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.     

Gelation of gellan – A review

Gellan is an anionic extracellular bacterial polysaccharide discovered in 1978. Acyl groups present in the native polymer are removed by alkaline hydrolysis in normal commercial production, giving the charged tetrasaccharide repeating sequence: → 3)-β-d-Glcp-(1 → 4)-β-d-GlcpA-(1 → 4)-β-d-Glcp-(1 → 4)-α-l-Rhap-(1 →. Deacylated gellan converts on cooling from disordered coils to 3-fold double helices. The coil–helix transition temperature (T_m) is raised by salt in the way expected from polyelectrolyte theory: equivalent molar concentrations of different monovalent cations (Group I and Me₄N⁺) cause the same increase in T_m; there is also no selectivity between different divalent (Group II) cations, but divalent cations cause greater elevation of T_m than monovalent. Cations present as counterions to the charged groups of the polymer have the same effect as those introduced by addition of salt. Increasing polymer concentration raises T_m because of the consequent increase in concentration of the counterions, but the concentration of polymer chains themselves does not affect T_m. Gelation occurs by aggregation of double helices. Aggregation stabilises the helices to temperatures higher than those at which they form on cooling, giving thermal hysteresis between gelation and melting. Melting of aggregated and non-aggregated helices can be seen as separate thermal and rheological processes. Reduction in pH promotes aggregation and gelation by decreasing the negative charge on the polymer and thus decreasing electrostatic repulsion between the helices. Group I cations decrease repulsion by binding to the helices in specific coordination sites around the carboxylate groups of the polymer. Strength of binding increases with increasing ionic size (Li⁺ < Na⁺ < K⁺ < Rb⁺ < Cs⁺); the extent of aggregation and effectiveness in promoting gel formation increase in the same order. Me₄N⁺ cations, which cannot form coordination complexes, act solely by non-specific screening of electrostatic repulsion, and give gels only at very high concentration (above ∼0.6 M). At low concentrations of monovalent cations, ordered gellan behaves like a normal polymer solution; as salt concentration is increased there is then a region where fluid “weak gels” are formed, before the cation concentration becomes sufficient to give true, self-supporting gels. Aggregation and consequent gelation with Group II cations occurs by direct site-binding of the divalent ions between gellan double helices. High concentrations of salt or acid cause excessive aggregation, with consequent reduction in gel strength. Maximum strength with divalent cations comes at about stoichiometric equivalence to the gellan carboxylate groups. Much higher concentrations of monovalent cations are required to attain maximum gel strength. The content of divalent cations in commercial gellan is normally sufficient to give cohesive gels at polymer concentrations down to ∼0.15 wt %. Gellan gels are very brittle, and have excellent flavour release. The networks are dynamic: gellan gels release polymer chains when immersed in water and show substantial recovery from mechanical disruption or expulsion of water by slow compression. High concentrations of sugar (∼70 wt % and above) inhibit aggregation and give sparingly-crosslinked networks which vitrify on cooling. Gellan forms coupled networks with konjac glucomannan and tamarind xyloglucan, phase-separated networks with kappa carrageenan and calcium alginate, interpenetrating networks with agarose and gelling maltodextrin, and complex coacervates with gelatin under acidic conditions. Native gellan carries acetyl and l-glyceryl groups at, respectively, O(6) and O(2) of the 3-linked glucose residue in the tetrasaccharide repeat unit. The presence of these substituents does not change the overall double helix structure, but has profound effects on gelation. l-Glyceryl groups stabilise the double helix by forming additional hydrogen bonds within and between the two strands, giving higher gelation temperatures, but abolish the binding site for metal ions by changing the orientation of the adjacent glucuronate residue and its carboxyl group. The consequent loss of cation-mediated aggregation reduces gel strength and brittleness, and eliminates thermal hysteresis. Aggregation is further inhibited by acetyl groups located on the periphery of the double helix. Gellan with a high content of residual acyl groups is available commercially as “high acyl gellan”. Mixtures of high acyl and deacylated gellan form interpenetrating networks, with no double helices incorporating strands of both types. Gellan has numerous existing and potential practical applications in food, cosmetics, toiletries, pharmaceuticals and microbiology.     

Sol-gel transition temperatures of high acyl gellan with monovalent and divalent cations from rheological measurements

The sol–gel transition temperatures of 0.1–1.0% high acyl gellan (HAG) with 0–200 mM NaCl or KCl and 0–20 mM CaCl₂ or MgCl₂ were determined using rheological measurements. Transition temperatures for monovalent cations, Na⁺ and K⁺, in the range of 50–80 °C were not significantly different (p > 0.5). Absence of thermal hysteresis was the salient feature. However, thermal hysteresis (∼4.4 °C) was observed for 0.1% HAG without added salt, but disappeared on increasing HAG and counterion concentrations. Few concentrations of HAG and added monovalent and divalent cations showed thermal hysteresis not higher than 2.5 °C. Transition temperatures for divalent cations were similar to those for monovalent cations although for considerably lower concentrations of Ca²⁺ or Mg²⁺. Increasing concentrations of monovalent and divalent counterions give rise to higher transition temperatures but not to higher storage moduli. This was interpreted as a lack of cross-link formation in the three-dimensional network structure of the gels. A single sol–gel transition diagram for monovalent cations is proposed, in which different zones associated with the presence of ordered and disordered conformations serve to identify the conditions in which HAG can exist in aqueous media.     

Gelling properties of a κ/ι hybrid carrageenan: effect of concentration and steady shear

The gelling properties of κ/ι hybrid carrageenans extracted from Portuguese seaweeds have been studied for various concentrations and shear conditions. The gel equilibrium storage modulus in 0.05 m KCl shows a power law dependence with the biopolymer concentration. Data analysis with a fibril model indicates that the fractal dimension of networking fibrils differ from the one displayed by pure κ‐ or ι‐carrageenan fibrils. κ/ι hybrid carrageenan gels show thermal hysteresis reminiscent from κ‐carrageenan gels under similar salt conditions. Application of steady shear rate during the cooling of a hot κ/ι hybrid carrageenan solution impedes the gel formation. However, a shear‐rate‐dependent gel structural rebuilding is observed after shear cessation. Shear‐processed gels are softer and show a depressed melting temperature when compared with gels formed under quiescent conditions. These experimental results are compared with data obtained with pure κ‐carrageenan and pure ι‐carrageenan solutions under similar steady shear and salt conditions.     

Characterization of the Effect of Solutes on the Water-Binding and Gel Strength Properties of Carrageenan

The water activity of carrageenan gels with incorporated solutes was determined by cryoscopic osmometry. Kappa (k), kappalambda (kλ) and iota (κ) carrageenan were utilized at concentrations of from 0.1 2% solids producing a sol, viscous sol, and gel. The solutes used were sucrose, NaCl, Na₂SO₄, KCl, NH₄Cl and urea at concentrations ranging from 0.05–1.0 kinetic units per kg H₂O. All the solutes were found to give a_w values as measured cryoscopically withhin 0.0005 units of literature values. The water activity of pure carrageenans at 0.1–2% solids was greater than 0.999. Addition of some solutes increased the water binding of the carrageenan-solute-water system as was found by a lower a_w than expected. This interaction effect increased with increasing concentration of solute and carrageenan and was greater for solutes with lower activity coefficients. The interaction effect increased in the following order: Na₂SO₄, NaCl, KCl, and NH₄ Cl. The force required to rupture the gel was measured using the Instron Universal Testing Machine. Solutes were found to influence the gel strength of k and kλ carrageenans, but not ι carrageenan. The solutes increased kλ carrageenan's gel strength in increasing order: urea, sucrose, Na₂SO₄, NaCl, NH₄Cl, and KCl and k carrageenan's gel strength in increasing order: sucrose, Na₂SO₄ and NaCl. There appears to be no simple relationship between gel strength and water-binding when solutes are added to carrageenan.     

Factors that determine the fracture properties and microstructure of globular protein gels

Protein gel matrices are responsible for the texture of many foods. Therefore an understanding of the chemical reactions and physical processes associated with fracture properties of gels provides a fundamental understanding of select mechanical properties associated with texture. Globular proteins form thermally induced gels that are classified as fine-stranded, mixed or particulate, based on the protein network appearance. The fundamental properties of true shear stress and true shear strain at fracture, used to describe the physical properties of gels, depend on the gel network. Type and amount of mineral salt in whey protein and β-lactoglobulin protein dispersions determines the type of thermally induced gel matrix that forms, and thus its fracture properties. A fine-stranded matrix is formed when protein suspensions contain monovalent cation (Li⁺, K⁺, Rb⁺, Cs⁺) chlorides, sodium sulfate or sodium phosphate at ionic strengths ≤0.1 mol/dm³. This matrix has a well-defined network structure, and varies in stress and strain at fracture at different salt concentrations. At ionic strengths >0.1 mol/dm³ the matrix becomes mixed. This network appears as a combination of fine strands and spherical aggregates, and has high stress values and minimum strain values at fracture. Higher concentrations of monovalent cation salts cause the formation of particulate gels, which are high in stress and strain at fracture. The salt concentration required to change microstructure depends on the salt's position in the Hofmeister series. The formation of a particulate matrix also occurs when protein suspensions contain low concentrations (10–20 mol/dm³) of divalent cation (Ca²⁺, Mg²⁺, Ba²⁺) chloride salts or di-cationic 1,6-hexanediamine at pH 7.0. The divalent cation effect on β-lactoglobulin gelation is associated with minor changes in tertiary structure involving amide—amide interproton connectivities (determined by ¹H NMR) at 40–45°C, increasing hydrophobicity and intermolecular aggregation. The type of matrix formed appears to be related to the dispersed or aggregated state of proteins prior to denaturation. Mixed and particulate matrices result from conditions which favor aggregation at temperatures (25–45°C) which are much lower than the denaturation temperature (~65°C). Therefore, general (e.g. Hofmeister series) and protein-specific factors can affect the dispersibility of proteins and thereby determine the microstructure and fracture properties of globular protein gels.     

CARRAGEENAN MEDIATED CLARIFICATION OF DIALYSED WORT SYSTEMS

Fining trials with kappa-carrageenan in dialysed wort demonstrated that potassium or calcium cations were essential for the flocculation of non-microbiological particulate material. The relative ability of metal cations to promote flocculation followed identical trends as established for carrageenan helix stabilising action and gelation (K⁺ > Ca²⁺ > Na⁺). Carrageenan also exhibited interaction with soluble wort polypeptides, in particular fractions of relative molecular mass (Mr) 70 000 and 40 000. This interaction occurred in the absence of added metal cations and was suppressed by increasing concentrations of potassium or calcium. Addition of sodium ions to systems containing potassium had no effect on either interaction with soluble polypeptides or the flocculation of particulate material. Decreasing the pH of dialysed wort impaired flocculation reactions but enhanced removal of soluble wort polypeptides. These results suggest that reaction between carrageenan and soluble polypeptides occurs via electrostatic interactions whereas flocculation of particulate material requires the presence of carrageenan in a helical conformation.     

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.     

Gelling Properties of Gellan Solutions Containing Monovalent and Divalent Cations

Gelling temperatures of gellan solutions with the addition of Na⁺ and K⁺ ranging from 15 to 450 mM or Ca⁺⁺ and Mg⁺⁺ from 2 to 40 mM were determined by dynamic rheological testing at four polymer concentrations between 0.4 and 2.0% (w/w). Gelling temperatures were much higher for gellan solutions containing divalent cations than for those containing the same amount of monovalent cations. Solutions containing K⁺ gelled at higher temperatures than those containing Na⁺. Effects of Ca⁺⁺ and Mg⁺⁺ on gelling temperatures were not significantly different. A general model was developed to predict the gelling temperature of gellan solutions as functions of cation and polymer concentrations.     

Molecular forces involved in heat-induced pea protein gelation: Effects of various reagents on the rheological properties of salt-extracted pea protein gels

The molecular forces involved in the gelation of heat-induced pea protein gel were studied by monitoring changes in gelation properties in the presence of different chemicals. At 0.3 M concentration, sodium thiocyanate (NaSCN) and sodium chloride (NaCl) showed more chaotropic characteristic and enhanced the gel stiffness, whereas sodium sulfate (Na₂SO₄) and sodium acetate (CH₃COONa) stabilized protein structure as noted by increasing denaturation temperatures (T_d) resulting in reduced storage moduli (G′). To determine the involvement of non-covalent bonds in pea protein gelation, guanidine hydrochloride (GuHCl), propylene glycol (PG), and urea were employed. The significant decrease in G′ of pea protein gels with the addition of 3 M GuHCl and 5 M urea indicated that hydrophobic interactions and hydrogen bonds are probably involved in pea protein gel formation. The increase in G′ with increasing PG concentration (5–20%), demonstrated hydrogen bonds and electrostatic interaction involvement. No significant influence was observed on G′ with addition of different concentrations of β-mercaptoethanol (2-ME), low levels of dithiothreitol (DTT), and up to 25 mM N-ethylmaleimide (NEM), which indicated that disulfide bonds are not required for gel formation, but data at higher DTT and NEM concentrations and slow cooling rates showed a minor contribution by disulfide bonds. Reheating and recooling demonstrated that gel strengthening during the cooling phase was thermally reversible but not all the hydrogen bonds disrupted in the reheating stage were recovered when recooled.     

Salt-induced modulation in inorganic nutrients, antioxidant enzymes, proline content and seed oil composition in safflower (Carthamus tinctorius L.)

BACKGROUND: Safflower (Carthamus tinctorius L.) has gained considerable ground as a potential oil‐seed crop. However, its yield and oil production are adversely affected under saline conditions. The present study was conducted to appraise the influence of salt (NaCl) stress on yield, accumulation of different inorganic elements, free proline and activities of some key antioxidant enzymes in plant tissues as well as seed oil components in safflower. Two safflower accessions differing in salt tolerance (Safflower‐33 (salt sensitive) and Safflower‐39 (salt tolerant)) were grown under saline (150 mmol L^?1) conditions and salt‐induced changes in the earlier‐mentioned physiological attributes were determined. RESULTS: Salt stress enhanced leaf and root Na⁺, Cl^? and proline accumulation and activities of leaf superoxide dismutase, catalase and peroxidase, while it decreased K⁺, Ca²⁺ and K⁺/Ca²⁺ and Ca²⁺/Na⁺ ratios and seed yield, 100‐seed weight, number of seeds, as well as capitula, seed oil contents and oil palmitic acid. No significant effect of salt stress was observed on seed oil α‐tocopherols, stearic acid, oleic acid or linoleic acid contents. Of the two safflower lines, salt‐sensitive Safflower‐33 was higher in leaf and root Na⁺ and Cl^?, while Safflower‐39 was higher in leaf and root K⁺, K⁺/Ca²⁺ and Ca²⁺/Na⁺ and seed yield, 100‐seed weight, catalase activity, seed oil contents, seed oil α‐tocopherol and palmitic acid. Other attributes remained almost unaffected in both accessions. CONCLUSION: Overall, high salt tolerance of Safflower‐39 could be attributed to Na⁺ and Cl^? exclusion, high accumulation of K⁺ and free proline, enhanced CAT activity, seed oil α‐tocopherols and palmitic acid contents. Copyright © 2011 Society of Chemical Industry     

Effect of polysaccharides with different ionic charge on the rheological,microstructural and textural properties of acid milk gels

The effects of addition of polysaccharides with different ionic charge on rheology, microstructure, texture and water holding capacity (WHC) of acid milk gels were studied and compared to that of gelatin addition. Similar to gelatin, starch (neutral) and xanthan gum (anionic) did not prevent milk gelation in the first 30 min of the acidification stage, even at high concentrations, and the typical casein network in acid milk gels could still be seen from electron micrographs; gelling and melting of these hydrocolloids were observed during the cooling and heating stages at specific concentrations. On the other hand, two neutral polysaccharides, guar gum (≥ 0.05%) and locust bean gum [LBG] (≥ 0.1%) inhibited milk gelation from the beginning of the acidification stage; the microstructure of the gel was modified greatly and no gelling/melting was observed during the cooling or heating stages. Another anionic polysaccharide, carrageenan, induced earlier milk gelation at low concentration (≤ 0.05%), but inhibited gelation entirely at high concentration (0.2%); inflections at ~ 27 °C and 21 °C were also observed during the cooling and heating stages at 0.05% concentration. The gel microstructure was not changed greatly, but showed smaller particle size at a carrageenan concentration of 0.05% than control sample. None of the polysaccharides showed as much improvement in WHC of the milk gels as gelatin did. Hence, xanthan and starch were found to be closer to gelatin in their effect on acid milk gels compared to guar gum, LBG and carrageenan.     

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.     

The effect of shear on the rheology and structure of heat‐induced whey protein gels

The influence of mechanical shearing on the small deformation properties and microstructure of heat‐induced whey protein gel has been studied. The viscoelastic properties of these gels at different concentrations of 10% and 20% (w/w) exposed to different shear rates of 0, 50, 100, 200 and 500 s^?1 during gelation were measured using dynamic oscillatory rheometry. The structure of both the shear treated and unsheared gels was then investigated using light microscopy. The results showed that the storage modulus of the gels at both concentrations was increased by increasing the shear rate exposure during gelation while the shear‐treated gels were more elastic and showed frequency‐independent behaviour. As the total protein concentration of the gel increased, the viscoelastic properties of the gels also increased significantly and the gels showed greater elasticity. The gels obtained from the higher shear rate exposure were stronger with higher elastic moduli at both protein concentrations. Images of the gels obtained using light microscopy showed that shearing resulted in phase separation and some aggregation in the structure of the gels at both concentrations. However, the shearing rates applied in this study were not enough to cause aggregation breakdown in the gel network.     

Gel—sol transition in gellan gum solutions. II. DSC studies on the effects of salts

The thermal properties of sodium form gellan gum solutions with and without sodium chloride, potassium chloride, calcium chloride and magnesium chloride were studied by differential scanning calorimetry (DSC). The DSC cooling or heating curves for 1% gellan gum solutions without salt showed a single exothermic or endothermic peak at ~30°C. DSC cooling curves showed a single exothermic peak, with the setting temperature (Ts) shifting to progressively higher temperatures with increasing concentration of the added NaCl or KCl. At low concentrations of NaCl or KCl, DSC heating curves showed a single endothermic peak; however with more addition of salt the endothermic peak gradually developed a bimodal character and eventually split into more than two distinct peaks. The onset of detectable splitting occurred at a high salt concentration which coincided with that at which elastic gels are formed at even a higher temperature as was observed by viscoelastic measurements. With a sufficient addition of monovalent cations the endothermic curve became again a single peak shifting to higher temperatures. In the presence of divalent cations, although Ts shifted to higher temperatures with increasing concentration of added CaCl₂ or MgCl₂, the melting temperature (Tm) in heating DSC curves shifted to higher temperatures (up to a certain temperature) and then shifted to lower temperatures with increasing concentration of salt. With increasing concentration of CaCl₂ or MgCl₂, the exothermic and endothermic enthalpies estimated for a main peak increased up to a certain salt concentration and then decreased; however many other peaks were observed at higher temperatures. The endothermic peaks for gels with excessive divalent cations were too broad to be resolved from the baseline; in contrast the exothermic peaks were much sharper and readily recognized. In comparing thermal properties with rheological properties, gellan gum solutions with excessive divalent cations form firm gels on cooling to below the setting temperature, and then it was difficult to remelt them. This was quite different from the behaviour of thermoreversible gels formed in the presence of monovalent cations. It seems that the mechanism of gel formation in gellan gum with divalent cations is markedly different from that with monovalent cations.     

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.     

Viscoelastic Properties of Xanthan Gels Interacting with Cations

Viscoelastic properties of gels were greatly affected by xanthan gum concentration and types of cations. The storage moduli (G'), measured at 1.0 Hz, were 8.3, 10, and 2700 Pa for xanthan gels at 0.5% polymer concentration and 37, 42, and 13000 Pa for xanthan gels at 1.0% polymer concentration in the presence of Na⁺, Ca²⁺, or Fe³⁺, respectively. The elastic recovery was 27.9, 61.6, and 66.3% for 0.5% xanthan gels, and 38.5, 22.5, and 69.1% for 1.0% xanthan gels, in the presence of Na⁺, Ca²⁺, or Fe³⁺, respectively. The generalized Kelvin model simulated creep compliance and ferric ion was an excellent crosslinker for a rigid, firm gel.     

Deletion of the N-terminal domain of the yeast vacuolar (Na+,K+)/H+ antiporter Vnx1p improves salt tolerance in yeast and transgenic Arabidopsis

Cation/proton antiporters play a major role in the control of cytosolic ion concentrations in prokaryotes and eukaryotes organisms. In yeast, we previously demonstrated that Vnx1p is a vacuolar monovalent cation/H⁺ exchanger showing Na⁺/H⁺ and K⁺/H⁺ antiporter activity. We have also shown that disruption of VNX1 results in an almost complete abolishment of vacuolar Na⁺/H⁺ exchange, but yeast cells overexpressing the complete protein do not show improved salinity tolerance. In this study, we have identified an autoinhibitory N-terminal domain and have engineered a constitutively activated version of Vnx1p, by removing this domain. Contrary to the wild type protein, the activated protein has a pronounced effect on yeast salt tolerance and vacuolar pH. Expression of this truncated VNX1 gene also improves Arabidopsis salt tolerance and increases Na⁺ and K⁺ accumulation of salt grown plants thus suggesting a biotechnological potential of activated Vnx1p to improve salt tolerance of crop plants.     

Modulation of thermal stability and heat-induced gelation of β-lactoglobulin by high glycerol and sorbitol levels

The influence of glycerol and sorbitol on the thermal stability and heat-induced gelation of β-lactoglobulin (β-lg) in aqueous solutions was investigated. The thermal stability of β-lg was characterized by measuring the thermal denaturation temperature (T_m) using differential scanning calorimetry, while its gelation properties were characterized by measuring the gelation temperature (T_gel) and final gel rigidity (G^∗) using dynamic shear rheology. All experiments were carried out using aqueous solutions containing 10% (w/w) β-lg, glycerol (0–70% w/w) or sorbitol (0–55% w/w), and 5 mM phosphate buffer (pH 7.0). No salt was added to these solutions so that there was a relatively strong electrostatic repulsion between the protein molecules, which usually prevents gelation. When the cosolvent concentration was increased from 0% to 50%, T_m increased from 74 to 86 °C for sorbitol, but only from 74 to 76 °C for glycerol, which indicated that sorbitol was much more effective at stabilizing the native state of the globular protein than glycerol. Protein solutions containing sorbitol (0–55%) did not form a gel after heating, but those containing glycerol formed gels when the cosolvent concentration exceeded about 10%, with G^∗ increasing with increasing glycerol concentration. We attribute these effects to differences in the preferential interactions of polyols and water with the surfaces of native and heat-denatured proteins, and their influence on the protein–protein collision frequency.     

Structural and mechanical characterization of κ/ι-hybrid carrageenan gels in potassium salt using Fourier Transform rheology

The mechanical and structural properties of κ/ι-hybrid carrageenan gels obtained at various concentrations in the presence of 0.1 m KCl were studied with Fourier Transform rheology (FTR) and cryoSEM imaging. FTR data show that gels formed at concentration below 1.25 wt% exhibit a strain hardening behavior. The strain hardening is characterized by a quadratic increase of the scaled third harmonic with the strain and a third harmonic phase angle of zero degree. Both features are weakly depending on the concentration and conform to predictions from a strain hardening model devised for fractal colloidal gels. However, the phase angle of the third harmonic reveals that κ/ι-hybrid carrageenan gels obtained at higher concentrations show shear thinning behavior. Colloidal gel models used to extract structural information from the concentration scaling of gel equilibrium shear modulus G₀ and the strain dependence of FTR parameters suggest that κ/ι-hybrid carrageenan gels are built from aggregating rod-like strands (with fractal dimension x = 1.13) which essentially stretch under increasing strain. The mechanically relevant structural parameters fairly match the gel fractal dimension (d = 1.66) obtained from the cryoSEM analysis.