22 research outputs found

    Rheological Behavior of Food Emulsions Mixed with Saliva: Effect of Oil Content, Salivary Protein Content, and Saliva Type

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    In this paper, we studied the effect of saliva on the rheological properties of ß-lactoglobulin- and lysozyme-stabilized emulsions, prepared at pH¿=¿6.7 in relation to variation of emulsions- and saliva-related parameters. The effect of oil¿volume fraction (2.5% w/w to 10% w/w), salivary protein concentration (0.1 to 0.8 mg ml¿1), and the use of both stimulated and unstimulated saliva was investigated. Viscosity and storage modulus were measured before (¿ emul and G¿emul, respectively) and after addition of saliva (¿ mix and G¿mix). To better estimate the changes due to saliva-induced flocculation of the emulsions, the ratios ¿ mix/¿ emul, G¿mix/G¿emul were calculated. In addition, tan ¿ (=the ratio of the loss and storage moduli) was investigated to evaluate the viscoelastic behavior of the emulsion/saliva mixtures. Increasing the oil¿volume fraction and salivary protein concentration resulted in an increase in ¿ mix/¿ emul and G¿mix/G¿emul, while a decrease in tan ¿ of the emulsion/saliva mixtures is occurring. When compared with unstimulated saliva, mixing ß-lactoglobulin-stabilized emulsions with stimulated saliva led to a reduction in ¿ mix/¿ emul and G¿mix/G¿emul, and an augment of tan ¿ at all measured deformations. In case of lysozyme-stabilized emulsions, the use of stimulated saliva increased G¿mix/G¿emul for ¿

    Recovery of proteins from dairy effluens by means of ultrafiltration

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    The purpose of this work was to investigate the potential of membrane ultrafiltration for the recovery of proteins from dairy effluents. Employing a 10 kDa tubular ceramic membrane in total recycle and batch modes, the effects of temperature, feed flow rate, and protein concentration in feed were evaluated by measuring permeate fiux-transmembrane pressure and permeate flux-time profiles, and total protein rejection coefficients. Results from these experiments have been used to analyze the technical viability of the recovery of dairy proteins by ultrafiltration. Last stage of ihe work consisted of a preliminary analysis of different phenomena limiting flux in this system. For this reason, previous experimental data were fitted with mathematical models proposed in bibliography by means of a computer tool of our own programming. Furthermore, a thermo-chemical washing method was successfully applied to clean tubular ceramic membranes previously fouled with dairy solutes

    Milk fouling in heat exchangers

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    The mechanisms of fouling of heat exchangers by milk were studied. Two major fouling mechanisms were indentified during the heat treatment of milk: (i) the formation and the subsequent deposition of activated serum protein molecules as a result of the heat denaturation; (ii) the precipitation of calcium phosphate as a result of the decreased solubility of this salt upon heating. Both foulants are formed in the bulk of the solution and are transported to the surface, where they can be deposited.If the stability of milk is lowered, e.g. by lowering the pH, coagulation of casein micelles can cause extreme fouling. A further cause of fouling is air bubbles, which arise in the milk on heating and stick to the stainless steel wall; they appear to act as nuclei for the formation of protein deposit.Fouling in heat exchangers can be reduced by controlling the formation of activated serum protein molecules and by preventing the precipitation of calcium phosphate. Various ways to achieve this are given.Once formed, milk deposits can readily be removed by alkaline cleaning followed by acid cleaning under the right conditions

    Total serum IgE quantification by microfluidic ELISA using magnetic beads

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    The present work reports on the quantification of total IgE in human serum using a microanalytical device whose fluidics is driven by gravity and capillary forces only. Thanks to the eight parallel microchannels in each microchip, calibration and sample analysis are performed simultaneously. A mixture of magnetic bead/analyte/second antibody is incubated off-line and then percolated through the channels where magnetic beads are trapped, enabling the separation of the solid phase from the excess reagents. The entire assay is performed in less than 1h, and thanks to the miniaturized format, only a small volume of serum is required. Non-specific adsorption was first investigated and a blocking agent compatible with this allergy-based test was chosen. Then, the assay was optimized by determining the best magnetic bead and labelled antibody concentrations. After achievement of a calibration curve with a reference material, the protocol was applied to total IgE quantification of a patient serum sample that showed results in good accordance with those obtained by ImmunoCap® and Immunoaffinity capillary electrophoresis measurements. A detection limit of 17.5ngml−1 was achieved and good reproducibility (RSD < 10%) inter- and intra-chip was observed. Figure Off-line incubation of the patient sample with anti-IgE grafted magnetic beads and ALP-labelled anti-IgE is carried out in an Eppendorff. Detection is then performed with the GRAVI®-Cell device from DiagnoSwiss, where fluidics is driven by gravity and capillary forces onl

    Total serum IgE quantification by microfluidic ELISA using magnetic beads

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    The present work reports on the quantification of total IgE in human serum using a microanalytical device whose fluidics is driven by gravity and capillary forces only. Thanks to the eight parallel microchannels in each microchip, calibration and sample analysis are performed simultaneously. A mixture of magnetic bead/analyte/second antibody is incubated off-line and then percolated through the channels where magnetic beads are trapped, enabling the separation of the solid phase from the excess reagents. The entire assay is performed in less than 1 h, and thanks to the miniaturized format, only a small volume of serum is required. Non-specific adsorption was first investigated and a blocking agent compatible with this allergy-based test was chosen. Then, the assay was optimized by determining the best magnetic bead and labelled antibody concentrations. After achievement of a calibration curve with a reference material, the protocol was applied to total IgE quantification of a patient serum sample that showed results in good accordance with those obtained by ImmunoCapA (R) and Immunoaffinity capillary electrophoresis measurements. A detection limit of 17.5 ng ml(-1) was achieved and good reproducibility (RSD < 10%) inter- and intra-chip was observed

    The rheology of gel formed during the California Mastitis Test

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    One of the most costly diseases in the dairy industry is mastitis, which is an inflammation of the mammary gland. Mastitis influences the quality of milk and therefore reduces financial returns to both the farmer and the processor. Early detection of mastitis typically reduces treatment cost and a significant amount of research has been done in this field. Currently, the three major methods for mastitis detection are: •The Foss Analysis, which physically counts each cell and is performed off-site. •The Whiteside Test, which is based on a direct relationship between the number of the blood cells and the intensity of a gel formed between NaOH and cells. It was developed for on-site mastitis detection, but is no longer used routinely. •The California Mastitis Test (CMT), which can be done on-site, but is only a quantitative indication of the severity of the infection. The California Mastitis Test has previously been adapted to determine the somatic cell count (SCC) in infected milk by correlating viscosity to cell count. Although highly successful, some uncertainty exists regarding the rheology of the gel formed during the test as well as factors that may influence the accuracy of the test. In this thesis, studies were undertaken on the rheology of the gel formed during the California Mastitis Test in order to develop an understanding of the mechanism of gel formation and how various factors influence the rheology of the gel. Basic biochemistry and physico-chemistry of the gel has been reviewed and it was found that the CMT gel is a DNA/histone/surfactant complex, which forms when SDS is introduced into infected milk with elevated somatic cell counts. Based on literature and some initial experimentation it was found that the gel is a time- and shear- dependent, non-Newtonian fluid. Since the reliability of the CMT hinges on the correlation between viscosity and SCC, this study investigated specific factors that may influence gelation, these were: •rheology •testing conditions, such as time delay prior to viscosity testing, shear rate and temperature •surfactant type and concentration •milk composition, including fat content, somatic cell count and protein content. It was found that when using capillary viscometry a linear relationship exists between the relative viscosity of the gel and the SCC. The surfactant concentration determines the slope of this linear relationship and it was found that at least 3% SDS is necessary for accurate results. Using more than 3% SDS resulted in more scatter in the data. It was also found that a linear relationship exists between the maximum apparent viscosity and SCC. Either capillary or Brookfield viscometry can be used, however, Brookfield viscometry was found to be more sensitive at the lower SCC range. It was found that the combination of surfactant concentration and SCC influenced the rheology of the gel. The lower the SCC the more SDS was required for gel formation. It was found that when using 1% SDS the critical SCC was 79 k cell/ml, while using 3% SDS this was lowered to 59 k cell/ml. It was found that above the critical SCC the gel is a non-Newtonian rheopectic fluid. Dependent on shear rate, the gel shows rheodestructive behaviour. With a delay time, the peak viscosity of the gel formed faster with longer delay times. However, more than 30 seconds delay had no additional influence on gel formation. It was found that the shear rate or spindle speed influences both the time to reach the peak viscosity as well as the magnitude of this maximum. Higher shear rates shortened the time to reach the maximum apparent viscosity as well as the maximum viscosity. This is likely due to physical breakdown of the gel which is accelerated due to increased shear. Different surfactants have different effects on raw milk. Both acetic acid and Triton- 114 were found to be ineffective as CMT reagents. Acetic acid only denatures proteins and the increased viscosity is due to the precipitation of casein. Triton-114 cannot lyse nuclei walls and therefore gel formation was prohibited due to no DNA/histone complexes being released. Mixing SDS with Triton-114 was found to be less effective than SDS alone either due to the nucleus not being lysed, or because of interaction effects between SDS and Triton-114, reducing the available SDS for gelation. Lastly it was concluded that protein and fat content only contributes to the viscosity of milk by changing the solids content of milk and neither of these affects gelation during the CMT. Also, temperature only has a small influence on the relative viscosity and this influence could be neglected if the CMT is done around room temperature

    The Effects Of Sucrose On The Mechanical Properties Of Acid Milk Proteins-κ-carrageenan Gels

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    Mechanical properties have been widely correlated with textural characteristics to determine the interactions during the process formation of dairy gel. These interactions are strongly affected by process conditions and system composition. In the present study, the rheological of acid-induced protein dairy gels with (2(7-3)) and without (2(6-2)) sucrose and subjected to small and large deformations were studied using an experimental design. The independent variables were the sodium caseinate, whey protein concentrate (WPC), carrageenan and sucrose concentrations as well as stirring speed and heat treatment time and temperature. Mechanical deformation tests were performed at 0.1, 1, 5, and 9 mm/s up to 80% of initial height. A heavy dependence of rupture stress on increasing crosshead speed and the formation of harder gels with the addition of sucrose were observed. Moreover the elastic and viscous moduli, obtained by fitting the Maxwell model to stress relaxation data, increased with increasing addition of sucrose. These results can be explained by preferential hydration of the casein with sucrose, causing an induction of casein-polysaccharide and casein-casein interactions.2315565Antipova, A.S., Semenova, M.G., Belyakova, L.E., Effect of sucrose on the thermodynamic properties of ovalbumin and sodium caseinate in bulk solution and at air-water interface (1999) Colloids and Surfaces B - Biointerfaces, 12, p. 261Antipova, A.S., Semenova, M.G., Effect of sucrose on the thermodynamic incompatibility of different biopolymers (1995) Carbohydrate Polymers, 28, p. 359Arakawa, T., Timasheff, S.N., Stabilization of protein-structure by sugars (1982) Biochemistry, 21, p. 6536Belyakova, L.E., Antipova, A.S., Semenova, M.G., Dickinson, E., Merino, L.M., Tsapkina, E.N., Effect of sucrose on molecular and interaction parameters of sodium caseinate in aqueous solution: Relationship to protein gelation (2003) Colloids and Surfaces B - Biointerfaces, 31, p. 31Bertola, N.C., Bevilacqua, A.E., Zaritzky, N.E., Changes in rheological and viscoelastic properties and protein breakdown during the ripening of "Port salut argentino" cheese (1991) International Journal of Food Science and Technology, 26, p. 467Braga, A.L.M., (2002) Characterization of Macromolecular Interactions in Acidified Caseinate-Xanthan-Sucrose Gels: Rheological and Thermal Analysis., , Master' Thesis, School of Food Engineering, State University of Campinas (In Portuguese)Capron, I., Nicolai, T., Durand, D., Heat induced aggregation and gelation of β-lactoglobulin in the presence of κ-carrageenan (1999) Food Hydrocolloids, 13, p. 1Dickinson, E., Merino, L.M., Effect of sugars on the rheological properties of acid caseinate-stabilized emulsion gels (2002) Food Hydrocolloids, 16, p. 321Farrell, H.M., Pessen, H., Brown, E.M., Kumosinski, T.F., Structural insights into the bovine casein micelle-small-angle x-ray-scattering studies and correlations with spectroscopy (1990) Journal of Dairy Science, 73, p. 3592Fly, J.A., Clarke, P.T., Du Parquet, H., Toyne, S., Augustin, M.A., Use of glucono-delta-lactone in manufacture of yogurt (1997) The Australian Journal of Dairy Technology, 52, p. 20Hemar, Y., Hall, C.E., Munro, P.A., Singh, H., Small and large deformation rheology and microstructure of κ-carrageenan gels containing commercial milk protein products (2002) International Dairy Journal, 12, p. 371Ju, Z.Y., Kilara, A., Textural properties of cold-set gels induced from heat-denatured whey protein isolates (1998) Journal of Food Science, 63, p. 288Koh, M.W.W., Merino, L.M., Dickinson, E., Rheology of acid-induced sodium caseinate gels containing added gelatin (2002) Food Hydrocolloids, 16, p. 619Kulmyrzaev, A., Bryant, C., McClements, D.J., Influence of sucrose on thermal denaturation, gelation, and emulsion stabilization of whey proteins (2000) Journal of Agriculture and Food Chemistry, 48, p. 1593Lucey, J.A., Singh, H., Formation and physical properties of acid milk gels: A review (1998) Food Research International, 30, p. 529Mleko, S., Li-Chan, E.C.Y., Pikus, S., Interactions of κ-carrageenan with whey proteins in gels formed at different pH (1997) Food Research International, 30, p. 427Mleko, S., Rheological properties of milk and whey protein desserts (1997) Milchwissenschaft, 52, p. 262Mora-Gutierrez, A., Farrell, H.M., Sugar-casein interaction in deuterated solutions of bovine and caprine casein as determined by oxygen-17 and carbon-13 nuclear magnetic resonance: A case of preferential interactions (2000) Journal of Agriculture and Food Chemistry, 48, p. 3245Mora-Gutierrez, A., Kumosinski, T.F., Farrell Jr., H.M., Oxygen-17 nuclear magnetic resonance studies of bovine and caprine hydration and activity in deuterated sugar solutions (1997) Journal of Agriculture and Food Chemistry, 45, p. 4545Mulvihill, D.M., Kinsella, J.E., Gelation of ß-lactoglobulin. effects of sodium chloride and calcium chloride on the rheological and structural properties of gels (1988) Journal of Food Science, 53, p. 231Nakamura, K., Shinoda, E., Tokita, M., The influence of compression velocity on strength and structure for gellan gels (2001) Food Hydrocolloids, 15, p. 247Oakenfull, D., Miyoshi, E., Nishinari, K., Scott, A., Rheological and thermal properties of milk gels formed with K-carrageenan. I. sodium caseinate (1999) Food Hydrocolloids, 13, p. 525Ribeiro, K.O., Rodrigues, M.I., Sabadini, E., Cunha, R.L., Mechanical properties of acid sodium caseinate - κ-carrageenan gels: Effect of co-solute addition (2004) Food Hydrocolloids, 18, p. 71Roefs, S.P.F.M., Degrootmostert, A.E.A., Van Vliet, T., Structure of acid casein gels. 1. formation and model of gel network (1990) Colloids and Surfaces A, 50, p. 141Schkoda, P., Hechler, A., Kessler, H.G., Effect of minerals and pH on rheological properties and syneresis of milk-based acid gels (1999) International Dairy Journal, 9, p. 269Schorsch, C., Jones, M.G., Norton, I.T., Thermodynamic incompatibility and microstructure of milk protein/ locust bean gum/sucrose systems (1999) Food Hydrocolloids, 13, p. 89Serpelloni, M., Lefevre, P., Dusautois, C., Glucono-delta-lactone in milk ripening (1990) Dairy Industries International, 55, p. 35Spiegel, T., Whey protein aggregation under shear conditions - Effects of lactose and heating temperature on aggregate size and structure (1999) International Journal Food Science and Technology, 34, p. 523Steffe, J.F., (1996) Rheological Methods in Food Process Engineering, pp. 1-93. , Freeman Press, East LansingThybo, A.K., Nielsen, M., Martens, M., Influence of uniaxial compression rate on rheological parameters and sensory texture prediction of cooked potatoes (2000) Journal of Textures Studies, 31, p. 25Tziboula, A., Home, D.S., Influence of milk proteins on kappa-carrageenan gelation (1999) International Dairy Journal, 9, p. 359Verheul, M., Roefs, S.P.F.M., Structure of whey protein gels, studied by permeability, scanning electron microscopy and rheology (1998) Food Hydrocolloids, 12, p. 17Walkenström, P., Windhab, E., Hermansson, A.M., Shear-induced structuring of particulate whey protein gels (1998) Food Hydrocolloids, 12, p. 45
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