Water-Holding Capacity in Hard-to-Cook Beans (Phaseolus vulgaris): Effect of pH and Ionic Strength

The effect of pH and ionic strength (IS) of soaking solution on the water holding capacity (WHC) of hard-to-cook (HTC) and control black beans (Phaseolus vulgaris) was evaluated. Beans were soaked 18 hr in solutions covering the pH range 1–7 at constant IS (1.0 M) or in solutions ranging in IS from 0.01 to 1.3M (prepared with either NaCl or CaCl₂) at pH 7. WHC was significantly reduced in the pH range 3.5 to 5.1 in control beans but the effect was not as pronounced with HTC samples which had a lower WHC at each pH. Solutions prepared with NaCl produced significantly lower WHC values than CaCl₂ solutions in the control but not in the HTC beans. WHC values in control beans tended to increase with higher IS, although this effect was not as apparent for HTC beans.     

Effect of amino acid,pH and mineral salts on glass transition and flow behaviour of soy protein concentrate

The objective of this study was to assess the effect of proline, mineral salts (NaCl and Na₂SO₄) and pH combined with moisture content on the glass transition temperature (T_g) and flow‐starting temperature (T_f) of soy protein concentrate (SPC). Initial screening of the variables based on fractional factorial design showed insignificant effect of NaCl on T_g and T_f. The design was extended to a face‐centred central composite design (CCD) excluding NaCl and data evaluated by use of response surface methodology. The established model for T_g (R² = 0.824) shows significant negative first‐order effects of moisture, proline and Na₂SO₄, and a positive interaction effect of moisture and Na₂SO₄. The T_f model (R² = 0.937) shows significant negative first‐order effects of moisture and proline, a positive first‐order and negative square effect of pH, and a negative interaction effect of moisture and proline. The main effect on T_g and T_f was 2.2 and 1.3 times higher, respectively, for moisture compared to proline. The study confirms that proline (or other free amino acids) can replace moisture as protein plasticiser in the extrusion process. Minor effects can also be obtained by reduction in pH.     

Changes of glycinin conformation due to pH, heat and salt determined by differential scanning calorimetry and circular dichroism

Conformational changes of glycinin caused by either pH, heat or salt were investigated using differential scanning calorimetry (DSC) and circular dichroism (CD). Glycinin of more than 97% purity was used for the experiments. Without the presence of salt (NaCl), glycinin (protein concentration of 16%) was most stable at pH 4.5; the temperature for midpoint of transition (T_m) and enthalpy change (ΔH) were 93.5 °C and 18.1 J g^?1 protein, respectively. Both parameters decreased gradually as the pH of the protein solution was increased to 9.5. The endothermic peak of glycinin disappeared when the pH was >11.5 or <3.0. DSC results showed that with increasing of salt concentration, glycinin was substantially stabilized even in acidic (pH 3.0) and alkaline (pH 11.5) conditions; the degree of stabilization was more significantly affected at the acidic pH. The CD profiles of soy glycinin were, however, not significantly altered even in acidic and alkaline conditions. Thermal denaturation was suppressed by NaCl even in 90 °C, pH 8.0, when the salt concentration was 0.45 m . The stabilizing effects of NaCl coincided with an increase in the percentage of α‐helix in glycinin. Therefore, soy glycinin appeared to have a well‐ordered structure under the pH conditions studied, especially in the presence of NaCl. The λ_min signal at 222 nm remained unchanged up to 80 °C, but the negative intensity increased substantially when the temperature was >80 °C.     

Rheological and Thermal Properties of Extruded Mixtures of Rice Starch and Isolated Soy Protein

Many foods gain new mechanical, thermal and textural properties after being processed due to interactions between carbohydrates and proteins. This effect is characteristic for each foodstuff. The properties of extruded isolated soy protein (ISP) and rice starch were studied considering the following extrusion variables: starch proportion with respect to ISP (0–100%), pH (3–9), moisture content (20–30%) and temperature (140–180ºC). The following characteristics were measured: Water absorption index (WAI), water solubility index (WSI), glass transition temperature (T_g), melting temperature (T_m), viscosity at 90ºC and at 50ºC, storage (G′), loss modulus (G′′) and tan δ. The results indicate that the extruded starch exhibits higher WAI and WSI values than untreated starch. For extruded ISP these values are much lower than for untreated ISP. Extrudates with higher starch proportion had higher T_g and T_m values; pH has a significant effect (p<0.05), at pH 3 higher T_g values were observed, and at pH 9 higher values of T_m. The highest viscosities at 90ºC and 50ºC were observed for extrudates with a higher starch proportion and pH 9. Extruded mixtures showed a more elastic than viscous behavior and an extruded 1:1 blend of starch‐ISP exhibited the behavior of a viscous liquid.     

Heat resistance of Escherichia coli O157:H7 in cook‐in‐bag ground beef as affected by pH and acidulant†

Summary The heat resistance of a four‐strain mixture of Escherichia coli O157:H7 was tested. The temperature range was 55–62.5 °C and the substrate was beef at pH 4.5 or 5.5, adjusted with either acetic or lactic acid. Inoculated meat, packaged in bags, was completely immersed in a circulating water bath and cooked to an internal temperature of 55, 58, 60, or 62.5 °C in 1 h, and then held for pre‐determined lengths of time. The surviving cell population was enumerated by spiral plating meat samples on tryptic soy agar overlaid with Sorbitol MacConkey agar. Regardless of the acidulant used to modify the pH, the D ‐values at all temperatures were significantly lower (P < 0.05) in ground beef at pH 4.5 as compared with the beef at pH 5.5. At the same pH levels, acetic acid rendered E. coli O157:H7 more sensitive to the lethal effect of heat. The analysis of covariance showed evidence of a significant acidulant and pH interaction on the slopes of the survivor curves at 55 °C. Based on the thermal‐death–time values, contaminated ground beef (pH 5.5/lactic acid) should be heated to an internal temperature of 55 °C for at least 116.3 min and beef (pH 4.5/acetic acid) for 64.8 min to achieve a 4‐log reduction of the pathogen. The heating time at 62.5 °C, to achieve the same level of reduction, was 4.4 and 2.6 min, respectively. Thermal‐death–time values from this study will assist the retail food processors in designing acceptance limits on critical control points that ensure safety of beef originally contaminated with E. coli O157:H7.     

Purification and identification of interacting components in a wheat starch–soy protein system

The objective of this research was to quantify the solubility, hydrophobicity and interaction characteristics of wheat–starch proteins (puroindoline, gliadin and glutenin) and protein-containing soy fractions (soy flour isolate [SFI], SFI 7S and 11S fractions, hexane-extracted textured soy flour [TVP] isolate, TVP 7S and 11S fractions, expelled, extruded soy flour [TSP] isolate, TSP 7S and11S fractions). Functional characteristics were assessed in aqueous sucrose solutions at pH 5.5 and 7.5 after heating to 25, 50, and 100 °C. Textured soy protein fractions were more soluble and had higher surface hydrophobicity profiles than their untextured counterparts. Sucrose addition decreased hydrophobicity in the textured proteins but increased it in untextured proteins. Characteristics of the isolate, as a whole, appear to be dictated by those of its 11S moiety. Dissociation constants (K_d values) for soy protein and starch-derived puroindoline were determined and indicated an extremely short association in all cases. The 11S fractions formed a complex with puroindoline in solution; however 7S fractions did not.     

In Vitro Digestibility of Phytate-Reduced and Phenolics-Reduced Soy Protein Isolates

The effect of removal of phytate and phenolic compounds upon the in vitro digestibility of soy protein isolates by trypsin and pronase enzymes at pH 8.0 and by pepsin at pH 2.0 was studied by pH stat and dialysis equilibrium methods, respectively. Phenolics-reduced (PRSPI) and phytate and phenolics-reduced (PPRSPI) soy protein isolates were both slightly more digestible than control (CSPI). 11S soy-protein with 0.07% phytate was slightly more digestible than 7S soy protein with 1.41% phytate. Kinetic studies indicated that differences in in vitro digestibility of soy protein isolates was probably due to accumulation of end products rather than stearic hindrance at enzyme-substrate reaction sites.     

Physical Properties of Whey Protein Stabilized Emulsions as Related to pH and NaCl

Corn oil-in-water emulsions (20 wt%, d₃₂～ 0.6 μm) stabilized by 2 wt% whey protein isolate were prepared with a range of pH (3–7) and salt concentrations (0–100 mM NaCl), and particle size, rheology and creaming were measured at 30°C. Appreciable droplet flocculation occurred near the isoelectric point of whey protein (pH 4–6), especially at higher NaCl concentrations. Droplet flocculation increased emulsion viscosity and decreased stability to creaming. Results are related to the influence of environmental conditions on electrostatic and other interactions between droplets.     

Hydrolysates of native and modified soy protein isolates: structural characteristics,solubility and foaming properties

The effect of enzymatic hydrolysis on structure characteristics (surface aromatic hydrophobicity and molecular size) of both native and modified soy protein isolates was studied. Effects on thermal behavior and functional properties (solubility and foam formation and stabilization at pH 4.5) were also analysed. Hydrolysates were obtained by bromelain digestion at pH 8 of native (N) and of thermally treated isolates at pH 7 (T7) and at pH 1.6 (T1.6). The differential effect of bromelain on the three isolates produced partially hydrolyzed structures, which exhibited an enhancement of their protein solubility (S_TCA and S_{pH 4.5}). Bromelain digestion was more effective on isolate T7 resulting hydrolysates with improved capacity to form foams at pH 4.5. The different functional behavior at pH 4.5 of hydrolysates was explained through the changes in thermal behavior, surface aromatic hydrophobicity and molecular mass distribution.     

Effect of pH on the growth,nodulation and nitrogen fixation of Centrosema pubescens and Stylosanthes gracilis

Centrosema pubescens and Stylosanthes gracilis were grown on two soils of different texture adjusted to pH values ranging from 5–7 to 8–0 by the addition of either dilute sulphuric acid or calcium carbonate. Centrosema grew best on a soil having final pH values of 6–1, while Stylosanthes grew best on a soil having a final pH value of 5–7. Nodulation followed a similar trend with dry matter yields but was increasingly suppressed by increases in pH, with complete suppression in some cases at pH8. Maximum nitrogen fixation in both cases occurred at a pH value of about 6.     

Association of Zinc with Soy Proteins as Affected by Heat and pH

The effect of heat on the chemical association of ⁶⁵Zn with proteins and of pH on the solubility of proteins, phytic acid, zinc, and their complex formation were studied in soybeans grown hydroponically and intrinsically labeled with ⁶⁵Zn. ⁶⁵Zn association with soy proteins was not affected by autoclaving. Zinc was not covalently associated with the major soy proteins, 11S and 7S. Protein, phytic acid and zinc content of the raw soyflour was determined at pH range 3.5–12 before and after dialysis. pH had only a slight effect on zinc solubility. Protein-zinc-phytate complex formation was maximum in the pH range 7.5–10.5.     

The solubility of potato proteins from industrial potato fruit juice as influenced by pH and various additives

The effects of pH and various additives on the precipitation and (re)solubility at pH 7 of potato proteins from industrial potato fruit juice (PFJ) were studied. The use of various strong and weak acids did not result in differences in protein precipitation, which on average occurred to a maximum of 60% of total protein at pH 3. Weak acids did, however, result in precipitates with a higher resolubility at pH 7 compared with strong acids. At pH 5, addition of FeCl₃ or ZnCl₂ increased both precipitation and resolubility compared with the situation without additives. The largest increases in both precipitation and resolubility were achieved using organic solvents at pH 5 as an additive, resulting in a maximum precipitation and maximum resolubility at pH 7 of 91 and 83% of total protein respectively. The results described in this study lead to the hypothesis that precipitation and resolubilisation of potato proteins from PFJ are not determined by their isoelectric pH but by their interactions with low‐molecular‐weight components. © 2001 Society of Chemical Industry     

The effect of pH,salts and sugars on the rheological properties of cress seed (Lepidium sativum) gum

Effect of shear rate (15–600 s^?1), gum concentration (1–2%), pH (3–9), sucrose (10–40%), lactose (5–15%), NaCl (100–300 mm ) and CaCl₂ (5–50 mm ) was evaluated on apparent viscosity (η_a), flow behaviour index (n), consistency coefficient (K) and yield stress (τ₀) indices of cress seed gum (CSG) solutions. Different rheological models were used to fit the experimental data, although the Herschel–Bulkley model was found the best model. An increase in gum concentration led to an increase in τ₀, η_a, and k and a decrease in n values. The addition of salts lowered the k value; however, the n value showed slight significant change. The presence of sugar resulted in the enhancement of n, k, τ₀ and η_ap values. The existence of yield stress and pseudoplastic behaviour of CSG, its stability against salts, wide range of pH and synergic effect of sugar make it a good thickener and stabiliser in food formulations.     

Effect of pH and temperature on the thermostability of prickly pear (Opuntia ficus‐indica) yellow‐orange pigments

The colour stability of the yellow‐orange pigment (λ_max = 476 nm) of prickly pear (Opuntia ficus‐indica) fruit was determined as a function of temperature and pH. The experiments were carried out at three different temperatures (50, 70 and 90°C) with pigment solutions at pH values ranging from 2–7. The degree of pigment retention decreased with increasing temperature as a function of increasing thermal exposure time with least pigment degradation at pH 5. The reaction rate constants were determined as 0.0062, 0.0383 and 0.1102 min^–1 for a thermal degradation reaction rate of pseudo‐first order. The activation energy was calculated as 65.1 kJ·mol^–1.     

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.     

Soybean Protein Dispersions at Acid pH. Thermal and Rheological Properties

The influence of pH, protein concentration, and ionic strength, on rheological properties of thermally treated acidic soy protein dispersions, was studied. Structural changes due to pH effect and thermal treatment were analized. DSC-thermograms at pH 3.5 showed a shoulder at 74.11±0.16°C that could be attributed to both β-conglycinin and the hexameric form of glycinin; and a peak at 81.88±0.29°C corresponding to 11S dodecameric form. At pH 2.75 one endotherm corresponded to denaturation of β-conglycinin. The acidic dispersions presented pseudoplastic behavior with_app values higher than those at pH 8.0. At pH 3.50 the ±_app was higher than at pH 2.75.The maximum viscoelasticiy was obtained with addition of 0.1 and 0.25M NaCl in the dispersions of pH 3.50 and 2.75, respectively. The increase in viscoelasticity was enhanced by the formation of 11S native fraction dimers.     

Miscibility of Quillaja Saponins with other Co‐surfactants under Different pH Values

The miscibility behavior of mixed surfactant systems and the influence of extrinsic parameters are crucial for their application as emulsifiers. Therefore, the objective of this study was to evaluate the miscibility behavior of mixed systems composed of commercial Quillaja saponin and a co‐surfactant, namely sodium caseinate, pea protein, rapeseed lecithin, or egg lecithin. These mixtures were evaluated macro‐ and microscopically at different concentration ratios (maximum concentration 5% w/v) at pH 3, 5, and 7 at 25 °C. The individual ingredients were also assessed for their charge properties and surface hydrophobicity. The results showed that Quillaja saponin–caseinate mixtures were miscible only at pH 7, and showed aggregation and precipitation at lower pH due to increasing electrostatic attraction forces. Rheological measurements showed that Quillaja saponin‐pea protein mixtures formed gelled structures at all tested pH values mainly via association of hydrophobic patches. Quillaja saponins mixed with rapeseed lecithin were miscible at all tested pH values due to electrostatic repulsion. Quillaja saponin–egg lecithin mixtures aggregated independent of pH and concentration ratio. The microscopic analysis revealed that the lower the pH and the higher the Quillaja saponin ratio, the denser were the formed Quillaja saponin–egg lecithin aggregates. The results are summarized in ternary phase diagrams that provide a useful tool in selecting a surfactant system for food applications.     

pH and ultrasound driven structure-function relationships of soy protein hydrolysate

The structural, thermodynamic and functional properties of soy protein hydrolysate (SPH) modified by treatment at different pH values (3, 5, and 9 and pH 7 as control) followed by ultrasound treatment (240 W, 30 min) were investigated. The treatment of SPH at alkaline pH combined with ultrasound treatment resulted in a reduction in the particle size and turbidity, enhancement in the surface negative charge and disulfide bond (SS) content, and exposure of more surface sulfhydryl (SH) groups, resulting in increased surface hydrophobicity and fluorescence intensity compared to those of the samples treated at pH 3–7. In addition, the alkaline-treated samples were more structurally stable than those treated at other pH values, having higher denaturation temperatures and enthalpies; moreover, these samples had higher solubility and emulsifying and foaming capacities. In addition, ultrasound-assisted pH treatment altered the secondary and tertiary structures of SPH by altering the covalent and non-covalent interactions, although there was no effect on the molecular weight distribution of proteins. In conclusion, ultrasound-assisted pH treatment is an effective method to improve physicochemical properties of SPH for applications in the food industry.     

Survival,growth characteristics and bioactive potential of Lactobacillus acidophilus in a soy‐based cream cheese

BACKGROUND: Soy‐based products have received much attention lately as dairy replacers and carriers for probiotics, without the cholesterol and lactose intolerance factors. We have previously developed a soy cream cheese product and would like to evaluate its suitability as a carrier for probiotic microorganisms. Soy cream cheese is commercially uncommon, while a probiotic soy cream cheese is yet to be available in the market. RESULTS: Five strains of probiotics were screened for their α‐galactosidase activity. Lactobacillus acidophilus FTCC 0291 showed the highest α‐galactosidase‐specific activity and was incorporated into soy cream cheese for a storage study of 20 days at 25 and 4 °C. L. acidophilus FTCC 0291 in soy cream cheese at both storage temperatures maintained a viability exceeding 10⁷ CFU g^?1 over storage. Oligosaccharide and reducing sugar analyses indicated that L. acidophilus FTCC 0291 was capable of utilizing the existing reducing sugars in soymilk and concurrently hydrolyzing the oligosaccharides into simpler sugars for growth. L. acidophilus FTCC 0291 also produced organic acids, leading to decreased pH. Under low pH and high organic acid concentration, the growth of total aerobes and anaerobes was significantly (P < 0.05) suppressed compared to the control. The hydrolysis of protein in soymilk produced essential growth factors such as peptides and amino acids that may have promoted the growth of L. acidophilus FTCC 0291 and the release of bioactive peptides with in vitro angiotensin I‐converting enzyme inhibitory activity. CONCLUSION: This study showed that soy cream cheese could be used as a carrier for probiotic bacteria, with potential antihypertensive property. Copyright © 2009 Society of Chemical Industry     

Influence of pH and CaCl2 on the stability of dilute whey protein stabilized emulsions

The influence of pH and CaCl₂ on the physical stability of dilute oil-in-water emulsions stabilized by whey protein isolate has been studied. The particle size, zeta potential and creaming stability of 0.05 wt% soy bean oil-in-water emulsions (d ≈ 0.53 μm) were measured with varying pH (3 to 7) and CaCl₂ concentration (0 to 20 μM). In the absence of CaCl₂ extensive droplet aggregation occurred around the isoelectric point of the whey proteins (4 < pH < 6) because of their low electrical charge, which led to creaming instability. Droplet aggregation occurred at higher pH when CaCl₂ was added to the emulsions. The minimum concentration of CaCl₂ required to promote aggregation increased as the pH increased. Aggregation was induced in the presence of CaCl₂ probably because of the reduction in electrostatic repulsion between droplets, caused by binding of counter ions to droplet surfaces and electrostatic screening effects.