free amino groups in the wheat gluten decreased during film formation. Amino acid analysis showed the presence of lysinoalanine (LAL). All these results indicate the formation of irreversible intermolecular cross‐linking upon film formation at pH 11.     

Foaming properties of enzymatically hydrolysed wheat gluten

A thermally treated wheat gluten (TTG) was structurally modified by enzymatic hydrolysis. Hydrolysis was carried out using a fungal protease. The solubility of hydrolysates having low, medium and high degrees of hydrolysis (DH) and the foaming properties of their extracts at each pH were determined. For comparison, a sample of TTG was used as a standard. The results showed that solubility increased as the DH increased, but foaming properties began to be impaired beyond a certain DH. Therefore, a minimum protein structure has to be retained, in order to keep good foaming properties. Mild hydrolysis (DH 14%) not only permitted the solubilisation of gluten proteins in a bigger pH range, but at pHs 9 and 6.5, good foaming properties were also obtained, which gave us the chance to expand wheat gluten utilisation.     

Physicochemical characteristics and functional properties of grape (Vitis vinifera L.) seeds protein

The amino acid composition, physicochemical and functional properties of grape (Vitis vinifera L.) seeds protein (GSP) were evaluated and compared with those of soybean protein isolate (SPI). Amino acid analyses of GSP revealed high levels of glutamic/glutamine, glycine and aspartic/asparagines. SDS‐PAGE analysis demonstrated that globulin was the major protein component in GSP, whose subunit molecular weights were mainly varied from 25.5 to 40.0 kDa. The isoelectric pH of GSP was found to be at the acidic pH of around 3.8. At all the pHs tested except pH 2.0, no significant changes of GSP secondary structure were observed. GSP exhibited beneficial functional properties such as preferable solubility and emulsifying activity, while the foaming properties and water holding capacity were relatively poor compared to SPI. It could then be employed to soup, sauce, beverage or meat product for improving nutritional and sensory quality of these foods at appropriate pHs.     

Rheological and Structural Properties of Wiener-Type Products Substituted with Vital Wheat Gluten

Mechanical properties of wiener batters substituted with vital wheat gluten (VWG) or acid-solubilized (deamidated) VWG were studied. Substitution led to decreased storage (G') and loss (G”) moduli. Cooking profiles showed initial modulus decreases due to fat melting, with G’ reaching minimum around 50-55°C, followed by rapid increases. Sharp G” and tan 5 transitions appeared near 48°C. Substitution caused upward shift in transition temperatures, and at 20%, decreased moduli. Substitution caused no significant (p < 0.05) decreases in cook yield or texture. Microscopical examination revealed random binding of gluten to meat protein, forming continuous networks. Batters containing deamidated gluten had structure similar to all-meat or VWG-substituted batters.     

Dispersion in the Presence of Acetic Acid or Ammonia Confers Gliadin‐Like Characteristics to the Glutenin in Wheat Gluten

Spray‐dried gluten has unique properties and is commercially available in the food industry worldwide. In this study, we examined the viscoelastic properties of gluten powder prepared by dispersion in the presence of acetic acid or an ammonia solvent and then followed by lyophilization instead of a spray drying. Mixograph measurements showed that the acid‐ and ammonia‐treated gluten powders had marked decreases in the time to peak dough resistance when compared with the control gluten powder. The integrals of the dough resistance and bandwidth for 3 min after peak dough resistance decreased in both treated gluten powders. Similar phenomena were observed when gliadin was supplemented to gluten powders. Basic and acidic conditions were applied to the acid‐ and ammonia‐treated gluten powders, respectively, and the viscoelastic behaviors were found to depend on the pH in the gluten dispersion just before lyophilization. These behaviors suggest that gluten may assume a reversible change in viscoelasticity by a fluctuation in pH during gluten dispersion. SDS‐PAGE showed that the extractable proteins substantially increased in some polymeric glutenins including the low molecular weight‐glutenin subunit (LMW‐GS) when the ammonia‐treated gluten powder was extracted with 70% ethanol. In contrast, the extractable proteins markedly increased in many polymeric glutenins including the high molecular weight‐glutenin subunit and/or the LMW‐GS when the acid‐treated gluten powder was extracted with 70% ethanol. It thus follows that the extractability of polymeric glutenin to ethanol increases similarly to gliadin when gluten is exposed to an acidic or a basic pH condition; therefore, glutenin adopts gliadin‐like characteristics.     

Effects of pH on the Textural Properties and Meltability of Pasteurized Process Cheese Made with Different Types of Emulsifying Salts

ABSTRACT: Functional properties of pasteurized process cheese (PPC) made with different types of emulsifying salts (ES) (2%, wt/wt) were investigated as a function of different pH values (from 5.3 to approximately 5.9). The ES investigated were trisodium citrate (TSC), disodium phosphate (DSP), sodium hexametaphosphate (SHMP), and tetrasodium pyrophosphate (TSPP). Meltability and textural properties were determined using UW‐MeltProfiler and uniaxial compression, respectively. All PPC samples exhibited an increase in degree of flow (DOF) determined at 45 °C when the pH was increased from 5.3 to 5.6, presumably reflecting greater Ca binding by the ES, increased charge repulsion and therefore greater casein dispersion. When the pH of PPC was increased from 5.6 to approximately 5.9, 2 types of ES (DSP and SHMP) exhibited no further increase in DOF at 45 °C; while DOF increased in 1 type of PPC (made with TSC) but decreased in another (made with TSPP). TSPP is able to form crosslinks with casein especially in the vicinity of pH 6, which likely restricted melt; in contrast TSC does not crosslink caseins and the increase in pH helped cause greater casein dispersion. Low pH samples (5.3) were not significantly harder than higher pH samples for all ES types but exhibited fracture. The PPC with the highest hardness values at pHs 5.3 and 5.6 were made with TSPP and TSC, respectively. The pH‐dependent functional behavior of PPC was strongly influenced by the type of ES and its physicochemical properties including its ability to bind Ca, the possible creation of crosslinks with casein and casein dispersion during cooking.     

Rheological and Stability Transitions in Meat Batters Containing Soy Protein Concentrate and Vital Wheat Gluten

Physical/rheological properties of meat batters during heat-processing were studied. Vital wheat gluten (VWG) and soy protein concentrate (SPC) were incorporated into meat batters which were heated to 40, 50, 60 and 70°C and held for 0, 30 and 60 min. Amounts of fat and aqueous fluid released during heating were determined. A two-cycle compression test and shear modulus determination were used to evaluate rheological changes. VWG and SPC did not have any significant effect on either stability or textural changes. There was a significant interaction between temperature and time for stability and textural characteristics. Significant changes in rheological and stability properties of meat batters occurred in the 50–70°C region. Shear modulus showed a major increase at 54–57°C.     

Changes in physicochemical properties and microstructure of dried squid during softening treatment

Dried squid were prepared at 4 or 40 °C and softened first in water and then in alkaline solution. The physicochemical and structural changes in the dried squid during the softening treatment were examined. A significantly higher wet weight was observed for the 4 °C‐dried squid during the softening treatment compared with the 40 °C‐dried squid. The rupture stress and rupture energy of the 40 °C‐dried squid were significantly higher than those of the 4 °C‐dried squid during the softening treatment. The sodium dodecyl sulphate polyacrylamide slab gel electrophoresis (SDS‐PAGE) pattern of the 4 °C‐dried squid was almost the same as that of raw squid. The SDS‐PAGE pattern of the 40 °C‐dried squid showed many fragments of lower molecular weight. After soaking in distilled water the SDS‐PAGE pattern of the 40 °C‐dried squid did not change significantly; however, the SDS‐PAGE pattern of the 4 °C‐dried squid became the same as that of the 40 °C‐dried squid. Histological analysis by light microscopy showed the formation of muscle fibre bundles in the 40 °C‐dried squid. A higher water permeation was observed among the muscle fibres of the alkali‐softened 4 °C‐dried squid when compared with the alkali‐softened 40 °C‐dried squid. Copyright © 2003 Society of Chemical Industry     

Enhanced water absorption of wheat gluten by hydrothermal treatment followed by microbial transglutaminase reaction

BACKGROUND: The water absorption of wheat gluten plays an important role in the weight, volume and form ratio of the breads. In this paper, hydrothermal treatment and microbial transglutaminase (MTGase) modification were combined to improve the water absorption ratio (WAR) of wheat gluten. To understand the increases in WAR, the changes in MTGase reaction after gluten hydrothermal treatment were also investigated. RESULTS: The sole hydrothermal treatment improved the WAR of gluten. The gluten treated at 100 °C for 30 min exhibited the highest WAR value (2.03 g g^?1 gluten) while the WAR of the control without hydrothermal treatment was 1.5 g g^?1 gluten. When gluten was exposed to 90 °C for 30 min followed by incubation with MTGase for 5 h, its WAR reached 2.48 g g^?1 gluten. In contrast to control gluten, the surface hydrophobicity of the gluten preheated at 90 °C for 30 min increased and fluctuated in a different way during the following MTGase reaction. Meantime, the trend in the amount of soluble protein of preheated gluten was also changed in the progress of MTGase reaction. CONCLUSION: Hydrothermal treatment followed by MTGase reaction is an efficient approach to improve the WAR of wheat gluten. The analysis of catalytic process, including determination of ammonia, gluten surface hydrophobicity, soluble protein and SDS–PAGE, suggested that hydrothermal pretreatment accelerated the cross‐linking reaction and may alter the ratio of gluten deamidation catalysed by MTGase, which induced an increase in the WAR. Copyright © 2010 Society of Chemical Industry     

Acid-thermal-induced formation of rice bran protein nano-particles: foaming properties and physicochemical characteristics

The purpose of this study was to expound on the correlation between foaming properties and physicochemical characteristics of rice bran protein (RBP) samples. RBP nano-particles (RBPNs) were prepared by acidic–thermal treatment under different RBP solution concentrations and treated times at 90 °C, and then the foaming properties were measured at pH 7.0 and pH 2.0. Compared to RBP, the foaming properties of RBPNs were increased at pH 7.0, and RBPNs could have better foam capacity but have no obvious changes in foam stability at pH 2.0. The results of Pearson correlation showed that the foaming properties were closely correlated with ζ potential, contact angle, and surface hydrophobicity for RBP and RBPNs, and a strong correlation between foaming capacity and surface hydrophobicity was shown for RBPNs. Additionally, the result of TEM images confirmed that RBPNs were inclined to form associated aggregates which may affect the physicochemical characteristics of RBPNs.     

Molecular Analysis of the Polymeric Glutenins with Gliadin‐Like Characteristics That Were Produced by Acid Dispersion of Wheat Gluten

We had earlier shown that the dispersion of wheat gluten in acetic acid solution conferred gliadin‐like characteristics to the polymeric glutenins. To elucidate the molecular behavior of its polymeric glutenins, the characteristics of gluten powder prepared from dispersions with various types of acid were investigated in this study. Mixograph measurements showed that the acid‐treated gluten powders, regardless of the type of acid, had dough properties markedly weakened in both resistance and elasticity properties, as though gliadin was supplemented. The polymeric glutenins extracted with 70% ethanol increased greatly in all acid‐treated gluten powders. Size exclusion HPLC and SDS‐PAGE indicated that the behavior of polymeric glutenins due to acid treatment was attributed to their subunit composition rich in high molecular weight glutenin subunit (HMW‐GS) and not their molecular size. The gluten prepared with the addition of NaCl in acid dispersion had properties similar to those of the control gluten. The results suggest that ionic repulsion induced by acid dispersion made the polymeric glutenins rich in HMW‐GS disaggregate, and therefore, act like gliadins.     

Solubilisation and Degradation of Wheat Gluten Proteins by Barley Malt Proteolytic Enzymes

Solubilisation and degradation of wheat gluten proteins by barley malt proteolytic enzymes (BMPE) was investigated with a model buffer system at pH 4.0 and pH 5.6, representing optimal pH for proteolysis and a pH value typical for beer brewing conditions respectively. Under the experimental conditions, incubation of commercial wheat gluten with BMPE solubilised 70% and 20% of the gluten proteins at pH 4.0 and pH 5.6 respectively. Gel permeation chromatography profiles and SDS‐PAGE showed that wheat gluten proteins were more degraded by BMPE at pH 4.0 than at pH 5.6. In a laboratory scale barley malt brewing experiment, proteins of worts, prepared with and without wheat gluten, were characterised. Results comparable to those in the model buffer system at pH 5.6 were obtained, which indicated that BMPE indeed solubilise wheat gluten during mashing, but that further degradation is rather limited under these conditions.     

Effect of heat treatment on the properties of soy protein‐stabilised emulsions

The effect of heat treatment on the properties of soy protein‐stabilised emulsions was investigated. Emulsions were prepared with unheated and heat‐treated soy protein (NSP and HSP) dispersions. Heating on soy protein dispersions at 95 °C for 30 min resulted in smaller average oil droplet size, lower tendency for oil droplet flocculation, higher protein adsorption and lower viscosity. The properties of emulsions were significantly influenced by the protein concentration. The sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS–PAGE) profiles showed that the heat treatment on soy protein dispersions increased the protein adsorption at O/W interface. The viscosity of all samples at low shear rate was inversely proportional to the d₃₂, suggesting a positive relation to the total interfacial area per unit volume. Emulsions showed shear‐thinning behaviour. The relaxation time was found to increase with aqueous phase viscosity determined by the Cross viscosity model.     

Effect of high‐pressure treatments on mechanical and functional properties of restructured products from arrowtooth flounder (Atheresthes stomias)

Restructured fish products from arrowtooth flounder (Atheresthes stomias), an abundant and subutilized species from the Gulf of Alaska, were obtained by hydrostatic pressure processing (HPP) at 400 and 600 MPa with 0–5 min pressure‐holding time. Minced fish meat was massaged with 20 g kg^?1 salt at 10 °C during 5 min, stuffed in commercial sausage case and HPP‐treated. Raw and cooked (90 °C for 15 min) pressure‐treated gels were characterized by changes in mechanical properties (texture profile analysis and punch test), protein solubility, electrophoretic profile, expressible water and color. The mechanical properties of raw fish gels increased with pressure level and pressure‐holding time while solubility decreased. Myosin aggregation shown by SDS‐PAGE was associated with changes in mechanical and functional properties. The values for mechanical properties of heat‐induced gels were higher in cooked pressure‐treated samples than in the heat‐only control. Copyright © 2004 Society of Chemical Industry     

花生湿热处理对其分离蛋白的结构和功能特性的影响

本文通过还原/非还原电泳、热差示扫描、表面疏水性及等电点测定等手段,表征了花生湿热处理对其分离蛋白结构和功能特性的影响.结果表明:在105℃随着湿热处理时间延长其分离蛋白中伴球蛋白所占比例逐渐减少,球蛋白在加热75min后产生热聚集,此外通过美拉德反应生成的糖蛋白含量逐渐增加,分离蛋白等电点向酸性偏移,表面疏水性先逐渐...     

Novel Radiofrequency‐Assisted Thermal Processing Improves the Gelling Properties of Standard Egg White Powder

Effect of radiofrequency (RF)‐assisted thermal processing on quality and functional properties of high‐foaming standard egg white powder (std. EWP, pH approximately 7.0) was investigated and compared with traditional processing (heat treatment in a hot room at 58 °C for at least 14 d). The RF‐assisted thermal treatments were selected to meet the pasteurization requirements and to improve the functional properties of the std. EWP. The treatment conditions were: RF heating to 60, 70, 80, and 90 °C followed by holding in a hot air oven at those temperatures for different periods ranging from 4 h at 90 °C to 72 h at 60 °C. The quality (color and solubility) and functional properties (foaming properties: foaming capacity and foam stability; and gelling properties: water holding capacity and gel‐firmness) of the std. EWP were investigated. RF‐assisted thermal processing did not affect the color and solubility of std. EWP at any of the treatment conditions. In general, the foaming and gelling properties of RF‐assisted thermally processed std. EWP increased with an increase in temperature and treatment duration. The optimal RF‐assisted treatment conditions to produce std. EWP with similar functional properties as the traditionally processed (hot room processed) std. EWP were 90 °C for ≥8 h. These optimal conditions were similar to those for high gel egg white powder (HG‐EWP, pH approximately 9.5). The RF‐assisted thermal pasteurization improved the gelling properties of std. EWP to the levels of HG‐EWP, leading to newer applications of this functionally improved safe product. The RF‐assisted thermal processing allows the processor to produce a HG‐EWP from std. EWP subsequent to processing while simultaneously pasteurizing the product, thus assuring the product safety.     

Effect of Modified Wheat Gluten on Boiling Resistance Capacity of Pork Meatballs

The effect of the modified wheat gluten (MWG) extender, prepared by alcalase‐based hydrolysis and transglutaminase cross‐linking, on meatballs was analyzed in this study. Here, we studied the effect of MWG addition on the boiling resistance capacity of pork meatballs (MB‐MWG) at high temperature (100 °C) and increasing cooking time; meatballs with added soy protein isolates (MB‐SPI) and raw wheat gluten (MB‐WG) were used as references. The cooking loss, water‐holding capacity (WHC), and textural properties of meatballs were investigated. The results revealed that MB‐MWG showed lower cooking loss, which decreased by 49.16% compared to meatballs without added extenders when treated for 30 min. The WHC of MB‐MWG significantly increased from 80.68% to 95.42%. The hardness, springiness, and chewiness (textural properties) of MB‐MWG were also significantly increased by 97.05%, 6.68%, and 121.96%, respectively. The addition of MWG increased the cross‐linking in meatballs during the cooking process, as indicated by the higher G′. SDS‐PAGE indicated an obvious decrease in myosin heavy chain in MB‐MWG cooked for 30 min at 100 °C, which was attributed to the interaction of myofibrillar proteins in pork meat with MWG. The nuclear magnetic resonance T₂ relaxation time patterns indicated that MWG addition caused an increase in the bound water content, and decrease in the free water content, of meatballs. An analysis of the microstructures revealed that the MB‐MWG formed the most regular and compact network. Therefore, MWG could be used as an ingredient to facilitate the processing of meat products.     

Influence of double enzymic hydrolyses on gluten functionality

Functional properties of chemically deamidated and/or double enzymically‐treated gluten were studied. Performances of the modified glutens were compared to those of egg white proteins, casein, deamidated gluten and gluten submitted to deamidation plus single enzymic treatment. Higher nitrogen solubility index (>90%) was obtained after treatment of the gluten with the sequence pepsin + alcalase and deamidation + pepsin + papain. The sequence pepsin + papain has permitted the production of a gluten with foaming properties close to those of egg white. Deamidation + papain treatment leads to interesting emulsifying properties although different from those of casein. The results show that modified glutens present thresholds in the degree of enzymic hydrolysis (DH) for foaming and emulsifying properties (respectively 1.3% and 2.0%). For higher DH the stability decreases. © 1999 Society of Chemical Industry     

A Comparison of Nonmeat Proteins, Sodium Tripolyphosphate and Processing Temperature Effects on Physical and Sensory Properties of Frankfurters

Frankfurters, with and without 0.5% sodium tripolyphosphate (STPP), containing 3.5% vital wheat gluten (VWC), calcium reduced nonfat dry milk (RNFDM) and soy protein concentrate (SPC) were processed to an internal temperature of 72° or 82°C and compared to an all-meat control. Processing yields, textural profile analysis (TPA) and sensory textural attributes were not different among protein treatments, but SPCand VWG contributed slight-to-moderate off-flavor. VWG and SPC franks were acceptable, but slightly less desirable than the control and RNFDM treatments. Franks processed to 82°C were more desirable, but at the expense of reduced yields. STPP did not affect yields, but increased sensory firmness and TPA fracturability and hardness. VWG, RNFDM and SPC were comparable to the control for most traits studied, but alterations in spice formulation are needed to improve VWG and SPC flavor.