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Rémi Saurel - One of the best experts on this subject based on the ideXlab platform.
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Interactions in casein micelle - Pea Protein system (Part II): mixture acid gelation with glucono-δ-lactone
Food Hydrocolloids, 2017Co-Authors: Jean-luc Mession, Sébastien Roustel, Rémi SaurelAbstract:Abstract In our preceding study (Part I), the thermal denaturation and aggregation of enriched Pea Protein fractions, namely vicilin/convicilin 7S (Vic) and legumin 11S (Leg), were investigated in the absence or in presence of casein micelles (CM) at pH ≈ 7.1. The present report (Part II) focuses on the glucono-δ-lactone (GDL) acid-induced gelation of either co-heated Proteins in admixture (namely route 1) or thermally-aggregated Pea Proteins mixed with unheated CM (route 2), while applying a Pea Protein (either non fractionated PP or Vic or Leg) - to - CM weight ratio of 1: 1 and total Protein concentration of 3.6 wt%. The Pea Protein thermal aggregates obtained by route 1 were of lower size and less soluble than those yielded in isolation. For route 1, gelation of the heated CM – Vic mixture was triggered at a higher pH value and led to higher final storage modulus G′ than corresponding Protein samples in isolation. In contrast, the presence of large and sedimentable aggregates in the case of the CM – PP and CM – Leg mixtures impaired gelation. Concerning route 2, either the PP or Vic aggregates mixed with unheated CM resulted in rapid gelation and higher final G’ values than those measured for their single-Protein sample counterparts. Viscoelastic properties of the mixed gel depended on the Pea Protein fraction used, thermal aggregation route, extent of physical interactions between Pea Proteins during acidification and further involvement of CM. Hence, route 2 would be more reliable than route 1 to produce a “mixed” dairy-like gelled product containing Pea Proteins with improved texture properties.
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Utilisation of pectin coating to enhance spray-dry stability of Pea Protein-stabilised oil-in-water emulsions
Food Chemistry, 2010Co-Authors: Adem Gharsallaoui, Eliane Cases, Odile Chambin, Rémi Saurel, Andrée Voilley, Philippe CayotAbstract:In this study, development of Pea (Pisum sativum) Protein stabilised dry and reconstituted emulsions is presented. Dry emulsions were prepared by spray-drying liquid emulsions in a laboratory spray-dryer. The effect of drying on the physical stability of oil-in-water emulsions containing Pea Protein-coated and Pea Protein/pectin-coated oil droplets has been studied. Oil-in-water emulsions (5 wt.% Miglyol 812 N, 0.25 wt.% Pea Protein, 11% maltodextrin, pH 2.4) were prepared that contained 0 (primary emulsion) or 0.2 wt.% pectin (secondary emulsion). The emulsions were then subjected to spray-drying and reconstitution (pH 2.4). The stability of the emulsions to dry processing was then analysed using oil droplet size, microstructure, Zeta potential, and creaming measurements. Obtained results showed that the secondary emulsions had better stability to droplet aggregation after drying than primary emulsions. To interpret these results, we propound that pectin, an anionic polysaccharide, formed a less charged protective layer around the Protein interfacial film surrounding the oil droplets that improved their stability to spray-drying mainly by increasing steric effects.
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Effect of high methoxyl pectin on Pea Protein in aqueous solution and at oil/water interface
Carbohydrate Polymers, 2010Co-Authors: Adem Gharsallaoui, Eliane Cases, Odile Chambin, Kosuke Yamauchi, Rémi SaurelAbstract:The effect of the addition of high methoxyl pectin on the stability of Pea Protein isolate emulsions was investigated. Except for low pectin concentrations at acidic pHs where bridging flocculation occurred the addition of pectin improved emulsion stability to pH changes and depletion flocculation induced by maltodextrin addition. The mechanism of pectin induced stability was probed by measuring Protein-pectin complex formation in solution, zeta potential of the emulsions droplets and the change in surface viscoelasticity on pectin addition. The phase diagrams of pectin-Pea Protein isolate in solution and pectin-Pea Protein-stabilized emulsions were established based on the obtained experimental results. These diagrams showed that under acidic conditions and at low pectin concentrations, electrostatic bridging phenomena leads to the formation of high size pectin-Protein complexes causing an increase in turbidity in solution and oil droplet flocculation in emulsions. It was concluded that the pectin induced stability could be mainly assigned to steric repulsion and oil-water interfacial membrane rigidity improvement after pectin adsorption. In fact, the emulsions formed after pectin adsorption could consist of oil droplets surrounded by multilayer interfacial coatings, which are comprised of an inner interfacial Protein film and an outer pectin layer.
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effect of high methoxyl pectin on Pea Protein in aqueous solution and at oil water interface
Carbohydrate Polymers, 2010Co-Authors: Adem Gharsallaoui, Eliane Cases, Odile Chambin, Kosuke Yamauchi, Rémi SaurelAbstract:Abstract The effect of the addition of high methoxyl pectin on the stability of Pea Protein isolate emulsions was investigated. Except for low pectin concentrations at acidic pHs where bridging flocculation occurred the addition of pectin improved emulsion stability to pH changes and depletion flocculation induced by maltodextrin addition. The mechanism of pectin induced stability was probed by measuring Protein–pectin complex formation in solution, zeta potential of the emulsions droplets and the change in surface viscoelasticity on pectin addition. The phase diagrams of pectin–Pea Protein isolate in solution and pectin–Pea Protein-stabilized emulsions were established based on the obtained experimental results. These diagrams showed that under acidic conditions and at low pectin concentrations, electrostatic bridging phenomena leads to the formation of high size pectin–Protein complexes causing an increase in turbidity in solution and oil droplet flocculation in emulsions. It was concluded that the pectin induced stability could be mainly assigned to steric repulsion and oil–water interfacial membrane rigidity improvement after pectin adsorption. In fact, the emulsions formed after pectin adsorption could consist of oil droplets surrounded by multilayer interfacial coatings, which are comprised of an inner interfacial Protein film and an outer pectin layer.
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Interfacial and Emulsifying Characteristics of Acid-treated Pea Protein
Food Biophysics, 2009Co-Authors: Adem Gharsallaoui, Eliane Cases, Odile Chambin, Rémi SaurelAbstract:This work presents equilibrium and dynamic aspects for the adsorption at the oil–water interface of Pea ( Pisum sativum L.) Protein isolate (PPI). Dynamic interfacial tension, γ , and surface viscoelasticity modulus, ε , were determined using pendant-drop method. Adsorption kinetics studies revealed that Pea Proteins adsorb faster at pH 7.0 than at acidic pH (pH 2.4). On the other hand, the measured ε is lower at pH 7.0. This is probably due to fast adsorption, leading to the formation of inhomogeneous film structures. In fact, compared with pHs above the isoelectric point (p I ~ 4.3), acidic conditions slow down the adsorption, but the modulus is increased. Pea-Protein-stabilized emulsions are more stable to creaming at acidic pH and their particle-size distributions are more homogeneous in these conditions. Effect of pH on interfacial properties and on properties of oil-in-water emulsions stabilized by PPI was interpreted in terms of Pea Protein solubility, globulin dissociation, and oil-droplet surface electrostatic charge. We propose that at acidic conditions, adsorbed dissociated globulins form stronger and denser viscoelastic networks when adsorbed at oil–water interface. Consequently, the pH-dependence of Pea-globulin-stabilized emulsions properties could be of great interest to tune barrier properties of oil/water interfacial membranes for several applications such as encapsulation and controlled release of lipophilic bioactive components within the food, medical, and pharmaceutical industries.
Adem Gharsallaoui - One of the best experts on this subject based on the ideXlab platform.
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Utilisation of pectin coating to enhance spray-dry stability of Pea Protein-stabilised oil-in-water emulsions
Food Chemistry, 2010Co-Authors: Adem Gharsallaoui, Eliane Cases, Odile Chambin, Rémi Saurel, Andrée Voilley, Philippe CayotAbstract:In this study, development of Pea (Pisum sativum) Protein stabilised dry and reconstituted emulsions is presented. Dry emulsions were prepared by spray-drying liquid emulsions in a laboratory spray-dryer. The effect of drying on the physical stability of oil-in-water emulsions containing Pea Protein-coated and Pea Protein/pectin-coated oil droplets has been studied. Oil-in-water emulsions (5 wt.% Miglyol 812 N, 0.25 wt.% Pea Protein, 11% maltodextrin, pH 2.4) were prepared that contained 0 (primary emulsion) or 0.2 wt.% pectin (secondary emulsion). The emulsions were then subjected to spray-drying and reconstitution (pH 2.4). The stability of the emulsions to dry processing was then analysed using oil droplet size, microstructure, Zeta potential, and creaming measurements. Obtained results showed that the secondary emulsions had better stability to droplet aggregation after drying than primary emulsions. To interpret these results, we propound that pectin, an anionic polysaccharide, formed a less charged protective layer around the Protein interfacial film surrounding the oil droplets that improved their stability to spray-drying mainly by increasing steric effects.
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Effect of high methoxyl pectin on Pea Protein in aqueous solution and at oil/water interface
Carbohydrate Polymers, 2010Co-Authors: Adem Gharsallaoui, Eliane Cases, Odile Chambin, Kosuke Yamauchi, Rémi SaurelAbstract:The effect of the addition of high methoxyl pectin on the stability of Pea Protein isolate emulsions was investigated. Except for low pectin concentrations at acidic pHs where bridging flocculation occurred the addition of pectin improved emulsion stability to pH changes and depletion flocculation induced by maltodextrin addition. The mechanism of pectin induced stability was probed by measuring Protein-pectin complex formation in solution, zeta potential of the emulsions droplets and the change in surface viscoelasticity on pectin addition. The phase diagrams of pectin-Pea Protein isolate in solution and pectin-Pea Protein-stabilized emulsions were established based on the obtained experimental results. These diagrams showed that under acidic conditions and at low pectin concentrations, electrostatic bridging phenomena leads to the formation of high size pectin-Protein complexes causing an increase in turbidity in solution and oil droplet flocculation in emulsions. It was concluded that the pectin induced stability could be mainly assigned to steric repulsion and oil-water interfacial membrane rigidity improvement after pectin adsorption. In fact, the emulsions formed after pectin adsorption could consist of oil droplets surrounded by multilayer interfacial coatings, which are comprised of an inner interfacial Protein film and an outer pectin layer.
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effect of high methoxyl pectin on Pea Protein in aqueous solution and at oil water interface
Carbohydrate Polymers, 2010Co-Authors: Adem Gharsallaoui, Eliane Cases, Odile Chambin, Kosuke Yamauchi, Rémi SaurelAbstract:Abstract The effect of the addition of high methoxyl pectin on the stability of Pea Protein isolate emulsions was investigated. Except for low pectin concentrations at acidic pHs where bridging flocculation occurred the addition of pectin improved emulsion stability to pH changes and depletion flocculation induced by maltodextrin addition. The mechanism of pectin induced stability was probed by measuring Protein–pectin complex formation in solution, zeta potential of the emulsions droplets and the change in surface viscoelasticity on pectin addition. The phase diagrams of pectin–Pea Protein isolate in solution and pectin–Pea Protein-stabilized emulsions were established based on the obtained experimental results. These diagrams showed that under acidic conditions and at low pectin concentrations, electrostatic bridging phenomena leads to the formation of high size pectin–Protein complexes causing an increase in turbidity in solution and oil droplet flocculation in emulsions. It was concluded that the pectin induced stability could be mainly assigned to steric repulsion and oil–water interfacial membrane rigidity improvement after pectin adsorption. In fact, the emulsions formed after pectin adsorption could consist of oil droplets surrounded by multilayer interfacial coatings, which are comprised of an inner interfacial Protein film and an outer pectin layer.
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Interfacial and Emulsifying Characteristics of Acid-treated Pea Protein
Food Biophysics, 2009Co-Authors: Adem Gharsallaoui, Eliane Cases, Odile Chambin, Rémi SaurelAbstract:This work presents equilibrium and dynamic aspects for the adsorption at the oil–water interface of Pea ( Pisum sativum L.) Protein isolate (PPI). Dynamic interfacial tension, γ , and surface viscoelasticity modulus, ε , were determined using pendant-drop method. Adsorption kinetics studies revealed that Pea Proteins adsorb faster at pH 7.0 than at acidic pH (pH 2.4). On the other hand, the measured ε is lower at pH 7.0. This is probably due to fast adsorption, leading to the formation of inhomogeneous film structures. In fact, compared with pHs above the isoelectric point (p I ~ 4.3), acidic conditions slow down the adsorption, but the modulus is increased. Pea-Protein-stabilized emulsions are more stable to creaming at acidic pH and their particle-size distributions are more homogeneous in these conditions. Effect of pH on interfacial properties and on properties of oil-in-water emulsions stabilized by PPI was interpreted in terms of Pea Protein solubility, globulin dissociation, and oil-droplet surface electrostatic charge. We propose that at acidic conditions, adsorbed dissociated globulins form stronger and denser viscoelastic networks when adsorbed at oil–water interface. Consequently, the pH-dependence of Pea-globulin-stabilized emulsions properties could be of great interest to tune barrier properties of oil/water interfacial membranes for several applications such as encapsulation and controlled release of lipophilic bioactive components within the food, medical, and pharmaceutical industries.
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Interfacial and Emulsifying Characteristics of Acid-treated Pea Protein
Food Biophysics, 2009Co-Authors: Adem Gharsallaoui, Eliane Cases, Odile Chambin, Rémi SaurelAbstract:This work presents equilibrium and dynamic aspects for the adsorption at the oil–water interface of Pea ( Pisum sativum L.) Protein isolate (PPI). Dynamic interfacial tension, γ , and surface viscoelasticity modulus, ε , were determined using pendant-drop method. Adsorption kinetics studies revealed that Pea Proteins adsorb faster at pH 7.0 than at acidic pH (pH 2.4). On the other hand, the measured ε is lower at pH 7.0. This is probably due to fast adsorption, leading to the formation of inhomogeneous film structures. In fact, compared with pHs above the isoelectric point (p I ~ 4.3), acidic conditions slow down the adsorption, but the modulus is increased. Pea-Protein-stabilized emulsions are more stable to creaming at acidic pH and their particle-size distributions are more homogeneous in these conditions. Effect of pH on interfacial properties and on properties of oil-in-water emulsions stabilized by PPI was interpreted in terms of Pea Protein solubility, globulin dissociation, and oil-droplet surface electrostatic charge. We propose that at acidic conditions, adsorbed dissociated globulins form stronger and denser viscoelastic networks when adsorbed at oil–water interface. Consequently, the pH-dependence of Pea-globulin-stabilized emulsions properties could be of great interest to tune barrier properties of oil/water interfacial membranes for several applications such as encapsulation and controlled release of lipophilic bioactive components within the food, medical, and pharmaceutical industries.
Eliane Cases - One of the best experts on this subject based on the ideXlab platform.
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Utilisation of pectin coating to enhance spray-dry stability of Pea Protein-stabilised oil-in-water emulsions
Food Chemistry, 2010Co-Authors: Adem Gharsallaoui, Eliane Cases, Odile Chambin, Rémi Saurel, Andrée Voilley, Philippe CayotAbstract:In this study, development of Pea (Pisum sativum) Protein stabilised dry and reconstituted emulsions is presented. Dry emulsions were prepared by spray-drying liquid emulsions in a laboratory spray-dryer. The effect of drying on the physical stability of oil-in-water emulsions containing Pea Protein-coated and Pea Protein/pectin-coated oil droplets has been studied. Oil-in-water emulsions (5 wt.% Miglyol 812 N, 0.25 wt.% Pea Protein, 11% maltodextrin, pH 2.4) were prepared that contained 0 (primary emulsion) or 0.2 wt.% pectin (secondary emulsion). The emulsions were then subjected to spray-drying and reconstitution (pH 2.4). The stability of the emulsions to dry processing was then analysed using oil droplet size, microstructure, Zeta potential, and creaming measurements. Obtained results showed that the secondary emulsions had better stability to droplet aggregation after drying than primary emulsions. To interpret these results, we propound that pectin, an anionic polysaccharide, formed a less charged protective layer around the Protein interfacial film surrounding the oil droplets that improved their stability to spray-drying mainly by increasing steric effects.
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Effect of high methoxyl pectin on Pea Protein in aqueous solution and at oil/water interface
Carbohydrate Polymers, 2010Co-Authors: Adem Gharsallaoui, Eliane Cases, Odile Chambin, Kosuke Yamauchi, Rémi SaurelAbstract:The effect of the addition of high methoxyl pectin on the stability of Pea Protein isolate emulsions was investigated. Except for low pectin concentrations at acidic pHs where bridging flocculation occurred the addition of pectin improved emulsion stability to pH changes and depletion flocculation induced by maltodextrin addition. The mechanism of pectin induced stability was probed by measuring Protein-pectin complex formation in solution, zeta potential of the emulsions droplets and the change in surface viscoelasticity on pectin addition. The phase diagrams of pectin-Pea Protein isolate in solution and pectin-Pea Protein-stabilized emulsions were established based on the obtained experimental results. These diagrams showed that under acidic conditions and at low pectin concentrations, electrostatic bridging phenomena leads to the formation of high size pectin-Protein complexes causing an increase in turbidity in solution and oil droplet flocculation in emulsions. It was concluded that the pectin induced stability could be mainly assigned to steric repulsion and oil-water interfacial membrane rigidity improvement after pectin adsorption. In fact, the emulsions formed after pectin adsorption could consist of oil droplets surrounded by multilayer interfacial coatings, which are comprised of an inner interfacial Protein film and an outer pectin layer.
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effect of high methoxyl pectin on Pea Protein in aqueous solution and at oil water interface
Carbohydrate Polymers, 2010Co-Authors: Adem Gharsallaoui, Eliane Cases, Odile Chambin, Kosuke Yamauchi, Rémi SaurelAbstract:Abstract The effect of the addition of high methoxyl pectin on the stability of Pea Protein isolate emulsions was investigated. Except for low pectin concentrations at acidic pHs where bridging flocculation occurred the addition of pectin improved emulsion stability to pH changes and depletion flocculation induced by maltodextrin addition. The mechanism of pectin induced stability was probed by measuring Protein–pectin complex formation in solution, zeta potential of the emulsions droplets and the change in surface viscoelasticity on pectin addition. The phase diagrams of pectin–Pea Protein isolate in solution and pectin–Pea Protein-stabilized emulsions were established based on the obtained experimental results. These diagrams showed that under acidic conditions and at low pectin concentrations, electrostatic bridging phenomena leads to the formation of high size pectin–Protein complexes causing an increase in turbidity in solution and oil droplet flocculation in emulsions. It was concluded that the pectin induced stability could be mainly assigned to steric repulsion and oil–water interfacial membrane rigidity improvement after pectin adsorption. In fact, the emulsions formed after pectin adsorption could consist of oil droplets surrounded by multilayer interfacial coatings, which are comprised of an inner interfacial Protein film and an outer pectin layer.
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Interfacial and Emulsifying Characteristics of Acid-treated Pea Protein
Food Biophysics, 2009Co-Authors: Adem Gharsallaoui, Eliane Cases, Odile Chambin, Rémi SaurelAbstract:This work presents equilibrium and dynamic aspects for the adsorption at the oil–water interface of Pea ( Pisum sativum L.) Protein isolate (PPI). Dynamic interfacial tension, γ , and surface viscoelasticity modulus, ε , were determined using pendant-drop method. Adsorption kinetics studies revealed that Pea Proteins adsorb faster at pH 7.0 than at acidic pH (pH 2.4). On the other hand, the measured ε is lower at pH 7.0. This is probably due to fast adsorption, leading to the formation of inhomogeneous film structures. In fact, compared with pHs above the isoelectric point (p I ~ 4.3), acidic conditions slow down the adsorption, but the modulus is increased. Pea-Protein-stabilized emulsions are more stable to creaming at acidic pH and their particle-size distributions are more homogeneous in these conditions. Effect of pH on interfacial properties and on properties of oil-in-water emulsions stabilized by PPI was interpreted in terms of Pea Protein solubility, globulin dissociation, and oil-droplet surface electrostatic charge. We propose that at acidic conditions, adsorbed dissociated globulins form stronger and denser viscoelastic networks when adsorbed at oil–water interface. Consequently, the pH-dependence of Pea-globulin-stabilized emulsions properties could be of great interest to tune barrier properties of oil/water interfacial membranes for several applications such as encapsulation and controlled release of lipophilic bioactive components within the food, medical, and pharmaceutical industries.
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Interfacial and Emulsifying Characteristics of Acid-treated Pea Protein
Food Biophysics, 2009Co-Authors: Adem Gharsallaoui, Eliane Cases, Odile Chambin, Rémi SaurelAbstract:This work presents equilibrium and dynamic aspects for the adsorption at the oil–water interface of Pea ( Pisum sativum L.) Protein isolate (PPI). Dynamic interfacial tension, γ , and surface viscoelasticity modulus, ε , were determined using pendant-drop method. Adsorption kinetics studies revealed that Pea Proteins adsorb faster at pH 7.0 than at acidic pH (pH 2.4). On the other hand, the measured ε is lower at pH 7.0. This is probably due to fast adsorption, leading to the formation of inhomogeneous film structures. In fact, compared with pHs above the isoelectric point (p I ~ 4.3), acidic conditions slow down the adsorption, but the modulus is increased. Pea-Protein-stabilized emulsions are more stable to creaming at acidic pH and their particle-size distributions are more homogeneous in these conditions. Effect of pH on interfacial properties and on properties of oil-in-water emulsions stabilized by PPI was interpreted in terms of Pea Protein solubility, globulin dissociation, and oil-droplet surface electrostatic charge. We propose that at acidic conditions, adsorbed dissociated globulins form stronger and denser viscoelastic networks when adsorbed at oil–water interface. Consequently, the pH-dependence of Pea-globulin-stabilized emulsions properties could be of great interest to tune barrier properties of oil/water interfacial membranes for several applications such as encapsulation and controlled release of lipophilic bioactive components within the food, medical, and pharmaceutical industries.
Odile Chambin - One of the best experts on this subject based on the ideXlab platform.
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Utilisation of pectin coating to enhance spray-dry stability of Pea Protein-stabilised oil-in-water emulsions
Food Chemistry, 2010Co-Authors: Adem Gharsallaoui, Eliane Cases, Odile Chambin, Rémi Saurel, Andrée Voilley, Philippe CayotAbstract:In this study, development of Pea (Pisum sativum) Protein stabilised dry and reconstituted emulsions is presented. Dry emulsions were prepared by spray-drying liquid emulsions in a laboratory spray-dryer. The effect of drying on the physical stability of oil-in-water emulsions containing Pea Protein-coated and Pea Protein/pectin-coated oil droplets has been studied. Oil-in-water emulsions (5 wt.% Miglyol 812 N, 0.25 wt.% Pea Protein, 11% maltodextrin, pH 2.4) were prepared that contained 0 (primary emulsion) or 0.2 wt.% pectin (secondary emulsion). The emulsions were then subjected to spray-drying and reconstitution (pH 2.4). The stability of the emulsions to dry processing was then analysed using oil droplet size, microstructure, Zeta potential, and creaming measurements. Obtained results showed that the secondary emulsions had better stability to droplet aggregation after drying than primary emulsions. To interpret these results, we propound that pectin, an anionic polysaccharide, formed a less charged protective layer around the Protein interfacial film surrounding the oil droplets that improved their stability to spray-drying mainly by increasing steric effects.
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Effect of high methoxyl pectin on Pea Protein in aqueous solution and at oil/water interface
Carbohydrate Polymers, 2010Co-Authors: Adem Gharsallaoui, Eliane Cases, Odile Chambin, Kosuke Yamauchi, Rémi SaurelAbstract:The effect of the addition of high methoxyl pectin on the stability of Pea Protein isolate emulsions was investigated. Except for low pectin concentrations at acidic pHs where bridging flocculation occurred the addition of pectin improved emulsion stability to pH changes and depletion flocculation induced by maltodextrin addition. The mechanism of pectin induced stability was probed by measuring Protein-pectin complex formation in solution, zeta potential of the emulsions droplets and the change in surface viscoelasticity on pectin addition. The phase diagrams of pectin-Pea Protein isolate in solution and pectin-Pea Protein-stabilized emulsions were established based on the obtained experimental results. These diagrams showed that under acidic conditions and at low pectin concentrations, electrostatic bridging phenomena leads to the formation of high size pectin-Protein complexes causing an increase in turbidity in solution and oil droplet flocculation in emulsions. It was concluded that the pectin induced stability could be mainly assigned to steric repulsion and oil-water interfacial membrane rigidity improvement after pectin adsorption. In fact, the emulsions formed after pectin adsorption could consist of oil droplets surrounded by multilayer interfacial coatings, which are comprised of an inner interfacial Protein film and an outer pectin layer.
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effect of high methoxyl pectin on Pea Protein in aqueous solution and at oil water interface
Carbohydrate Polymers, 2010Co-Authors: Adem Gharsallaoui, Eliane Cases, Odile Chambin, Kosuke Yamauchi, Rémi SaurelAbstract:Abstract The effect of the addition of high methoxyl pectin on the stability of Pea Protein isolate emulsions was investigated. Except for low pectin concentrations at acidic pHs where bridging flocculation occurred the addition of pectin improved emulsion stability to pH changes and depletion flocculation induced by maltodextrin addition. The mechanism of pectin induced stability was probed by measuring Protein–pectin complex formation in solution, zeta potential of the emulsions droplets and the change in surface viscoelasticity on pectin addition. The phase diagrams of pectin–Pea Protein isolate in solution and pectin–Pea Protein-stabilized emulsions were established based on the obtained experimental results. These diagrams showed that under acidic conditions and at low pectin concentrations, electrostatic bridging phenomena leads to the formation of high size pectin–Protein complexes causing an increase in turbidity in solution and oil droplet flocculation in emulsions. It was concluded that the pectin induced stability could be mainly assigned to steric repulsion and oil–water interfacial membrane rigidity improvement after pectin adsorption. In fact, the emulsions formed after pectin adsorption could consist of oil droplets surrounded by multilayer interfacial coatings, which are comprised of an inner interfacial Protein film and an outer pectin layer.
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Interfacial and Emulsifying Characteristics of Acid-treated Pea Protein
Food Biophysics, 2009Co-Authors: Adem Gharsallaoui, Eliane Cases, Odile Chambin, Rémi SaurelAbstract:This work presents equilibrium and dynamic aspects for the adsorption at the oil–water interface of Pea ( Pisum sativum L.) Protein isolate (PPI). Dynamic interfacial tension, γ , and surface viscoelasticity modulus, ε , were determined using pendant-drop method. Adsorption kinetics studies revealed that Pea Proteins adsorb faster at pH 7.0 than at acidic pH (pH 2.4). On the other hand, the measured ε is lower at pH 7.0. This is probably due to fast adsorption, leading to the formation of inhomogeneous film structures. In fact, compared with pHs above the isoelectric point (p I ~ 4.3), acidic conditions slow down the adsorption, but the modulus is increased. Pea-Protein-stabilized emulsions are more stable to creaming at acidic pH and their particle-size distributions are more homogeneous in these conditions. Effect of pH on interfacial properties and on properties of oil-in-water emulsions stabilized by PPI was interpreted in terms of Pea Protein solubility, globulin dissociation, and oil-droplet surface electrostatic charge. We propose that at acidic conditions, adsorbed dissociated globulins form stronger and denser viscoelastic networks when adsorbed at oil–water interface. Consequently, the pH-dependence of Pea-globulin-stabilized emulsions properties could be of great interest to tune barrier properties of oil/water interfacial membranes for several applications such as encapsulation and controlled release of lipophilic bioactive components within the food, medical, and pharmaceutical industries.
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Interfacial and Emulsifying Characteristics of Acid-treated Pea Protein
Food Biophysics, 2009Co-Authors: Adem Gharsallaoui, Eliane Cases, Odile Chambin, Rémi SaurelAbstract:This work presents equilibrium and dynamic aspects for the adsorption at the oil–water interface of Pea ( Pisum sativum L.) Protein isolate (PPI). Dynamic interfacial tension, γ , and surface viscoelasticity modulus, ε , were determined using pendant-drop method. Adsorption kinetics studies revealed that Pea Proteins adsorb faster at pH 7.0 than at acidic pH (pH 2.4). On the other hand, the measured ε is lower at pH 7.0. This is probably due to fast adsorption, leading to the formation of inhomogeneous film structures. In fact, compared with pHs above the isoelectric point (p I ~ 4.3), acidic conditions slow down the adsorption, but the modulus is increased. Pea-Protein-stabilized emulsions are more stable to creaming at acidic pH and their particle-size distributions are more homogeneous in these conditions. Effect of pH on interfacial properties and on properties of oil-in-water emulsions stabilized by PPI was interpreted in terms of Pea Protein solubility, globulin dissociation, and oil-droplet surface electrostatic charge. We propose that at acidic conditions, adsorbed dissociated globulins form stronger and denser viscoelastic networks when adsorbed at oil–water interface. Consequently, the pH-dependence of Pea-globulin-stabilized emulsions properties could be of great interest to tune barrier properties of oil/water interfacial membranes for several applications such as encapsulation and controlled release of lipophilic bioactive components within the food, medical, and pharmaceutical industries.
Rotimi E. Aluko - One of the best experts on this subject based on the ideXlab platform.
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Enzymatic Pea Protein Hydrolysates Are Active Trypsin and Chymotrypsin Inhibitors
Foods, 2019Co-Authors: Temitola O. Awosika, Rotimi E. AlukoAbstract:In this work, we report the potency of enzymatic hydrolysates of Pea Proteins against trypsin and chymotrypsin. Pea Protein concentrate was digested with each of alcalase, chymotrypsin, pepsin, and trypsin, followed by membrane separation of the Protein hydrolysates into peptide fractions ( 3 kDa. Kinetics of enzyme inhibition indicate peptides were bound to the enzyme active site in a competitive mode that led to reduced catalysis. We conclude that the Pea peptides could function as useful tools to promote human health and as a preservative during food processing and storage.
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Modification of the structural, emulsifying, and foaming properties of an isolated Pea Protein by thermal pretreatment
Cyta-journal of Food, 2018Co-Authors: Dongfang Chao, Rotimi E. AlukoAbstract:Pea Protein isolate (PPI) prepared through isoelectric Protein precipitation was heat-treated between 50°C and 100°C. The effect of heat treatment on the structural and functional properties of pro...
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blood pressure lowering effect of a Pea Protein hydrolysate in hypertensive rats and humans
Journal of Agricultural and Food Chemistry, 2011Co-Authors: Natalie Prairie, Chibuike C. Udenigwe, Abayomi P Adebiyi, Paramjit S Tappia, Harold M Aukema, Peter J H Jones, Rotimi E. AlukoAbstract:The blood pressure lowering effect of a Pea Protein hydrolysate (PPH) that contained <3 kDa peptides, isolated by membrane ultrafiltration from the thermolysin digest of Pea Protein isolate (PPI), was examined using different rat models of hypertension as well as hypertensive human subjects. The PPH showed weak in vitro activities against renin and angiotensin converting enzyme (ACE) with inhibitory activities of 17 and 19%, respectively, at 1 mg/mL test concentration. Oral administration of the PPH to spontaneously hypertensive rats (SHR) at doses of 100 and 200 mg/kg body weight led to a lowering of hourly systolic blood pressure (SBP), with a maximum reduction of 19 mmHg at 4 h. In contrast, orally administered unhydrolyzed PPI had no blood pressure reducing effect in SHR, suggesting that thermolysin hydrolysis may have been responsible for releasing bioactive peptides from the native Protein. Oral administration of the PPH to the Han:SPRD-cy rat (a model of chronic kidney disease) over an 8-week perio...
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Effects of cationic property on the in vitro antioxidant activities of Pea Protein hydrolysate fractions
Food Research International, 2011Co-Authors: Trisha L. Pownall, Chibuike C. Udenigwe, Rotimi E. AlukoAbstract:Abstract Yellow Pea seed Protein-derived peptides were produced through enzymatic hydrolysis of Pea Protein isolate, which was followed by ultrafiltration to isolate peptides with
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Structural modulation of calmodulin and calmodulin-dependent Protein kinase II by Pea Protein hydrolysates
International Journal of Food Sciences and Nutrition, 2009Co-Authors: Rotimi E. AlukoAbstract:The effects of two fractions of Pea Protein hydrolysate with high levels of positively charged amino acids on the structural conformations of calmodulin (CaM) and CaM-dependent Protein kinase II (CaMKII) were determined using fluorescence and circular dichroism methods. In the presence of Ca2 + , addition of the Protein hydrolysates to CaM and CaM/CaMKII complex led to increased exposure of aromatic groups as measured by intrinsic and extrinsic fluorescence spectroscopy. Near-UV circular dichroism data revealed an increase in the tertiary structure of CaM in the presence of Pea Protein hydrolysates. Effect of the Protein hydrolysates on the CaM structure was greater with the fraction that contained higher contents of arginine and lysine when compared with the fraction with lower levels of these two amino acids. We concluded that the presence of the Pea Protein hydrolysates led to rearrangement of the native Protein structure and exposure of buried hydrophobic groups of CaM and/or CaMKII.