Protein and Salt Effects on Ca2+-Induced Cold Gelation of Whey Protein Isolate

Increasing whey protein concentration (from 6 to 10% w/v) decreased gel opacity but increased gel strength and water-holding capacity (WHC). Increasing CaCl₂, concentration (from 5 to 150 mM) increased gel opacity and gel strength at the high protein concentration (i.e., 10%). However, it lowered gel strength at protein concentration > 10%. Young's modulus and distance to fracture values indicated that gels were most rigid at 30 mM CaCl₂, at which point the extent of aggregation (measured by turbidity) was the highest. Increasing CaCl₂ concentration from 5 to 150 mM slightly affected the WHC of Ca²⁺-induced gels. Protein concentration was the major factor in determining fracture properties and WHC.     

Ca2+-Induced Gelation of Pre-heated Whey Protein Isolate

Addition of CaCl₂ to pre-heated whey protein isolate (WPI) suspensions caused an increase in turbidity when pre-heating temperatures were ≥ 64°C. Pre-heating to ≥ 70°C was required for gelation. WPI suspensions which contained CaCl₂ became turbid at 45°C and formed thermally induced gels at 66°C. Thermally and Ca²⁺-induced gels showed significant time/temperature effects but the penetration force values in the Ca²⁺-induced gels were always lower. However, Ca²⁺-induced gels were higher in shear stress at fracture. The Ca²⁺-induced gels had a fine-stranded protein matrix that was more transparent than the thermally induced gels, which showed a particulate microstructure.     

Temperature-Dependency of Rigor-Mortis of Fish Muscle: Myofibrillar Mg2+-ATPase Activity and Ca2+ Uptake by Sarcoplasmic Reticulum

Myofibrillar Mg²⁺-ATPase activity of plaice and red sea bream increased with increase in reaction temperature and Ca²⁺ concentration. However, temperature decrease tended to lower Ca²⁺ sensitivity of Mg²⁺-ATPase activity. While it was assumed that spiked fish muscle was relaxed and the myofibrillar Ca²⁺ concentration was low, the progress rate of rigor-mortis correlated well with Mg²⁺-ATPase activity in the presence of a few micromolar Ca²⁺ at 0°C. Correspondingly, it was found that Ca²⁺ uptake by plaice sarcoplasmic reticulum decreased with the decrease in reaction temperature. These results strongly suggest the acceleration of fish rigor-mortis at 0°C is due to the increase of Ca²⁺ concentration in myofibrils during storage at this temperature.     

Effects of Heat Processing on the Functionality of Whey Protein Concentrates

The effects of heat processing on the composition and functionality of whey protein concentrations (WPC) were investigated. WPC was manufactured from milk, whey and retentate that had either been pasteurized at 72°C for 15 sec or had received no heat treatment. Eight combinations of heat treatment were utilized. Pasteurization of the milk had a positive effect on overrun and foam stability, but a negative effect on gel strength at pH 6.5, protein hydrophobicity, and neutral lipid content. Pasteurization of the whey resulted in decreased mineral content bud did not affect functionality. Pasteurization of the retentate caused a decrease in emulsion capacity, soluble β-lactoglobulin, solubility, whipped topping overrun and gel strength at pH 8.0.     

KCI, CaCI2, Na+ Binding, and Salt Taste of Gum Systems

Aqueous nonionic (0.3% w/v) and ionic (0.1% and 0.3% w/v) gum systems containing NaCl, or equal weights of NaCl plus KCl, or NaCl plus CaCl, were examined. At equivalent molar concentrations of added ions, ²³Na NMR transverse relaxation rates (R₂, set^?1) showed an increase in average Na⁺ mobility with the addition of K⁺ or Ca²⁺ to ionic gum systems. Correspondingly, salt taste increased with addition of KCl as determined by Decision Boundary modeling of subject identification data. Viscosity did not affect saltiness. Na⁺ was free to induce salt taste when K⁺ was bound to the gum. Enhancement of salt taste by KCl is due, in part, to competitive binding of Na⁺ and K⁺ in a system.     

Mg2+ Selectively Isolates Gellan Gum from Dairy Products

Gellan gum was precipitated from the papain digest of dairy products by 5% MgSO₄. The precipitate was collected by centrifugation and washed with 2.5% MgSO₄ until the washings were negative to the phenol H_aSO₄ test. It was dispersed with hot 50% H₂SO₄ and the amount in the dispersion determined by the H₂SO₄-thiourea-cyste-ine-HCl reagent. Recovery from chocolate milk, yogurt, evaporated milk, ice cream, cream cheese, process cheese spread, flan and blue cheese (no oil) dressing ranged from 76–95%. Prior removal of fat and starch was unnecessary. Carrageenan, xanthan gum, alginate, pectin and other hydrocolloids did not interfere.     

Effects of pH, CaCl2 and Soy Protein on [Ca2+] in Reconstituted Nonfat Dry Milk and on Rennet-Induced Coagulum Properties

Increasing CaCl₂ and lowering pH caused a significant increase in [Ca²⁺] in reconstituted nonfat dry milk (RNDM), while the addition of soy protein caused a significant reduction in [Ca²⁺]. Lowering pH greatly increased rennet-induced coagulum firmness in RNDM and slightly increased it in RNDM-soy protein mixtures. Added CaCl₂ increased coagulum textural parameters and syneresis in both systems. The extent to which these properties were increased was higher in RNDM than in the coagulum containing soy protein depending on the time after rennet addition and the amount of CaCl₂ added. The first increment of CaCl₂ added had the highest effect in improving textural properties and increasing syneresis.     

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.     

Emulsifying Properties of Lipid-Reduced, and Calcium-Reduced Whey Protein Concentrates

Emulsifying properties of six experimental and three commercial control, lipid-reduced, and calcium-reduced whey protein concentrates (WPC) were evaluated on the basis of mean droplet size and creaming intensity in model emulsions. Mean droplet sizes ranged from 225 to 395 nm. Model emulsions made with a commercial control (WPC F), experimental lipid-reduced (WPC MF. 1, MF. 45), commercial lipid-reduced (WPC E), and experimental calcium and lipid-reduced (WPC B) samples had low stabilities. Emulsion stabilities of the WPC most strongly correlated with protein solubility and fatty acid compositions, but did not correlate with mean droplet size.     

Gelation Properties of Lipid-Reduced, and Calcium-Reduced Whey Protein Concentrates

Gels made from six experimental whey protein concentrate (WPC) processes using chemical pretreatment, ultrafiltration and microfiltration (MF) of Swiss cheese whey, and three commercial WPC, were compared for rheological, microstructural and sensory properties. Based on relations between shear stress (ST) and total sulfhydryl levels, we contirmed that disulfide bonding is important in gelation. Other components, i.e., lipids, lactose, calcium and sodium, interacting simultaneously, affected gel formation. Gel water holding capacity (WHC) was related to microstructure but not to ST. WHC was useful to characterize the 3-dimensional gel structure formations. Light microscopy showed the strongest gel had a fine-stranded, solvent-retaining structure.     

Acceleration of Postmortem Tenderization in Ovine Carcasses Through Activation of Ca2+ -Dependent Proteases

Infusion of lamb carcasses with 0.3M CaCl₂ resulted in acceleration of postmortem tenderization process. Control and treated animals had similar cathepsin B, H, and L activities. Various control groups had similar CDP-I, -II and inhibitor activities, whereas these were all decreased in CaCl₂ infused animals. Hence, it was concluded that the activation of Ca²⁺ -dependent proteases was responsible for the observed postmortem proteolysis and tenderization and, it seems unlikely that activity of these cathepsins is related to postmortem tenderization under conditions used in this experiment.     

Na+ Binding as Measured by 23Na Nuclear Magnetic Resonance Spectroscopy Influences the Perception of Saltiness in Gum Solutions

Binding of Na⁺ in aqueous gum systems as determined by ²³Na nuclear magnetic resonance (NMR) spectroscopy and its relations to perceived saltiness were examined. Two levels of NaCl (0.1% and 0.2%) were added to two concentrations (0.1% and 0.3%) of two ionic (xanthan and kappa carrageenan) and two non-ionic (locust bean and guar) gum solutions. Saltiness perception was affected by the ionic properties of the gums. NMR transverse relaxation rates (R₂, see^?l) indicated Na⁺ was less mobile in ionic than nonionic systems. Ionic gums correspondingly suppressed saltiness perception- compared to nonionic gums. As Na⁺ increased in both ionic and nonionic systems, R₂ values converged and perceived saltiness equalized. Food components that bind Na⁺ may suppress saltiness perception, which may be important in low-sodium foods.     

Composition, Physicochemical and Functional Properties of Reference Whey Protein Concentrates

Four reference whey protein concentrates (WPCs) were prepared from pasteurized and nonpasteurized acid casein whey and Cheddar cheese whey using ultrafiltration/diafiltration and spray drying processes. The WPCs exhibited comparable composition, protein solubility and PAGE and reverse phase HPLC properties. Major differences were observed in the viscosity and foaming properties of the reference WPCs as a function of pH. The WPCs generally produced higher foam expansion but lower viscosity and stability values than for liquid egg white protein. The findings were discussed in terms of the need for additional, fundamental knowledge of the physicochemical structure and reactivity of whey proteins to understand the reasons for their poor functional performance.     

Foaming Properties of Lipid-Reduced and Calcium-Reduced Whey Protein Concentrates

The ability of whey protein concentrates (WPC) to form highly expanded and stable foams is critical for food applications such as whipped toppings and meringue-type products. The foaming properties were studied on six experimental and three commercial WPC, manufactured by membrane fractionation processes to contain reduced lipids and calcium. Lipid-reduced WPC had excellent foaming properties. Experimental delipidized WPC MF 0.45 and commercial delipidized WPC E had higher (P < 0.05) foam expansion than egg white protein (EWP). However. WPC B made bv low-pH UF and isoelectric orecinitation did not form a foam. Lipids and ash were the main factors affecting foaming properties.     

Ca2+ Affects Physicochemical and Conformational Changes of Threadfin Bream Myosin and Actin in a Setting Model

The effect of Ca²⁺ on physicochemical and conformational changes of threadfin bream (TB) myosin and actin during setting at 25 and 40°C was investigated. Ca²⁺ ion at 10 to 100 mM induced the unfolding of myosin and actin as evident by an increase of surface hydrophobicity (S_o ANS) at 40 °C. Total SH groups also decreased with an increased Ca²⁺ concentration, suggesting that Ca²⁺ promoted the formation of disulfide bonds during setting at 40 °C. Both hydrophobic interactions and disulfide linkages were involved in formation of myosin aggregates at 40 °C and were enhanced by addition of 10 to 100 mM Ca²⁺. Myosin Ca‐ATPase activity decreased when Ca²⁺ was greater than 50 mM, indicating conformational changes of myosin head. Circular dichroism spectra demonstrated that Ca²⁺ reduced the α‐helical content of myosin and actin incubated at either 25 or 40 °C. Ca²⁺ induced conformational changes of TB myosin and actin incubated at 40 °C to a greater extent than at 25 °C.     

Influence of NaCl and CaCl2 on Cold-Set Gelation of Heat-denatured Whey Protein

Heat‐denatured whey‐protein isolate (HD‐WPI) solutions were prepared by heating a 10 wt% WPI solution (pH 7) to 80 °C for 10 min and then cooling it back to 30 °C. Cold‐set gelation was initiated by adding either NaCl (0 to 400 mM) or CaCl₂ (0 to 15 mM). Both salts increased the turbidity and rigidity of the HD‐WPI solutions. Gelation rate and final gel strength increased with salt concentration and were greater for CaCl₂ than NaCl at the same concentration because the former is more effective at screening electrostatic interactions and can form salt bridges.