Thermal Aggregation Properties of Duck Salt-Soluble Proteins at Selected pH Values

Thermal aggregation properties of duck breast and leg salt-soluble proteins (SSP) were studied at pH 5.50, 5.75 and 6.00. At pH 5.50, a major transition for breast was observed at 60.3°C and for leg at 41.8°C. At pH 5.75, major transitions at 44.6 and 43.2°C were obtained, respectively, for the breast and leg SSP. Three transitions at 46.0, 53.0 and 59.0°C were exhibited by breast SSP at pH 6.00, whereas only two major transitions at 47.4 and 54.0°C were identified in leg SSP. Changes in transition peak heights and shifts in transition temperatures as a result of pH changes indicated that, depending on fiber type, pH may enhance or suppress the aggregation behavior of specific constituents of the myosin/actomyosin complex, thereby altering the overall aggregation pattern of the protein preparation.     

Gelation of Proteins from Washed Muscle of Threadfin Bream (Nemipterus japonicus) under Mild Acidic Conditions

Gelation of proteins of washed mince of threadfin bream was induced by the organic acids: acetic, lactic, tartaric, and citric. Washing of mince was essential for gelation. The strength of acetic acid-induced gel was affected by setting conditions and heat treatment. Gelation was associated with degradation of myosin heavy chain and appearance of a new protein band of about 160 kDa. Solubility studies of the gel in various solvents suggested structural changes. Gelation was also associated with oxidation of sulfhydryl groups. Salts negatively influenced gelation.     

Structural and Functional Properties of Caseinate and Whey Protein Isolate as Affected by Temperature and pH

The structural properties, i.e., active sulfhydryl (SH), flexibility and hydrophobicity, and functional properties, i.e., solubility, emulsion activity (EA), emulsion stability (ES), foam overrun (FO) and foam stability (FS), of commercial sodium caseinate (SC) and whey protein isolate (WPI) solutions were investigated at pH 6, 7 and 8 and at 25, 55 and 65°C. WPI contained a higher concentration of active SH and was more hydrophobic than SC. WPI provided comparable solubility and EA, lower FO, but higher FS than SC. Temperature and pH effects on the two proteins were somewhat inconsistent.     

Phosphates and Muscle Fiber Type Influence Thermal Transitions in Porcine Salt-Soluble Protein Aggregation

Salt-soluble proteins (SSP) were extracted from porcine Serratus ventralis (red), Vastus intermedius (red) and Longissimus dorsi (white) muscles and heated to examine dynamic changes and transitions in protein aggregation. At pH 6.0, red muscle SSP typically showed 1 or 2 transitions and white muscle SSP exhibited 3 transitions. Addition of ortho-, pyro-, tripoly- and hexametaphosphate up to 1% increased SSP transition temperatures and altered transition patterns; NaCl at comparable ionic strengths did not show this effect. SSP transitions were most affected by 0.15-0.25% tripolyphosphate and low pH (<6.0). Red and white SSP exhibited different thermal properties and responses to phosphate treatments. These findings indicate red and white muscle types should undergo different processing treatments for optimum quality meat products.     

Foaming Properties of Proteins as Affected by Concentration

Commercial sodium caseinate and whey protein isolate were evaluated at protein concentrations 0.25 to 16% with ovalbumin solutions as reference. Logarithmic models were developed to express the effect of protein concentration on foam expansion and serum drainage. The kinetics of gas release from milk protein-stabilized foams followed a three-phase pattern. Low foam collapse rates were observed in initial and final phases while rapid collapse occurred during the transition phase. No transition was observed for ovalbumin-stabilized foams. Globally, foam collapse rate increased with increasing protein concentration. Apparent viscosity of protein-stabilized foams increased with concentration to a maximum; beyond which, a reverse trend was observed. Maximum viscosities of milk protein foams were at concentrations & lt;0.5%, while ovalbumin foams showed maximum viscosity around 2% protein.     

猪肉盐溶性蛋白热诱导凝胶特性的研究

盐溶性蛋白是影响猪肉制品的保水性及凝胶特性的一类最主要蛋白质,其中对蛋白质热凝胶起决定作用的是肌球蛋白.本试验以猪肉为原料,首先通过单因素试验研究贮藏时间、离子强度、磷酸盐等因素的影响,再通过正交试验得出猪背最长肌(P1d)盐溶蛋白最合适的提取条件:MgCl2浓度0.01 mol/L、NaCl浓度0.5 mol/L、焦磷酸钠及多聚磷酸钠的比例均为0.4%.     

不同添加剂对鸡肉盐溶蛋白质热诱导凝胶性质的影响

采用质构分析法、动态流变分析法、差示扫描微量热法研究大豆分离蛋白、花生蛋白、卡拉胶对鸡胸肉和鸡腿肉盐溶蛋白热诱导凝胶性质的影响。试验结果表明:不同添加剂可在不同程度上改善鸡胸肉和鸡腿肉盐溶蛋白热诱导凝胶特性,其中卡拉胶添加效果最好。由动态流变学分析可知,鸡胸肉和鸡腿肉盐溶蛋白形成凝胶存在不同作用机理。热稳定性分析表明,鸡肉混合蛋白热诱导凝胶形成主要与肌球蛋白有关,肌动蛋白作用效果不明显。不同添加剂可增强鸡胸肉和鸡腿肉盐溶蛋白的变性温度和变性热,其中大豆分离蛋白添加效果最显著。     

Heat-induced Gelation of Chicken Gizzard Myosin

Chicken gizzard myosin solution formed a gel when heated above 40°C. The rigidity of the gel was constant above 65°C. Maximum pH for gel formation was 5.9 at 0.6M and 5.7 at 0.15M KCl. Higher rigidity of the myosin gel was observed at low ionic strength than at high ionic strength. Rigidities of myosin at 0.6M KCl increased by (mg/mL)^2.5 and at 0.15M (mg/mL)^{1, 4} myosin concentration. The strength of gizzard myosin gels was comparable to that of myosin gels from chicken breast muscle under similar conditions.     

Gelation of Egg White Proteins as Affected by Combined Heating and Freezing

Combined effects of preheating (60°C, 0 ～ 30 min) and freezing (– 10 or –20°C, 20 hr) on the gelation of dried egg white induced by reheating (80°C, 30 min) were examined in comparison with those of refrigerating (5°C, 20 hr). Refrigeration consistently induced harder gels, while freezing resulted in either harder or softer gels. Results of soluble protein content, turbidity, SDS-PAGE and gel filtration indicated that the unfolded and aggregated levels of ovotransferrin, caused by the cooperative effects of preheating and freezing or refrigerating, mainly determined the characteristics of gel properties.     

Protease-Induced Aggregation and Gelation of Whey Proteins

Aggregation and gelation of whey proteins induced by a specific protease from Bacillus licheniformis was revealed by turbidimetry, size exclusion chromatography, dynamic light scattering and rheology. The microstructure of the gel was examined by transmission electron microscopy. During incubation of 12% whey protein isolate solutions at 40°C and pH 7, the major whey proteins were partly hydrolyzed and the solution gradually became turbid due to formation of aggregates of increasing size. The viscosity of the hydrolysate simultaneously increased and eventually a gel formed. The gel had a particulate type of microstructure. We hypothesized that the aggregates forming the gel were held together by noncovalent interactions.     

Physical Properties of Extruded Products as Affected by Cheese Whey

Corn, rice and potato flour were extruded with sweet whey solids (SWS) or whey protein concentrate (WPC) using low and high shear extrusion processing conditions. WPC added at product content of 25% had minimal effect on the texture of extruded products. Expansion and breaking strength were improved in some processes through changes in extrusion shear and moisture. Whey product incorporation resulted in reduced specific mechanical energy input to the process. Increasing whey product concentration beyond 25% reduced expansion and water absorption indices significantly, affecting textural hardness. Product quality characteristics were directly related to the whey product content.     

Gelation of Calcium-Reduced and Lipid-Reduced Whey Protein Concentrates as Affected by Total and Ionic Mineral Concentrations

Rheological and microstructural properties of five dialyzed whey protein concentrate (WPC) gels were investigated. Maximum WPC gel hardness as determined by shear stress (ST) was observed at 2.7–4.5 mM Ca and 0.6–1.1 mM Ca²⁺ concentrations with a Ca ionization of 20–25%. Gel cohesiveness by shear strain (SN) correlated with total lipid and phospholipid (PLP) concentrations and percent of lipid unsaturation. Microstructural characteristics of the gels, as determined by light microscopy (LM), confirmed their water holding capacity (WHC) and rheological properties.     

Interaction of Commercial Dairy Proteins and Chicken Breast Myosin in an Emulsion System

The compatibility of commercial dairy proteins with chicken breast myosin in an emulsion system was examined. SDS-PAGE of the solution remaining after emulsion formation indicated that myosin incorporation into the cream layer was much more limited with the flexible additives such as sodium-caseinate and milk protein isolate resulting in decreased emulsion stability. However, myosin incorporation and emulsion stability were maintained with whey protein concentrate or whey protein isolate at all additive levels. No hydrophobicity changes were found in myosin with additive mixtures except for heated myosin and WPC (P=0.04). The stability of an emulsion was primarily determined by the amount of myosin incorporated.     

Insolubilized Whey Protein Concentrate and/or Chicken Salt-Soluble Protein Gel Properties

Properties of gels prepared from five whey protein concentrates (WPC) with protein solubilities ranging from 27.5% to 98.1% in 0.1M NaCl, pH 7.0, chicken breast salt-soluble protein (SSP), or a combination of SSP and WPC at pH 6.0, 7.0 or 8.0 were compared. WPC did not form gels when heated to 65°C. SSP gels heated to 65°C were harder than those heated to 90°C at all pHs and hardness decreased as pH was increased. Hardness of combination gels heated to 65°C increased as WPC solubility decreased at all pHs; however, the opposite trend was observed at 90°C. Combination gels of the same WPC solubility at 65°C were more deformable than those heated to 90°C.     

Gelation of Beef Heart Surimi as Affected by Antioxidants

Oxidation of proteins (carbonyls) and lipids (TBARS) in beef heart surimi-like materials during preparation and storage (2°C) was inhibited by propyl gallate (0.02%) or α-tocopherol (0.2%). Inhibition of oxidation did not affect surimi gel property (storage modulus, G'). Storage promoted oxidation of proteins in 0.2% ascorbate-washed mince, leading to increases in peak (～ 55°C) and final (70°C) G' of thermally induced surimi gel. Protein carbonyls in stored surimi and its sol (salted), as well as TBARS of the sol, strongly correlated with both peak and final G of gels. Incorporation of tripolyphosphate into washed mince promoted gelation whether the surimi-like material was oxidized or not.     

Gelation Properties of Ovalbumin as Affected by Fatty Acid Salts

The physicochemical properties of heat-induced ovalbumin (OVA) gels containing fatty acid salts (FAS) were investigated. Water-holding ability and transparency markedly increased in the presence of sodium caprate or sodium laurate. At 9% of the protein concentration transparent and hard gels formed; at 7%, transparent and soft gels formed. Scanning electron microscopy showed that the transparent gels had a more homogeneous structure than turbid gels without FAS. Differential scanning calorimetry indicated that denaturation temperature of OVA was decreased and the peaks became broader after addition of FAS.     

Interactive Effects of Factors Affecting Gelation of Whey Proteins

The individual effects of heating time (15–120 min), pH (3–9) and NaCl (0–2M), sucrose (0–30% w/v) and protein (10–30% w/v) concentrations on the strength, turbidity and water holding capacity were investigated on a commercial whey protein concentrate (WPC, 75% protein) when heated at temperatures ranging from 65 to 90°C. Interactive effects were investigated using a four-variable, five-level central composite rotatable design (CCRD) analyzed by response surface methodology (RSM). Gel strength (GS) and water holding capacity (WHC) increased with protein concentration, heating temperature and time. Increasing sucrose concentration decreased GS but increased WHC. Increasing NaCl concentration increased GS and WHC below pH 5 but resulted in weaker gels at high pH (>7).     

Factors Affecting the Gelation Properties of Hydrolyzed Sunflower Proteins

The effects of temperature and several chemicals on gelation time and strength of gels formed by heating (pH 8) 5% solutions of trypsin hydrolyzed sunflower proteins were studied by dynamic rheological methods. The storage modulus reached a maximum at 80°C. Ca₂Cl (and NaCl at > 0.2M) accelerated gelation and weakened the gel. NaCOCH₃Na₂SO₄ and NaSCN decreased the storage modulus. Urea decreased gelstrength and at high concentrations slowed gelation. Time for gelation diminished and gel strength increased with increasing mercaptoethanol concentration up to 0.1M. Propylene glycol at 5–20% concentrations accelerated gelation and at 5% also increased gel strength. Trypsin hydrolyzed sunflower proteins could be useful in products requiring strong gels at high temperatures.     

Factors Affecting the Functional Properties of Whey Protein Products: A Review

Numerous why protein products (WPP) have been developed as excellent food ingredients with unique functional properties. However, the functional properties of WPP are affected by several compositional and processing factors. Recently, novel processing technologies such as high hydrostatic pressure, ultrasound, extrusion and tribomechanical activation have been used to modify the functional properties of WPP. Also, WPP have been used as delivery systems for functional ingredients and in edible films. The present paper reviews the latest developments in the role of different factors on the functional properties of WPP with emphasis on novel processing technologies, and interaction with other food ingredients     

Disulfide Bonds Influence the Heat-induced Gel Properties of Chicken Breast Muscle Myosin

The functions of thiol groups in the denaturation, aggregation and gelation of chicken breast muscle myosin during heating in 0.6M NaCl, 50mM sodium phosphate buffer, pH 6.5, was investigated by inhibiting disulfide (SS) bond formation using dithiothreitol (DTT). The endotherm of myosin heated in the presence or absence of DTT had similar thermal transition temperatures. Preventing SS bond formation increased the onset temperature for aggregation and gelation and decreased the elastic-like properties of the final gel matrix. Results indicated that SS bond formation was not a prerequisite for the gelation of chicken breast myosin. However, intermolecular SS bonds, especially from thiol groups on subfragment-1, contributed to gel network formation.