Isolation of Tomato Seed Meal Proteins with Salt Solutions

Salt solutions were used in isolating tomato seed meal proteins. Na₂SO₃ and NaCl solutions at different concentrations, and pH were included in a central composite design to find optimum conditions of protein isolation. The highest total protein yield was achieved with water extraction (no salt present). Salt extraction at pH 7.5 produced isolates with protein content of 93.4% (NaCl 5% w/v) and 77.1% (Na₂SO₃ 0.5% w/v). Observed values were in good agreement with predicted values. Isolates extracted with different salt solutions ranged from less soluble but very resistant to heat and Ca²⁺, to very surface active with functional properties comparable to commercial soy isolates.     

Factors controlling the growth of Clostridium botulinum types A and B in pasteurized, cured meats III. The effect of potassium sorbate

The growth of Clostridium botulinum types A and B spores, at 10¹ or 10³ per container, was studied in a pork slurry system containing nitrite (40 μg/g), sodium chloride (2.5, 3.5, 4.5% w/v) sodium isoascorbate (550 μg/g) at varying pH levels, with or without potassium sorbate (0.26% w/v), without heating and after two heat treatments (80°C for 7 min, and 80°C for 7 min + 70°C for 1 hr) followed by storage at 15, 17.5, 20 or 35°C for up to 6 months. At a given spore inoculum, potassium sorbate significantly decreased toxin production, as did increasing NaCl, decreasing pH or decreasing storage temperature. Heat treatment did not significantly affect spoilage or toxin production overall, but interacted significantly with some factors. The effect of sorbate was greater at 3.5% NaCl than at 2.5%, at pH values below 6.0, and at low storage temperature.     

SOLUBILIZATION AND FUNCTIONAL PROPERTIES OF MOTH BEAN (VIGNA ACONITIFOLIA (Jacq.) Marechal AND HORSE GRAM (MACROTYLOMA UNIFLORUM (Lam.) Verdc. PROTEINS

Horse gram and moth bean seeds contained 23.6% and 21.9% protein (N x 6.25), respectively. Both the legumes are rich sources of iron. The iron contents in horse gram and moth beans were 11.0 and 9.6 mg/100 g, respectively. NaCl at 10% (w/v) and Na₂CO₃ at 0.5% (w/v) were found to be effective in extracting 89% and 80% of moth bean and horse gram proteins from defatted flour The minimum solubility of horse gram proteins from defatted flour was at pH 4.0 whereas proteins from moth bean exhibited minimum solubility at pH 4.5. The water and oil absorption, and foaming capacities in case of horse gram and moth bean flours were 2.0 g/g and 2.2 g/g, 23.0% and 2.0 g/g, 1.6 g/g, 27.6%, respectively.     

Optimization of Medium Composition for Cultivating Clostridium butyricum with Response Surface Methodology

ABSTRACT: Probiotic bacteria, such as some strains of Clostridium butyricum , have been frequently used as the active ingredient in functional foods. However, slow growth of the probiotic bacteria has been one of the big concerns for their potential commercial application. In the present study, a fractional factorial design was applied to investigate the main factors, namely, the concentrations of the glucose, tryptone, yeast extract, beef extract, cys-teine, (NH₄) ₂SO₄, NaCl, K₂HPO₄, and the medium initial pH that affected the growth of 1 probiotic strain, C. butyricum ZJUCB, currently preserved in our laboratory. Central composite experimental design and response surface methodology were adopted to derive a statistical model for optimizing the composition of the medium. The experimental results showed that the optimum medium for incubating the C. butyricum ZJUCB was composed of 2.44% (w/v) glucose, 2.08% yeast extract (w/v), 1% tryptone (w/v), 0.1% (NH₄)₂SO₄ (w/v), 0.1% NaHCO₃ (w/v), 0.02% MnSO₄. H₂O (w/v), 0.02% MgSO₄. 7H₂O (w/v), 0.002% CaCl₂ (w/v), and 2% agar (w/v) (if necessary) at pH 8.55. After incubation for 24 h in the optimum medium, the populations of the viable organisms could reach 10⁹ colony-forming units (CFU)/mL, which was 100 times higher than that incubated in the initial medium.     

Temperature-Sensitive Microcapsules Containing Lactoferrin and Their Action Against Carnobacterium viridans on Bologna

ABSTRACT:  Lactoferrin (LF) was encapsulated in 2 types of emulsion to protect it from contact with agents like divalent cations, which interfere with its antimicrobial activity. First, paste-like microcapsules were prepared as water-in-oil (W₁/O) emulsions from mixtures of 20% w/v LF in distilled water, 20% w/v LF in 3% w/v sodium lactate or in 20 mM sodium bicarbonate, which were emulsified with an oil mixture of 22% butter fat plus 78% corn oil and 0.1% polyglycerol polyricinoleate. Second, freeze-dried double emulsion (W₁/O/W₂), powdered microcapsules were produced following emulsification of paste-like microcapsules in an external aqueous phase (W₂) consisting of a denatured whey protein isolate (WPI) solution. The release of LF from the W₁/O microcapsules was dependent on temperature and NaCl concentration. LF was not released from the W₁/O emulsion at <5.5 °C. Its release was greater from W₁/O microcapsules when suspended in 5% aqueous NaCl than in water at ≥10 °C, whereas LF release from freeze-dried microcapsules was not controlled by temperature change. Paste-like microcapsules were incorporated in edible WPI packaging film to test the antimicrobial activity of LF against a meat spoilage organism Carnobacterium viridans . The film was applied to the surface of bologna after its inoculation with the organism and stored under vacuum at 4 or 10 °C for 28 d. The growth of C. viridans was delayed at both temperatures and microencapsulated LF had greater antimicrobial activity than when unencapsulated. The temperature-sensitive property of the W₁/O microcapsules was reduced when they were incorporated into a WPI film.     

EFFECT OF SEVERAL VARIABLES ON THE EXTRACTABILITY OF SUNFLOWER SEED PROTEINS

SUMMARY— The effect of several variables on the extraction of sunflower seed protein has been investigated. Solubility studies on the meal show that globulin is the main protein component. Albumin, nonprotein nitrogen and insoluble nitrogen are very low. Glutelin comprises about 17% of the total nitrogen. 15 min and a meal to solvent ratio of 1:10 (w/v) were found to extract a maximum amount of protein at pH 7.0. The optimum temperature of extraction is 45°C, although over a temperature range of 26-6°C the extraction remains essentially constant. More protein was extracted by 1.0 M NaCl and 0.75 M CaCl₂ at various pH's than by the higher or the lower concentrations of these salts. Results with several other salts show that concentration as well as pH is very important. Reducing agents do not appear to have any marked effect on the extractability of protein.     

Optimization of Medium Composition for Nisin Fermentation with Response Surface Methodology

ABSTRACT:  Nisin is an effective food biopreservative widely used in food industry. However, 1 problem of concern is limited production rate and final nisin concentration. A nisin-producing strain, L. lactis Lac2, a mutant strain with high yield of nisin, was obtained in our laboratory recently. In the present study, a fractional factorial design was applied to investigate the main factors that affect the yield of L. lactis Lac2. Central composite experimental design and response surface methodology were adopted to derive a statistical model for optimizing the composition of the medium. The results showed that the optimum medium for nisin production of L. lactis Lac2 was composed of 2.68% sucrose (w/v), 0.5% tryptone (w/v), 1% yeast extract (w/v), 0.3% Tween-80 (w/v), 0.02% MgSO₄·7H₂O (w/v), 0.81% NaCl (w/v), 1.91% K₂HPO₄ (w/v), 0.05% ascorbic acid (w/v), and 2% agar (w/v) (if necessary) at pH 6.5. When cultured in the optimum medium, the nisin yield is an average of 3381.81 IU/mL, which nearly doubled the yield when incubated in the initial medium. Also, the concentration of tryptone was decreased while that of the sucrose was increased when compared with CM broth, which means a reduction of the fermentation cost.     

ROLE OF pH IN SOLUBILITY AND CONFORMATIONAL CHANGES OF PACIFIC WHITING MUSCLE PROTEINS

This study was conducted to better understand biochemical changes of fish muscle proteins as affected by novel surimi process, acid- or alkali-aided solubilization. At 10 mM NaCl, between pH 5 and 10, the solubility of Pacific whiting muscle proteins was low but increased dramatically as the pH was shifted to either acidic or alkaline pH. At 600 mM NaCl, the isoelectric point was shifted to the acidic direction by about 2 pH units, resulting in aggregation of proteins at low pH, but improving the solubility of MHC (myosin heavy chain) between pH 6 and 10. ANS surface hydrophobicity (ANS-S_O) showed much greater values than PRODAN surface hydrophobicity (PRODAN-S_O) for samples treated at pH 2 - 4 perhaps due to an enhancement of the electrostatic interactions between the ANS probe and proteins. At very high pH, according to hydrophobicity results, proteins were partially refolded when the ionic strength increased. Under acidic conditions, SDS-PAGE demonstrated the degradation of MHC at 10 mM NaCl. The formation of MHC polymers was observed under alkaline treatment with a concomitant decrease of SH content.     

Effects of inulin/oligofructose on the thermal stability and acid-induced gelation of soy proteins

ABSTRACT:  Differential scanning calorimetry (DSC) and dynamic oscillatory shear testing were performed to study the influence of inulin (Raftiline^® HP-gel and Raftiline^® ST-gel) and oligofructose (Raftilose^® P95) on the thermal stability and gelation (using glucono-δ-lactone [GDL] as a coagulant) of soy protein isolate (SPI) dispersions. Addition of 10% (w/v) inulin/oligofructose or sucrose increased ( P < 0.05) the peak denaturation temperatures ( T_m ) of 7S and 11S soy proteins in SPI dispersion (5%[w/v], pH 7.0) by an average of 1.9 and 2.3 °C, respectively. GDL induced SPI thermal gelation, and the gel rheology was affected by both the pH decline and the specific temperature of heating. Addition of inulin/oligofructose (8%, w/v) improved the gelling properties of preheated SPI dispersion (8%, w/v) coagulated with GDL, showing 14.4 to 45.6% increase ( P < 0.05) in gel rigidity ( G ' value) at the end of heating (81 °C). Microstructural examination revealed a denser protein cross-linking structure and reduced pore sizes in SPI gels containing inulin/oligofructose. In general, inulin was more capable of improving SPI gelation than oligofructose, suggesting that the degree of fructose polymerization in the fructans was of thermal and rheological importance.     

Control of Listeria monocytogenes in ready-to-eat meats containing sodium levulinate, sodium lactate, or a combination of sodium lactate and sodium diacetate

ABSTRACT:  This study investigated the use of sodium levulinate to prevent outgrowth of Listeria monocytogenes in refrigerated ready-to-eat (RTE) meat products. Turkey breast roll and bologna were formulated to contain 1%, 2%, or 3% (w/w) sodium levulinate, 2% sodium lactate, a 2% combination of sodium lactate and sodium diacetate (1.875% sodium lactate and 0.125% sodium diacetate), or no antimicrobial (control). Samples of the RTE products were sliced, inoculated with 10² to 10³ CFU/cm² of a 5-strain cocktail of L. monocytogenes , vacuum packaged, and stored at refrigeration temperature for 0 to 12 wk. Counts reached 10⁸ CFU/cm² on control turkey roll product after 8 wk, and over 10⁷ CFU/cm² on control bologna after 12 wk. Addition of 2% or more sodium levulinate to turkey roll and 1% or more sodium levulinate to bologna completely prevented growth of L. monocytogenes during 12 wk of refrigerated storage. A consumer taste panel with pathogen-free samples found no differences in the overall liking among the preparations of turkey roll or among preparations of bologna. These results show that sodium levulinate is at least as effective at inhibiting outgrowth of L. monocytogenes in RTE meat products as the current industry standards of lactate or lactate and diacetate, and levulinate addition does not alter the overall liking of the RTE meat products.     

Synergistic enhancement in the co-gelation of salt-soluble pea proteins and whey proteins

This paper investigated the enhancement of thermal gelation properties when salt-soluble pea proteins were co-gelated with whey proteins in NaCl solutions, using different blend ratios, total protein concentrations, pH, and salt concentrations. Results showed that the thermal co-gelation of pea/whey proteins blended in ratio of 2:8 in NaCl solutions showed synergistic enhancement in storage modulus, gel hardness, paste viscosity and minimum gelation concentrations. The highest synergistic enhancement was observed at pH 6.0 as compared with pH 4.0 and 8.0, and at the lower total protein concentration of 10% as compared with 16% and 22% (w/v), as well as in lower NaCl concentrations of 0.5% and 1.0% as compared with 1.5%, 2.0%, 2.5%, and 3.0% (w/v). The least gelation concentrations were also lower in the different pea/whey protein blend ratios than in pure pea or whey proteins, when dissolved in 1.0% or 2.5% (w/v) NaCl aqueous solutions.     

Factors Determining Yield Stress and Overrun of Whey Protein Foams

ABSTRACT: Foams were formed by whipping whey protein solutions (15% w/v protein) containing NaCl, CaCl₂, lactose, or glycine. Foam overrun and yield stress were determined. Foams made from whey protein ingredients have greater overrun and yield stress if the concentration of β-lactoglobulin is high relative to a-lactalbumin. The presence of 0.4 M CaCl₂ in the foaming solution increases overrun and yield stress for β-lactoglobulin and a-lactalbumin. The high yield stress of β-lactoglobulin and a-lactalbumin foams made from solutions containing CaCl₂ suggests that CaCl₂ is altering rheological properties of the interfacial protein film and/or contributing to protein aggregation or network formation in the lamellae.     

RHEOLOGICAL PROPERTIES AND APPLICATIONS OF MESQUITE TREE (PROSOPIS JULIFLORA) GUM. 1. RHEOLOGICAL PROPERTIES OF AQUEOUS MESQUITE GUM SOLUTIONS

The viscosities of aqueous mesquite gum solutions were measured at gum concentrations extending to 16.7% (w/v). Very dilute solutions exhibited typical polyelectrolyte behavior with respect to the influence of gum concentration on the reduced viscosity in the absence and presence of electrolyte. Shear thickening was exhibited at concentrations of 1–16.67% (w/v) when the shear rate exceeded ∼100 s⁻¹, whereas shear thinning was exhibited at lower shear rates. Shear thickening was attributed to configurational changes in the gum molecules at high shear rates. Electrolytes (0.1N NaCl and 0.1N CaCl₂) reduced the viscosity of concentrated solutions at high shear rates to a larger extent than increasing the pH. Charge screening by electrolyte permits the gum molecules to assume a more compact configuration.     

Antimicrobial effect of electrolyzed oxidizing water against Escherichia coli O157:H7 and Listeria monocytogenes on fresh strawberries (Fragaria x ananassa)

ABSTRACT:  Antibacterial activity of electrolyzed oxidizing (EO) water prepared from 0.05% or 0.10% (w/v) sodium chloride (NaCl) solutions against indigenous bacteria associated with fresh strawberries ( Fragaria × ananassa ) was evaluated. The efficacy of EO water and sodium hypochlorite (NaOCl) solution in eliminating and controlling the growth of Listeria monocytogenes and Escherichia coli O157:H7 inoculated onto strawberries stored at 4 ± 1 °C up to 15 d was investigated at exposure time of 1, 5, or 10 min. Posttreatment neutralization of fruit surfaces was also determined. More than 2 log₁₀ CFU/g reductions of aerobic mesophiles were obtained in fruits washed for 10 or 15 min in EO water prepared from 0.10% (w/v) NaCl solution. Bactericidal activity of the disinfectants against L. monocytogenes and E. coli O157:H7 was not affected by posttreatment neutralization, and increasing exposure time did not significantly increase the antibacterial efficacy against both pathogens. While washing fruit surfaces with distilled water resulted in 1.90 and 1.27 log₁₀ CFU/mL of rinse fluid reduction of L. monocytogenes and E. coli O157:H7, respectively, ≥ 2.60 log₁₀ CFU/mL of rinse fluid reduction of L. monocytogenes and up to 2.35 and 3.12 log₁₀ CFU/mL of rinse fluid reduction of E. coli O157:H7 were observed on fruit surfaces washed with EO water and NaOCl solution, respectively. Listeria monocytogenes and E. coli O157:H7 populations decreased over storage regardless of prior treatment. However, EO water and aqueous NaOCl did not show higher antimicrobial potential than water treatment during refrigeration storage.     

Low Temperature Growth of Type E Clostridium botulinum Spores. 1. Effects of Sodium Chloride, Sodium Nitrite and pH

SUMMARY— The effects of pH and the addition of sodium chloride (NaCl) or sodium nitrite (NaNO₂) to trypticase-peptone-glucose (TPGI and trypticase-peptone-sucrose-yeast extract (TPSY) media upon spore outgrowth were investigated using seven Type E Clostridium botulinum strains. An inoculum of 1.0 × 10⁵ spores/ml was used and the pH was adjusted with hydrochloric acid to cover the range of 5.2 to 6.6. To define salt tolerance, NaCl was added to the media at intervals of 0.5% in the range of 2.0 to 5.0% and at 0.1% intervals in the 4.5 to 5.0% range. The effect of NaNO₂ was investigated with the addition of 100 and 200 ppm NaNO₂ to the media. Samples were incubated at 30, 15.6, 10, 7.2, 5.0 and 3.4°C. Outgrowth of all strains tested was inhibited at pH 5.2 at 15.6°C. Inhibition occurred at higher pH at lower temperatures. None of the strains showed outgrowth with 4.87% NaCl in the media at any of the incubation temperatures used. Addition of 100 and 200 ppm NaNO₂ to the media inhibited the outgrowth of the Minneapolis, 517, 26080 and A6247 strains but not the Kalamazoo and Seattle Forks strains.     

Effect of hydrogen peroxide on quality of fresh-cut tomato

ABSTRACT:  The effect of hydrogen peroxide (H₂O₂; 0, 0.1, 0.2, and 0.4 M) on selected nutritional quality of fresh-cut tomato was investigated. Microbial population of tomato slices stored at 10 °C and treated with H₂O₂ was lower than the control by 1-(0.2 and 0.4 M) and 5-log (0.4 M), 3 and 7 d after processing, respectively. Dipping fresh-cut tomato into H₂O₂ resulted in reduced phenolic and antioxidant levels after 7 d in storage by at least 5% and 20%, respectively, and produced an initial decline in vitamin C and lycopene. Change in color values in the H₂O₂ treatments were associated with reduced carotenoid content. Our results confirmed antimicrobial benefits of H₂O₂ but revealed a compromise in antioxidant and carotenoid contents of fresh-cut tomatoes.     

Osmotic dehydration kinetics of carrot cubes in sodium chloride solution

Osmotic dehydration kinetics of carrot cubes in sodium chloride solution having concentrations 5%, 10% and 15% (w/v), solution temperature 35, 45 and 55 °C, sample to solution ratio (STSR) 1:4, 1:5 and 1:6 were studied up to 240 min duration. During the experimentation, effect of solution temperature and process duration was significant and that of solution concentration and STSR were non-significant on water loss. Among the different models applied (Penetration model, Magee Model, and Azuara model), Azuara model best fitted to the experimental data for water loss and solute gain during osmotic dehydration. Effective diffusivities of water and solute were calculated by using the analytical solution of Fick's unsteady state law of diffusion by iterative technique with a computer program. For the above conditions, the effective diffusivity of water was found to be in the range between 2.6323 × 10⁻⁹ and 6.2397 × 10⁻⁹ m²/s and that of solute between 3.1522 × 10⁻⁹ and 4.6400 × 10⁻⁹ m²/s.     

Textural Properties of Cold-set Gels Induced from Heat-denatured Whey Protein Isolates

A 9% whey protein (WP) isolate solution at pH 7.0 was heat-denatured at 80°C for 30 min. Size-exclusion HPLC showed that native WP formed soluble aggregates after heat-treatment. Additions of CaCl2 (10–40 mM), NaCl (50–400 mM) or glucono-delta-lactone (GDL, 0.4–2.0%, w/v) or hydrolysis by a protease from Bacillus licheniformis caused gelation of the denatured solution at 45°C. Textural parameters, hardness, adhesiveness, and cohesiveness of the gels so formed changed markedly with concentration of added salts or pH by added GDL. Maximum gel hardness occurred at 200 mM NaCl or pH 4.7. Increasing CaCl2 concentration continuously increased gel hardness. Generally, GDL-induced gels were harder than salt-induced gels, and much harder than the protease-induced gel.     

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.     

DETERMINATION OF CARBOXYMETHYLCELLULOSE IN FOOD PRODUCTS

SUMMARY –A method was developed to determine sodium carboxymethylcellulose (CMC) in food products containing three or more hydrocolloids after prior removal of interfering substances. Papain was used to digest the proteins; calcium chloride was added to precipitate algin and pectic acid and sulfated hydrocolloids were then precipitated by cetylpyridinium chloride (CPC) in the presence of 0.5M NaCl. Celite 535 or Hyflo Super Cel was added, the mixture filtered over Reeve angel No. 202 paper and the residue washed with 0.01% CPC-0.01M NaCl. The filtrate and washings were collected and diluted with distilled water to attain a final concentration of 0.2M NaCl at which concentration the CMC was precipitated selectively by CPC. The mixture was filtered over a Celite 535 or Hyflo Super Cel column and the residue washed with 0.5M Na₂SO₄ and then with 0.01% CPC-0.01M NaCl until the washings were negative to the phenol-H₂SO₄ reagent. Finally, the residue on the column was washed with hot 30% H₂SO₄ and the hydrolyzed CMC in the eluate determined by the 2,7-naphthalenediol test. Based on the amount added to mixtures, recoveries of 75–86% were obtained from milk and other highly complex and proteinaceous products, with a standard deviation of ± 0.58 mg, when 10 mg of CMC were added. The determination is critically dependent upon the degree of substitution (DS) of the CMC. As a consequence, the method cannot be applied with absolute certainty to unknown samples.