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Monique Lacroix - One of the best experts on this subject based on the ideXlab platform.
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γ-Irradiation Influence on the Structure and Properties of Calcium Caseinate−Whey Protein Isolate Based Films. Part 2. Influence of Polysaccharide Addition and Radiation Treatment on the Structure and Functional Properties of the Films
Journal of Agricultural and Food Chemistry, 2006Co-Authors: Krystyna Cieśla, And Stephane Salmieri, Monique LacroixAbstract:The influence of γ-irradiation (32 kGy) followed by the addition of polysaccharides (potato starch, soluble potato starch, and sodium alginate) and heating on the properties of the films based on Calcium Caseinate (CC)−whey proteins isolate (WPI) and the gels formed with CaCl2 was evaluated. Radiation induced an improvement of the mechanical and barrier properties of all films. The polysaccharides' effect on the irradiated and non-irradiated CC−WPI gels could be predicted as the sum of their separate effects on CC and on WPI, apart from the alginate interaction with the irradiated CC−WPI. The better properties of the films achieved after admixing polysaccharides to the formerly irradiated protein solution correspond to the smaller strength of gels. Properties of the films and gels prepared using the irradiated proteins and alginate differed depending on whether alginate was admixed before or after irradiation. Results were related to the protein structure, interaction with polysaccharides, and the film's ...
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γ irradiation influence on the structure and properties of Calcium Caseinate whey protein isolate based films part 2 influence of polysaccharide addition and radiation treatment on the structure and functional properties of the films
Journal of Agricultural and Food Chemistry, 2006Co-Authors: Krystyna Cieśla, And Stephane Salmieri, Monique LacroixAbstract:The influence of γ-irradiation (32 kGy) followed by the addition of polysaccharides (potato starch, soluble potato starch, and sodium alginate) and heating on the properties of the films based on Calcium Caseinate (CC)−whey proteins isolate (WPI) and the gels formed with CaCl2 was evaluated. Radiation induced an improvement of the mechanical and barrier properties of all films. The polysaccharides' effect on the irradiated and non-irradiated CC−WPI gels could be predicted as the sum of their separate effects on CC and on WPI, apart from the alginate interaction with the irradiated CC−WPI. The better properties of the films achieved after admixing polysaccharides to the formerly irradiated protein solution correspond to the smaller strength of gels. Properties of the films and gels prepared using the irradiated proteins and alginate differed depending on whether alginate was admixed before or after irradiation. Results were related to the protein structure, interaction with polysaccharides, and the film's ...
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γ-Irradiation Influence on the Structure and Properties of Calcium Caseinate−Whey Protein Isolate Based Films. Part 1. Radiation Effect On the Structure of Proteins Gels and Films
Journal of Agricultural and Food Chemistry, 2006Co-Authors: Krystyna Cieśla, Stephane Salmieri, Monique LacroixAbstract:Brookfield viscosimetry, Fourier transform infrared spectroscopy, transmission electron microscopy (TEM), and measurements of the texture strength of gels formed with CaCl2 and the mechanical and barrier properties of the film were applied in studies of gel formation and structural and mechanical properties of gels and films prepared using Calcium Caseinate (CC)−whey protein isolate (WPI)−glycerol (1:1:1), control, and irradiated with 60Co γ rays using a 32 kGy dose. The irradiated gels have appeared to be more “fine-stranded” as compared to the more “particulate” control gels and lead to the formation of more rigid films with improved mechanical strength and barrier properties. This results from cross-linking and the modification of protein conformations were induced by irradiation, in particular the increase in the β-sheet and β-strand contents. Structural modifications taking place in CC−WPI composition are related to modifications taking place separately in CC and WPI. Improvement of the properties of...
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γ irradiation influence on the structure and properties of Calcium Caseinate whey protein isolate based films part 1 radiation effect on the structure of proteins gels and films
Journal of Agricultural and Food Chemistry, 2006Co-Authors: Krystyna Cieśla, Stephane Salmieri, Monique LacroixAbstract:Brookfield viscosimetry, Fourier transform infrared spectroscopy, transmission electron microscopy (TEM), and measurements of the texture strength of gels formed with CaCl2 and the mechanical and barrier properties of the film were applied in studies of gel formation and structural and mechanical properties of gels and films prepared using Calcium Caseinate (CC)−whey protein isolate (WPI)−glycerol (1:1:1), control, and irradiated with 60Co γ rays using a 32 kGy dose. The irradiated gels have appeared to be more “fine-stranded” as compared to the more “particulate” control gels and lead to the formation of more rigid films with improved mechanical strength and barrier properties. This results from cross-linking and the modification of protein conformations were induced by irradiation, in particular the increase in the β-sheet and β-strand contents. Structural modifications taking place in CC−WPI composition are related to modifications taking place separately in CC and WPI. Improvement of the properties of...
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Effect of Edible Coating Process and Irradiation Treatment of Strawberry fragaria spp. on Storage-keeping Quality
Journal of Food Science, 2003Co-Authors: C. Vachon, Monique Lacroix, G. D'aprano, M. LetendreAbstract:ABSTRACT: Gamma-irradiation and various edible coatings were tested on fresh strawberries (Fragaria spp.) for keeping fruit quality and extending shelf life. Four coatings based on milk protein were evaluated. In 1 experiment, coating formulation based on Caseinate and/or strawberries were irradiated using a 60Co source. Both gamma-irradiation treatment and edible coating process significantly delayed (p ≤ 0.05) molds growth. Edible coating based on irradiated Caseinate was more effective than that of unirradiated Caseinate. In a 2nd experiment, 3 irradiated coatings based on Calcium Caseinate and whey proteins were evaluated. The coating formulation based on 1:1 Caseinate-whey was found to be more effective than those based on Calcium Caseinate. Addition of Calcium chloride or a mixture of pectin and agar increased the effectiveness of the coating by delaying molds' apparition.
Wim G. Bouwman - One of the best experts on this subject based on the ideXlab platform.
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Small angle neutron scattering quantifies the hierarchical structure in fibrous Calcium Caseinate
Food Hydrocolloids, 2020Co-Authors: Bei Tian, Zhaojun Wang, Atze Jan Van Der Goot, Liliana De Campo, Elliot P. Gilbert, Robert M. Dalgliesh, Evgenii Velichko, Wim G. BouwmanAbstract:Pronounced fibres are formed through simple shearing of a dense Calcium Caseinate dispersion. Both mechanical tests and scanning electron microscopy images demonstrate that the material is anisotropic. It is hypothesised that Calcium Caseinate aggregates, under shear, align into micro-fibres and bundle further into a hierarchical structure. Yet no direct evidence at the sub-micron length scale can support the assumption. Small angle neutron scattering (SANS) experiments were conducted on Calcium Caseinate samples prepared at different conditions. Analysis of the SANS data revealed that the micro-fibres have a diameter of ∼100nm and a length of ∼300nm. The addition of enzyme and air contributed to longer and thinner micro-fibres. Furthermore, the extent of fibre alignment at the micro-scale and the macroscopic anisotropy index followed the same trends with varying processing conditions. It is concluded that the material does indeed possess a hierarchical structure and the micro-fibres are responsible for the anisotropy on the macro-scale.
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Fibre formation in Calcium Caseinate influenced by solvent isotope effect and drying method – A neutron spectroscopy study
Chemical Engineering Science, 2019Co-Authors: Bei Tian, Atze Jan Van Der Goot, Victoria García Sakai, Catherine Pappas, Wim G. BouwmanAbstract:Abstract We present an investigation of the dynamics of Calcium Caseinate as a function of hydration, solvent isotope (H2O and D2O) and drying methods (roller drying and spray drying), using quasi-elastic neutron scattering (QENS). These factors are key to the formation of fibres in this material which makes it a potential candidate as a next-generation meat analogue. Using a phenomenological model, we find that the relaxation times of the dry spray dried powder decrease with increasing temperatures, while they do not change for the roller dried powder. The spectra of the hydrated samples reveal two independent picosecond processes, both reflecting localized re-orientational motions. We hypothesize that the faster motion is due to the external protein groups that are hydrophilic and the slower motion is due to the internal groups that are hydrophobic. The solvent effect of D2O is not limited to the external groups but prevails to the internal groups where less protons are mobile compared to the H2O hydrated samples. Higher temperatures narrow the number difference in mobile protons, possibly by altering the weak interactions inside the protein aggregates. These findings suggest that a harsh and longer drying process contributes to less active protein side-groups and highlight the hydrophobic effect of D2O on the fibre formation in Calcium Caseinate.
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fibre formation in Calcium Caseinate influenced by solvent isotope effect and drying method a neutron spectroscopy study
Chemical Engineering Science, 2019Co-Authors: Bei Tian, Atze Jan Van Der Goot, Victoria García Sakai, Catherine Pappas, Wim G. BouwmanAbstract:Abstract We present an investigation of the dynamics of Calcium Caseinate as a function of hydration, solvent isotope (H2O and D2O) and drying methods (roller drying and spray drying), using quasi-elastic neutron scattering (QENS). These factors are key to the formation of fibres in this material which makes it a potential candidate as a next-generation meat analogue. Using a phenomenological model, we find that the relaxation times of the dry spray dried powder decrease with increasing temperatures, while they do not change for the roller dried powder. The spectra of the hydrated samples reveal two independent picosecond processes, both reflecting localized re-orientational motions. We hypothesize that the faster motion is due to the external protein groups that are hydrophilic and the slower motion is due to the internal groups that are hydrophobic. The solvent effect of D2O is not limited to the external groups but prevails to the internal groups where less protons are mobile compared to the H2O hydrated samples. Higher temperatures narrow the number difference in mobile protons, possibly by altering the weak interactions inside the protein aggregates. These findings suggest that a harsh and longer drying process contributes to less active protein side-groups and highlight the hydrophobic effect of D2O on the fibre formation in Calcium Caseinate.
Atze Jan Van Der Goot - One of the best experts on this subject based on the ideXlab platform.
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Small angle neutron scattering quantifies the hierarchical structure in fibrous Calcium Caseinate
Food Hydrocolloids, 2020Co-Authors: Bei Tian, Zhaojun Wang, Atze Jan Van Der Goot, Liliana De Campo, Elliot P. Gilbert, Robert M. Dalgliesh, Evgenii Velichko, Wim G. BouwmanAbstract:Pronounced fibres are formed through simple shearing of a dense Calcium Caseinate dispersion. Both mechanical tests and scanning electron microscopy images demonstrate that the material is anisotropic. It is hypothesised that Calcium Caseinate aggregates, under shear, align into micro-fibres and bundle further into a hierarchical structure. Yet no direct evidence at the sub-micron length scale can support the assumption. Small angle neutron scattering (SANS) experiments were conducted on Calcium Caseinate samples prepared at different conditions. Analysis of the SANS data revealed that the micro-fibres have a diameter of ∼100nm and a length of ∼300nm. The addition of enzyme and air contributed to longer and thinner micro-fibres. Furthermore, the extent of fibre alignment at the micro-scale and the macroscopic anisotropy index followed the same trends with varying processing conditions. It is concluded that the material does indeed possess a hierarchical structure and the micro-fibres are responsible for the anisotropy on the macro-scale.
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Process history of Calcium Caseinate affects fibre formation
Journal of Food Engineering, 2020Co-Authors: Zhaojun Wang, Birgit L. Dekkers, Atze Jan Van Der GootAbstract:Abstract In this study, we compared the physical properties and structuring potential of spray-dried Calcium Caseinate (Scaca) and roller-dried Calcium Caseinate (Rcaca). Scaca formed more pronounced fibrous materials upon shearing compared with Rcaca. The rheological measurements revealed that the Scaca dispersion exhibited more solid-like behaviour. Besides, the particle size in excess water was larger for Rcaca (2–300 μm), while Scaca mainly contained small Caseinate aggregates (
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Fibre formation in Calcium Caseinate influenced by solvent isotope effect and drying method – A neutron spectroscopy study
Chemical Engineering Science, 2019Co-Authors: Bei Tian, Atze Jan Van Der Goot, Victoria García Sakai, Catherine Pappas, Wim G. BouwmanAbstract:Abstract We present an investigation of the dynamics of Calcium Caseinate as a function of hydration, solvent isotope (H2O and D2O) and drying methods (roller drying and spray drying), using quasi-elastic neutron scattering (QENS). These factors are key to the formation of fibres in this material which makes it a potential candidate as a next-generation meat analogue. Using a phenomenological model, we find that the relaxation times of the dry spray dried powder decrease with increasing temperatures, while they do not change for the roller dried powder. The spectra of the hydrated samples reveal two independent picosecond processes, both reflecting localized re-orientational motions. We hypothesize that the faster motion is due to the external protein groups that are hydrophilic and the slower motion is due to the internal groups that are hydrophobic. The solvent effect of D2O is not limited to the external groups but prevails to the internal groups where less protons are mobile compared to the H2O hydrated samples. Higher temperatures narrow the number difference in mobile protons, possibly by altering the weak interactions inside the protein aggregates. These findings suggest that a harsh and longer drying process contributes to less active protein side-groups and highlight the hydrophobic effect of D2O on the fibre formation in Calcium Caseinate.
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fibre formation in Calcium Caseinate influenced by solvent isotope effect and drying method a neutron spectroscopy study
Chemical Engineering Science, 2019Co-Authors: Bei Tian, Atze Jan Van Der Goot, Victoria García Sakai, Catherine Pappas, Wim G. BouwmanAbstract:Abstract We present an investigation of the dynamics of Calcium Caseinate as a function of hydration, solvent isotope (H2O and D2O) and drying methods (roller drying and spray drying), using quasi-elastic neutron scattering (QENS). These factors are key to the formation of fibres in this material which makes it a potential candidate as a next-generation meat analogue. Using a phenomenological model, we find that the relaxation times of the dry spray dried powder decrease with increasing temperatures, while they do not change for the roller dried powder. The spectra of the hydrated samples reveal two independent picosecond processes, both reflecting localized re-orientational motions. We hypothesize that the faster motion is due to the external protein groups that are hydrophilic and the slower motion is due to the internal groups that are hydrophobic. The solvent effect of D2O is not limited to the external groups but prevails to the internal groups where less protons are mobile compared to the H2O hydrated samples. Higher temperatures narrow the number difference in mobile protons, possibly by altering the weak interactions inside the protein aggregates. These findings suggest that a harsh and longer drying process contributes to less active protein side-groups and highlight the hydrophobic effect of D2O on the fibre formation in Calcium Caseinate.
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Maltodextrin promotes Calcium Caseinate fibre formation through air inclusion
Food Hydrocolloids, 2019Co-Authors: Zhaojun Wang, Birgit L. Dekkers, Remko M. Boom, Atze Jan Van Der GootAbstract:Abstract Commercial Calcium Caseinate is available as spray-dried and roller-dried powder. Shearing a dense spray-dried Calcium Caseinate dispersion gives rise to a fibrous material, whereas shearing dense roller-dried Calcium Caseinate yields a layered material with only slight anisotropy in mechanical strength. The addition of a polysaccharide phase in a continuous protein phase may lead to formation of fibrous structures after shearing, which is hypothesized to be a result of the elongation and orientation of the dispersed polysaccharide domains. We report the effect of the addition of maltodextrin to roller-dried Calcium Caseinate on structure formation. The strength of the material increased with the addition of maltodextrin, which is partly caused by the withdrawal of water from the Caseinate phase towards the maltodextrin phase, leading to a higher local Caseinate concentration. The anisotropy of fracture stress and fracture strain were enhanced with up to 5 wt% maltodextrin. The effect of maltodextrin on the mechanical anisotropy and fibrous appearance could be ascribed to the greater air incorporation as a result of the presence of maltodextrin.
Bei Tian - One of the best experts on this subject based on the ideXlab platform.
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Small angle neutron scattering quantifies the hierarchical structure in fibrous Calcium Caseinate
Food Hydrocolloids, 2020Co-Authors: Bei Tian, Zhaojun Wang, Atze Jan Van Der Goot, Liliana De Campo, Elliot P. Gilbert, Robert M. Dalgliesh, Evgenii Velichko, Wim G. BouwmanAbstract:Pronounced fibres are formed through simple shearing of a dense Calcium Caseinate dispersion. Both mechanical tests and scanning electron microscopy images demonstrate that the material is anisotropic. It is hypothesised that Calcium Caseinate aggregates, under shear, align into micro-fibres and bundle further into a hierarchical structure. Yet no direct evidence at the sub-micron length scale can support the assumption. Small angle neutron scattering (SANS) experiments were conducted on Calcium Caseinate samples prepared at different conditions. Analysis of the SANS data revealed that the micro-fibres have a diameter of ∼100nm and a length of ∼300nm. The addition of enzyme and air contributed to longer and thinner micro-fibres. Furthermore, the extent of fibre alignment at the micro-scale and the macroscopic anisotropy index followed the same trends with varying processing conditions. It is concluded that the material does indeed possess a hierarchical structure and the micro-fibres are responsible for the anisotropy on the macro-scale.
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Fibre formation in Calcium Caseinate influenced by solvent isotope effect and drying method – A neutron spectroscopy study
Chemical Engineering Science, 2019Co-Authors: Bei Tian, Atze Jan Van Der Goot, Victoria García Sakai, Catherine Pappas, Wim G. BouwmanAbstract:Abstract We present an investigation of the dynamics of Calcium Caseinate as a function of hydration, solvent isotope (H2O and D2O) and drying methods (roller drying and spray drying), using quasi-elastic neutron scattering (QENS). These factors are key to the formation of fibres in this material which makes it a potential candidate as a next-generation meat analogue. Using a phenomenological model, we find that the relaxation times of the dry spray dried powder decrease with increasing temperatures, while they do not change for the roller dried powder. The spectra of the hydrated samples reveal two independent picosecond processes, both reflecting localized re-orientational motions. We hypothesize that the faster motion is due to the external protein groups that are hydrophilic and the slower motion is due to the internal groups that are hydrophobic. The solvent effect of D2O is not limited to the external groups but prevails to the internal groups where less protons are mobile compared to the H2O hydrated samples. Higher temperatures narrow the number difference in mobile protons, possibly by altering the weak interactions inside the protein aggregates. These findings suggest that a harsh and longer drying process contributes to less active protein side-groups and highlight the hydrophobic effect of D2O on the fibre formation in Calcium Caseinate.
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fibre formation in Calcium Caseinate influenced by solvent isotope effect and drying method a neutron spectroscopy study
Chemical Engineering Science, 2019Co-Authors: Bei Tian, Atze Jan Van Der Goot, Victoria García Sakai, Catherine Pappas, Wim G. BouwmanAbstract:Abstract We present an investigation of the dynamics of Calcium Caseinate as a function of hydration, solvent isotope (H2O and D2O) and drying methods (roller drying and spray drying), using quasi-elastic neutron scattering (QENS). These factors are key to the formation of fibres in this material which makes it a potential candidate as a next-generation meat analogue. Using a phenomenological model, we find that the relaxation times of the dry spray dried powder decrease with increasing temperatures, while they do not change for the roller dried powder. The spectra of the hydrated samples reveal two independent picosecond processes, both reflecting localized re-orientational motions. We hypothesize that the faster motion is due to the external protein groups that are hydrophilic and the slower motion is due to the internal groups that are hydrophobic. The solvent effect of D2O is not limited to the external groups but prevails to the internal groups where less protons are mobile compared to the H2O hydrated samples. Higher temperatures narrow the number difference in mobile protons, possibly by altering the weak interactions inside the protein aggregates. These findings suggest that a harsh and longer drying process contributes to less active protein side-groups and highlight the hydrophobic effect of D2O on the fibre formation in Calcium Caseinate.
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Air bubbles in Calcium Caseinate fibrous material enhances anisotropy
Food Hydrocolloids, 2019Co-Authors: Zhaojun Wang, Remko M. Boom, Bei Tian, Atze Jan Van Der GootAbstract:Dense Calcium Caseinate dispersions can be transformed into hierarchically fibrous structures by shear deformation. This transformation can be attributed to the intrinsic properties of Calcium Caseinate. Depending on the dispersion preparation method, a certain amount of air gets entrapped in the sheared protein matrix. Although anisotropy is obtained in the absence of entrapped air, the fibrous appearance and mechanical anisotropy of the Calcium Caseinate materials are more pronounced with dispersed air present. The presence of air induces the protein fibers to be arranged in microscale bundles, and the fracture strain and stress in the parallel direction are larger compared with the material without air. The effects can be understood from the alignment of the fibers in the parallel direction, providing strain energy dissipation. This study shows that creation of anisotropy is the result of interactions between multiple phases.
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Understanding the role of air and protein phase on mechanical anisotropy of Calcium Caseinate fibers.
Food Research International, 2019Co-Authors: Zhaojun Wang, Remko M. Boom, Bei Tian, Atze Jan Van Der GootAbstract:Calcium Caseinate dispersions can be transformed into anisotropic, fibrous materials using the concept of shear-induced structuring. The aim of this study is to further investigate the relative importance of air bubbles and protein on the mechanical anisotropy of Calcium Caseinate material. In this study, the effect of air on mechanical anisotropy of these fibrous materials was described with a load-bearing model, with the void fraction, and the bubble length and width as input parameters. The anisotropy of the protein phase was estimated using materials obtained from deaerated dispersions after shearing at different shear rates. We concluded that the deformation of air bubbles can only partly explain the mechanical anisotropy; the anisotropy of the protein phase is more important. Based on all results, we further concluded that the anisotropy of the protein phase was affected by the air bubbles present during the structuring process. This effect was explained by locally higher shear rate in the protein matrix during the structuring process.
Krystyna Cieśla - One of the best experts on this subject based on the ideXlab platform.
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γ-Irradiation Influence on the Structure and Properties of Calcium Caseinate−Whey Protein Isolate Based Films. Part 2. Influence of Polysaccharide Addition and Radiation Treatment on the Structure and Functional Properties of the Films
Journal of Agricultural and Food Chemistry, 2006Co-Authors: Krystyna Cieśla, And Stephane Salmieri, Monique LacroixAbstract:The influence of γ-irradiation (32 kGy) followed by the addition of polysaccharides (potato starch, soluble potato starch, and sodium alginate) and heating on the properties of the films based on Calcium Caseinate (CC)−whey proteins isolate (WPI) and the gels formed with CaCl2 was evaluated. Radiation induced an improvement of the mechanical and barrier properties of all films. The polysaccharides' effect on the irradiated and non-irradiated CC−WPI gels could be predicted as the sum of their separate effects on CC and on WPI, apart from the alginate interaction with the irradiated CC−WPI. The better properties of the films achieved after admixing polysaccharides to the formerly irradiated protein solution correspond to the smaller strength of gels. Properties of the films and gels prepared using the irradiated proteins and alginate differed depending on whether alginate was admixed before or after irradiation. Results were related to the protein structure, interaction with polysaccharides, and the film's ...
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γ irradiation influence on the structure and properties of Calcium Caseinate whey protein isolate based films part 2 influence of polysaccharide addition and radiation treatment on the structure and functional properties of the films
Journal of Agricultural and Food Chemistry, 2006Co-Authors: Krystyna Cieśla, And Stephane Salmieri, Monique LacroixAbstract:The influence of γ-irradiation (32 kGy) followed by the addition of polysaccharides (potato starch, soluble potato starch, and sodium alginate) and heating on the properties of the films based on Calcium Caseinate (CC)−whey proteins isolate (WPI) and the gels formed with CaCl2 was evaluated. Radiation induced an improvement of the mechanical and barrier properties of all films. The polysaccharides' effect on the irradiated and non-irradiated CC−WPI gels could be predicted as the sum of their separate effects on CC and on WPI, apart from the alginate interaction with the irradiated CC−WPI. The better properties of the films achieved after admixing polysaccharides to the formerly irradiated protein solution correspond to the smaller strength of gels. Properties of the films and gels prepared using the irradiated proteins and alginate differed depending on whether alginate was admixed before or after irradiation. Results were related to the protein structure, interaction with polysaccharides, and the film's ...
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γ-Irradiation Influence on the Structure and Properties of Calcium Caseinate−Whey Protein Isolate Based Films. Part 1. Radiation Effect On the Structure of Proteins Gels and Films
Journal of Agricultural and Food Chemistry, 2006Co-Authors: Krystyna Cieśla, Stephane Salmieri, Monique LacroixAbstract:Brookfield viscosimetry, Fourier transform infrared spectroscopy, transmission electron microscopy (TEM), and measurements of the texture strength of gels formed with CaCl2 and the mechanical and barrier properties of the film were applied in studies of gel formation and structural and mechanical properties of gels and films prepared using Calcium Caseinate (CC)−whey protein isolate (WPI)−glycerol (1:1:1), control, and irradiated with 60Co γ rays using a 32 kGy dose. The irradiated gels have appeared to be more “fine-stranded” as compared to the more “particulate” control gels and lead to the formation of more rigid films with improved mechanical strength and barrier properties. This results from cross-linking and the modification of protein conformations were induced by irradiation, in particular the increase in the β-sheet and β-strand contents. Structural modifications taking place in CC−WPI composition are related to modifications taking place separately in CC and WPI. Improvement of the properties of...
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γ irradiation influence on the structure and properties of Calcium Caseinate whey protein isolate based films part 1 radiation effect on the structure of proteins gels and films
Journal of Agricultural and Food Chemistry, 2006Co-Authors: Krystyna Cieśla, Stephane Salmieri, Monique LacroixAbstract:Brookfield viscosimetry, Fourier transform infrared spectroscopy, transmission electron microscopy (TEM), and measurements of the texture strength of gels formed with CaCl2 and the mechanical and barrier properties of the film were applied in studies of gel formation and structural and mechanical properties of gels and films prepared using Calcium Caseinate (CC)−whey protein isolate (WPI)−glycerol (1:1:1), control, and irradiated with 60Co γ rays using a 32 kGy dose. The irradiated gels have appeared to be more “fine-stranded” as compared to the more “particulate” control gels and lead to the formation of more rigid films with improved mechanical strength and barrier properties. This results from cross-linking and the modification of protein conformations were induced by irradiation, in particular the increase in the β-sheet and β-strand contents. Structural modifications taking place in CC−WPI composition are related to modifications taking place separately in CC and WPI. Improvement of the properties of...