Protein Extractability and Thermally Induced Gelation Properties of Myofibrils Isolated from Pre- and Postrigor Chicken Muscles

Purified chicken myofibrils were suspended in 0.6M NaCl at various pH values to study gelation properties of the myofibrils. Postrigor breast myofibrils showed a greater protein extractability and gel strength than prerigor breast myofibrils, but the reverse was found for leg myofibrils. Salt-soluble protein was least extractable at pH 5.50 for both breast and leg myofibrils. The pH for optimum gelation, indicated by increased penetration force, was 6.00 for breast and 5.50 for leg myofibrils. Heating at 1°C/min from 20 to 70°C produced stronger breast but weaker leg myofibril gels than isothermal heating at 70°C for 20 min. Muscle rigor state showed a greater effect on protein extractability and gel strength for breast myofibrils than for leg myofibrils.     

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.     

Chicken muscle homogenate gelation properties: effect of pH and muscle fiber type

Gelation properties of chicken breast and thigh muscle homogenates at a protein concentration of 4.5% under different pH conditions (5.80–6.60) and those of myofibrillar proteins at a protein concentration of 2% were compared to determine the influence of muscle fibre types on gelation. The optimal gelling pH for breast muscle homogenates (pH 6.30) was slightly higher than that for thigh muscle homogenates (pH 5.80–6.30), a similar trend was found for the isolated chicken myofibrillar proteins (pH 6.00 for breast and 5.50 for leg). Similarly, the pH values at which breast muscle homogenate gels were weaker (pH<6.20) or stronger (pH6.20) than thigh muscle homogenate gels were higher when compared with chicken breast and leg myofibrillar protein gels (pH<5.80 and pH>5.90, respectively).     

Physicochemical and Gelation Properties of Pre- and Postrigor Chicken Salt-soluble Proteins

The physicochemical and gelation properties of salt-soluble proteins (SSP) extracted from chicken muscles were studied at 0.6M NaCl, pH 6.00. Thermally induced protein unfolding and protein-protein interaction were determined by 8-anilino-1-naphthalene sulfonate (ANS) fluorescence and turbidity. Breast and leg SSP showed similar changes in protein unfolding, but differed in protein-protein interactions. Post-rigor breast SSP formed stronger and more elastic gels than prerigor breast and pre and postrigor leg SSP. Leg SSP gelation was less affected by muscle rigor state than breast SSP. Protein conformational changes were concluded to precede SSP association, which was a prerequisite for gel formation.     

Thermally Induced Interactions and Gelation of Combined Myofibrillar Protein from White and Red Broiler Muscles

The gelling properties of broiler myofibrillar protein were studied by determining protein-protein interactions during heating. Breast and leg salt-soluble protein (SSP) showed 1–3 transitions in protein-protein interactions within pH 5.5–6.5. The maximum transition temperatures of leg SSP decreased when leg SSP was mixed with breast SSP. The combined breast/leg myofibrils formed stronger gels than leg myofibrils alone at pH ≥ 6.0, and stronger gels than breast myofibrils alone at pH < 6.0. The results suggest that interactions existed between breast and leg myofibrillar proteins, and the transitions in these interactions were useful for predicting gel strength of the combined breast/ leg myofibrils.     

Changes in Protein Solubility and Gelation Properties of Chicken Myofibrils during Storage

The effect of storage on protein solubility and heat-induced gelation properties of chicken hen breast and leg myofibrils was investigated. Myofibrils suspended in 0.6M NaCl, pH 6.0, showed increasing protein solubility, viscosity, gel strength and water holding capacity with storage at 4°C. However, the effect of storage was most dramatic only during the initial 10 hr for all of the parameters studied. The relative distribution of the proteins comprising the salt soluble protein (SSP) extract changed during storage. Although storage had little effect on breast SSP, it was detrimental to leg SSP gelation. Breast myofibril suspensions, for all storage times, contained a greater amount of SSP and had better gelation properties than leg myofibril suspensions.     

Effect of Heating Rate on Thermally Formed Myosin, Fibrinogen and Albumin Gels

Myosin, fibrinogen and albumin gels were formed by heating in pH 6.0 phosphate buffer at three heating rates. Turbidity (A_660nm) and solubility were monitored along with gel strength, as measured with an annular pump. Myosin and fibrinogen suspensions became turbid and solubility decreased as temperatures preceding the development of gel strength. Linearly increasing heating rates of 12°C/hr and 50°C/hr produced the strongest myosin and fibrinogen gels at 70°C, whereas albumin gels formed at 95°C by heating at 12°C/hr or constant heating for 20 min did not differ in strength.     

Stability of milk protein concentrate suspensions to in-container sterilisation heating conditions

Milk protein concentrate (MPC) powders, ranging from 35 (MPC35) to 87 (MPC90)% protein, were reconstituted to 8.5% protein and assessed for heat stability at 120 °C, Ca-ion activity, heat-induced dissociation of κ-casein, and heat-induced gelation of serum-phase proteins in ultracentrifugal supernatants of unheated MPC suspensions. Heat stability of MPC suspensions depended on the protein content of the powder from which the suspensions were prepared. MPC70 had excellent heat stability compared with MPC35; however, MPC80, MPC85 and MPC90 were highly unstable to heating. Ca-ion activity increased with increasing protein content of the MPCs, whereas the extent of heat-induced dissociation of κ-casein and gelation of serum-phase proteins decreased. Increased heat stability with increasing protein content from MPC35 to MPC70 was attributed to decreased κ-casein dissociation and reduced gelation of serum-phase proteins. Despite these stabilising factors, excessively high Ca-ion activity caused MPC80, MPC85 and MPC90 to have very poor heat stability at pH 6.3–6.8, 6.3–7.1 and 6.3–7.3, respectively.     

pH Induced Aggregation and Weak Gel Formation of Whey Protein Polymers

Whey protein polymers were formed by heating (80 °C) a 4% (w/v) whey protein (WP) isolate dispersion at pH 8.0 for 15, 25, 35, 45, or 53 min. Dispersions were adjusted to pH 6.0, 6.5, 7.0, 7.5, or 8.0 after heating and the rheological properties were determined. Viscosity increased with increased heating time and decreased pH. At pH 7.0 and 7.5, high-viscosity dispersions with pseudoplastic and thixotropic flow behavior were formed, while weak gels were formed at pH 6.0 and 6.5. The storage (elastic) and loss (viscous) moduli of pH-induced gels increased when temperature was increased from 7 °C to 25 °C, suggesting that hydrophobic forces are responsible for gelation. Key Words: weak-gels, whey proteins, polymers, gelation, functionality     

Penetration Studies of Blood Globin Gels

Studies were made on the effect of temperature, pH and protein and salt concentration on the penetration force withstood by globin gels. The registered force increased with heating temperature (60 - 95°C) and protein concentration (1.4 - 5.0%). The gelation pH was dependent on both protein and salt concentration; the higher the protein or salt concentration the lower the gelation pH. At 3% protein concentration globin formed a gel around pH 5 - 6. At 0.7% concentration and higher, the presence of salt weakened the gel strength, while the addition of plasma increased the gelation pH of salt-containing globin gels. A substantially higher penetration force was measured for bovine globin gels than porcine globin gels. Further concentration and spray-drying decreased the gel strength of globin gels.     

Interaction of Myosin-Albumin and Myosin-Fibrinogen to Form Protein Gels

Myosin, fibrinogen, albumin, myosin-fibrinogen and myosin-albumin gels were formed by heating in pH 6.0 phosphate buffer at two heating rates. Gel strength was measured with an annular pump and soluble protein was determined. Myosin and fibrinogen interacted to form a gel which was stronger than the sum of the gel strengths for the two individual proteins. The strength of myosin-fibrinogen gels formed at 50°C was not affected by heating method; however, the strength of gels developed between 55°C and 70°C was related to heating method. Myosin and albumin did not interact to form a gel matrix until 80°C where sufficient thermal alteration of albumin had occurred.     

Development of a Test to Predict Gelation Properties of Raw Turkey Muscle Proteins

A method for extraction and fractionation of muscle proteins into five fractions based on salt (NaCl) solubility was developed. The influence of protein extractability, solubility, muscle pH and total protein on gelation was investigated. Shear stress (gel strength) and shear strain (gel deformability) at failure of cooked (70°C) comminuted turkey breast gels were correlated with the 10 min protein extract and proteins soluble in 0.30–0.35M NaCl. Shear strain was correlated with muscle pH and shear stress was sensitive to total protein. Meat pH and the extraction/fraction method can be used on raw meat to indicate functional properties related to texture of cooked meat.     

Effect of feed texture, meal frequency and pre-slaughter fasting on carcass and meat quality, and urinary cortisol in pigs

The gelation characteristics of myofibrillar proteins are indicative of meat product texture. Defining the performance of myofibrillar proteins during gelation is beneficial in maintaining quality and developing processed meat products and processes. This study investigates the impact of pH on viscoelastic properties of porcine myofibrillar proteins prepared from different muscles (semimembranosus (SM), longissimus dorsi (LD) and psoas major (PM)) during heat-induced gelation. Dynamic rheological properties were measured while heating at 1 °C/min from 20 to 85 °C, followed by a holding phase at 85 °C for 3 min and a cooling phase from 85 to 5 °C at a rate of 5 °C/min. Storage modulus (G′, the elastic response of the gelling material) increased as gel formation occurred, but decreased after reaching the temperature of myosin denaturation (52 °C) until approximately 60 °C when the gel strength increased again. This resulted in a peak and depression in the thermogram. Following 60 °C, the treatments maintained observed trends in gel strength, showing SM myofibrils produced the strongest gels. Myofibrillar protein from SM and PM formed stronger gels at pH 6.0 than at pH 6.5. Differences may be attributed to subtle variations in their protein profile related to muscle type or postmortem metabolism. Significant correlations were determined between G′ at 57, 72, 85 and 5 °C, indicating that changes affecting gel strength took effect prior to 57 °C. Muscle type was found to influence water-holding capacity to a greater degree than pH.     

Rapid Heating of Alaska Pollock and Chicken Breast Myofibrillar Proteins as Affecting Gel Rheological Properties

Surimi seafoods (fish/poikilotherm protein) in the U.S.A. are typically cooked rapidly to 90+°C, while comminuted products made from land animals (meat/homeotherm protein) are purposely cooked much more slowly, and to lower endpoint temperatures (near 70 °C). We studied heating rate (0.5, 25, or 90 °C/min) and endpoint temperature (45 to 90 °C) effects on rheological properties (fracture, small strain) of washed myofibril gels derived from fish (Alaska pollock) compared with chicken breast at a common pH (6.75). This was contrasted with published data on gelation kinetics of chicken myosin over the same temperature range. Heating rate had no effect on fracture properties of fish gels but slow heating did yield somewhat stronger, but not more deformable, chicken gels. Maximum gel strength by rapid heating could be achieved within 5 min holding after less than 1 min heating time. Dynamic testing by small strain revealed poor correspondence of the present data to that published for gelling response of chicken breast myosin in the same temperature range. The common practice of reporting small‐strain rheological parameters measured at the endpoint temperature was also shown to be misleading, since upon cooling, there was much less difference in rigidity between rapidly and slowly heated gels for either species.     

Functional Properties of Turkey Salt-Soluble Proteins

The functional properties of salt-soluble proteins (SSP) extracted from turkey breast and thigh were determined. Breast and thigh SSP extracts were comprised of similar proteins and there was no difference in the effect of pH and NaCl concentration on solubility. Gels formed in a pH 6.0, 0.5M NaCl phosphate buffer were stable to centrifugation and had the greatest rigidity. Gels formed at pH 7.0 with breast SSP were stable to centrifugation, whereas pH 7.0 thigh SSP gels were not consistently stable. Uniaxial compression was used to determine failure shear stress, failure shear strain and hardness of gels. Breast SSP at 25 mg/mL and 35 mg/mL formed gels suitable for compression analysis, whereas thigh SSP gels of similar concentration were too frail for analysis. Breast SSP had more favorable gelation properties than thigh SSP.     

Acid-induced gelation of whey protein polymers: effects of pH and calcium concentration during polymerization

Heating whey protein dispersions (90°C for 15 min) at low ionic strength and pH values far from isoelectric point (pH>6.5) induced the formation of soluble polymers. The effect of mineral environment during heating on the hydrodynamic characteristics and acid-induced gelation properties of polymers was studied. Whey protein dispersions (80 g/l) were denatured at different pH (6.5–8.5) and calcium concentrations (0–4 mm) according to a factorial design. At pH 6.5, the hydrodynamic radius of protein polymers increased with increasing calcium concentration, while the opposite trend was observed at pH 8.5. Intrinsic viscosity results suggested that heating conditions altered the shape of protein polymers. Whey protein polymers were acidified to pH 4.6 with glucono-δ-lactone and formed opaque particulate gels. The storage modulus and firmness of gels were both affected by conditions used to prepare protein polymers. As a general trend, polymers with high intrinsic viscosity produced stronger gels, suggesting a relationship between polymer shape and gel strength.Acid gelation properties of whey protein polymers makes them suitable ingredients for yoghurt applications. Using whey protein polymers to standardize protein content increased yoghurt viscosity to 813 Pa.s while using skim milk powder at same protein concentration increased yoghurt viscosity to 393 Pa.s. Water holding capacity of protein polymers in yoghurt was 19.8 ml/g compared to 7.2 ml/g for skim milk powder protein. Acid gelation properties of whey protein polymers are modulated by calcium concentration and heating pH and offers new alternatives to control the texture of fermented dairy products.     

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.     

HEAT-INDUCED GELATION AND PROTEIN-PROTEIN INTERACTION OF ACTOMYOSIN1

Natural actomyosin (NAM) and “crude” actomyosin formed gels yielding maximum strengths (from back extrusion force) at pH 5.0 and 5.5, respectively. At pH 6.0, NAM gels had a least protein concentration endpoint (LCE) value of 6 mg/ml. Gel strength increased exponentially with an increase of NAM concentration from 3.75–10 mg/ml. With constant time (30 min)-temperature heating, NAM gel forces increased by 20.5% (NS, P>0.05) in the 30–80°C range. Arrhenius plots of NAM interaction in solution and in gelation at pH 6.0 indicated two different reaction mechanisms within the temperature zones above and below approximately 35°C for solutions and 40°C for gels. Similarity of interaction slopes above the 35–40°C region suggested one reaction mechanism for NAM molecular aggregation in solution and gelation.     

Thermal Gelation of Brown Trout Myofibrils: Effect of Muscle Type, Heating Rate and Protein Concentration

The thermal gelation properties of myofibril solutions (KCl 0.6M; pH 6.0) from reared brown trout white and red muscles were analyzed by thermal scanning rheometry. With a heating rate of 1°C/min, red muscle myofibrils exhibited a lower gelation capacity than white muscle myofibrils at low temperatures. No difference was observed above 60°C where solid gels were formed from the two myofibril types. Increasing protein concentration or reducing heating rate increased the values of the rheological parameters at 80°C for the two muscle type myofibrils. With a low heating rate (0.25°C/min), white muscle myofibrils formed stronger gels whatever the temperature.     

The effect of pH and calcium ion on rheological behaviour of β‐lactoglobulin‐basil seed gum mixed gels

Effect of pH (4.5–7.5) and Ca²⁺ (0.01–0.5 m ) on gelation of single and mixed systems of 10% β‐lactoglobulin (BLG) and 1% basil seed gum (BSG) was investigated. The gelling point of BLG and BSG gels was strongly pH‐dependent, and stiffer gels formed at higher pH. The BLG gels were formed upon heating to 90 °C and reinforced on cooling to 20 °C; however, the gelation of BSG occurred at temperatures below 70 °C. By increasing Ca²⁺ concentration, storage modulus of BLG and BSG gels were increased, although pH had a greater effect than Ca²⁺. In contrast, mixed systems showed two distinct types of behaviour: BLG gel formation and BSG network, suggesting that phase‐separated gels were formed. In addition, higher strength was obtained for BLG‐BSG mixture at higher Ca²⁺ concentration.