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  1. Article ; Online: High-pressure microfluidization of whey proteins: Impact on protein structure and ability to bind and protect lutein.

    Vidotto, Danilo C / Mantovani, Raphaela A / Tavares, Guilherme M

    Food chemistry

    2022  Volume 382, Page(s) 132298

    Abstract: Dynamic high-pressure homogenization microfluidization (DHPM) is a versatile emerging technology that may be applied to food processing to achieve several goals. DHPM may, depending on nature of the molecules and the working parameters, induce changes in ...

    Abstract Dynamic high-pressure homogenization microfluidization (DHPM) is a versatile emerging technology that may be applied to food processing to achieve several goals. DHPM may, depending on nature of the molecules and the working parameters, induce changes in protein structure, which may improve or impair their techno-functional properties and ability to bind other molecules. In this context, DHPM (12 passes, 120 MPa), coupled or not to a cooling device, was applied to β-lactoglobulin (β-lg) and whey protein isolate (WPI) dispersions. Minor changes in the structure of whey proteins were induced by DHPM with sample cooling; although, when sample cooling was not applied, aggregation and increases of around 30% of protein surface hydrophobicity were noticeable for the WPI dispersion. The association constant between the proteins and lutein was in the magnitude of 10
    MeSH term(s) Food Handling ; Lactoglobulins/chemistry ; Lutein ; Pressure ; Whey Proteins
    Chemical Substances Lactoglobulins ; Whey Proteins ; Lutein (X72A60C9MT)
    Language English
    Publishing date 2022-02-02
    Publishing country England
    Document type Journal Article
    ZDB-ID 243123-3
    ISSN 1873-7072 ; 0308-8146
    ISSN (online) 1873-7072
    ISSN 0308-8146
    DOI 10.1016/j.foodchem.2022.132298
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Does the protein structure of β-lactoglobulin impact its complex coacervation with type a gelatin and the ability of the complexes to entrap lutein?

    Aya Rodriguez, Martin Daniel / Vidotto, Danilo C. / Xavier, Ana Augusta O. / Mantovani, Raphaela A. / Tavares, Guilherme M.

    Food Hydrocolloids. 2023 Mar. 03, p.108651-

    2023  , Page(s) 108651–

    Abstract: The heteroprotein complex coavervation (HPCC) is triggered by the interaction between oppositely charged proteins resulting in two liquid phases in equilibrium: the coacervate phase, which is rich in protein and the equilibrium solution which has low ... ...

    Abstract The heteroprotein complex coavervation (HPCC) is triggered by the interaction between oppositely charged proteins resulting in two liquid phases in equilibrium: the coacervate phase, which is rich in protein and the equilibrium solution which has low protein concentration. Several intrinsic and extrinsic factors affect the HPCC, including the nature and the conformational state of the involved proteins. In this work, the mechanism of complex coacervation between type A gelatin (GA) and native and thermal treated (70 °C/5 min) β-lactoglobulin (β-lg and β-lg (TT)) was investigated. In addition, the ability of the obtained complex coacervates to entrap lutein was evaluated. The applied thermal treatment led to an increase of about 20% in the concentration of surface free sulfhydryl groups and increased around 66% the surface hydrophobicity of β-lg (TT), compared with the untreated one. Nevertheless, minor impact was noticed in the aggregation state of the proteins, as well as in their ability to bind lutein (Ksv in the magnitude order of 10⁴ M⁻¹). The optimal condition for the complex coacervation between GA-β-lg and GA-β-lg (TT) was pH 6.5, minimal ionic strength and mass ratio of 2.5:1. Even if the applied thermal treatment did not promote important changes in the thermodynamic parameters of the molecular interaction between GA-β-lg (TT) compared with those for the molecular interaction between GA-β-lg, it negatively affected the coacervation yield (from 64% to 57% in the optical condition). Both obtained complex coacervates exhibited high lutein entrapment efficiency, demonstrating their potential for protecting and delivering this bioactive compound.
    Keywords bioactive compounds ; gelatin ; heat treatment ; hydrocolloids ; hydrophobicity ; ionic strength ; liquids ; lutein ; pH ; protein structure ; thermodynamics ; Complex coacervation ; Proteins ; Denaturation ; Encapsulation
    Language English
    Dates of publication 2023-0303
    Publishing place Elsevier Ltd
    Document type Article ; Online
    Note Pre-press version
    ZDB-ID 742742-6
    ISSN 1873-7137 ; 0268-005X
    ISSN (online) 1873-7137
    ISSN 0268-005X
    DOI 10.1016/j.foodhyd.2023.108651
    Database NAL-Catalogue (AGRICOLA)

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  3. Article ; Online: Lutein bioaccessibility in casein-stabilized emulsions is influenced by the free to acylated carotenoid ratio, but not by the casein aggregation state

    Mantovani, Raphaela A. / Xavier, Ana Augusta O. / Tavares, Guilherme M. / Mercadante, Adriana Z.

    Food Research International. 2022 Nov., v. 161 p.111778-

    2022  

    Abstract: Considering that carotenoids are found acylated to fatty acids in most edible fruits, the influence of the ratio of free to acylated lutein on the hydrolysis extent and bioaccessibility was evaluated by in vitro digestion. For this purpose, for the first ...

    Abstract Considering that carotenoids are found acylated to fatty acids in most edible fruits, the influence of the ratio of free to acylated lutein on the hydrolysis extent and bioaccessibility was evaluated by in vitro digestion. For this purpose, for the first time, esterified, free, or a mixture of both carotenoid forms was used in the lipid phase of emulsions stabilized by sodium caseinate (NaCas) and native phosphocaseinate (PPCN). Marigold petals was used as a source of lutein-rich extracts. The emulsions were characterized and the extent of ester hydrolysis, carotenoid recovery, and bioaccessibility were evaluated by LC-DAD-MS/MS. Besides low polydispersity, NaCas and PPCN stabilized emulsions exhibited a constant mean droplet diameter of about 260 and 330 nm, respectively, after 7 days. Caseins were completely digested after the gastric digestion step. Moreover, casein supramolecular structure did not significantly affect carotenoid bioaccessibility. Lutein was majorly found in its free form in all bioaccessible fractions. The carotenoid bioaccessibility increased from 3% to 40% by increasing the percentage of free carotenoids from 0.5 to 100% in the emulsions; but the carotenoid recovery and hydrolysis extent of lutein esters were not affected. In conclusion, emulsion-based systems for carotenoid delivery stabilized either by NaCas or PPCN provided similar carotenoid bioaccessibility. Furthermore, bioaccessibility was inversely dependent on the overall hydrophobicity of the carotenoid extract. Our results suggest that the low bioaccessibility of esterified carotenoids was a consequence of their limited hydrolysis extent. This study provides information that may help design emulsion-based systems stabilized by food protein as a vehicle for carotenoids.
    Keywords bioavailability ; casein ; digestion ; droplets ; esterification ; food research ; hydrolysis ; hydrophobicity ; lipids ; lutein ; sodium caseinate ; Carotenoid ; Native phosphocaseinate ; Emulsion ; In vitro digestion ; LC-MS ; Lutein ester hydrolysis
    Language English
    Dates of publication 2022-11
    Publishing place Elsevier Ltd
    Document type Article ; Online
    ZDB-ID 1111695-x
    ISSN 1873-7145 ; 0963-9969
    ISSN (online) 1873-7145
    ISSN 0963-9969
    DOI 10.1016/j.foodres.2022.111778
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

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  4. Article ; Online: High-pressure microfluidization of whey proteins: Impact on protein structure and ability to bind and protect lutein

    Vidotto, Danilo C. / Mantovani, Raphaela A. / Tavares, Guilherme M.

    Food Chemistry. 2022 July, v. 382 p.132298-

    2022  

    Abstract: Dynamic high-pressure homogenization microfluidization (DHPM) is a versatile emerging technology that may be applied to food processing to achieve several goals. DHPM may, depending on nature of the molecules and the working parameters, induce changes in ...

    Abstract Dynamic high-pressure homogenization microfluidization (DHPM) is a versatile emerging technology that may be applied to food processing to achieve several goals. DHPM may, depending on nature of the molecules and the working parameters, induce changes in protein structure, which may improve or impair their techno-functional properties and ability to bind other molecules. In this context, DHPM (12 passes, 120 MPa), coupled or not to a cooling device, was applied to β-lactoglobulin (β-lg) and whey protein isolate (WPI) dispersions. Minor changes in the structure of whey proteins were induced by DHPM with sample cooling; although, when sample cooling was not applied, aggregation and increases of around 30% of protein surface hydrophobicity were noticeable for the WPI dispersion. The association constant between the proteins and lutein was in the magnitude of 10⁴ M⁻¹, and lutein photodegradation constant diminished about 3 times in the presence of proteins, compared to in their absence.
    Keywords cooling ; food chemistry ; homogenization ; hydrophobicity ; lutein ; photolysis ; protein structure ; whey ; whey protein isolate ; Microfluidization ; Whey proteins ; Fluorescence quenching ; Photodegradation
    Language English
    Dates of publication 2022-07
    Publishing place Elsevier Ltd
    Document type Article ; Online
    ZDB-ID 243123-3
    ISSN 1873-7072 ; 0308-8146
    ISSN (online) 1873-7072
    ISSN 0308-8146
    DOI 10.1016/j.foodchem.2022.132298
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 3634: Show issues

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    Inter-library loan at ZB MED

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  5. Article ; Online: Lutein bioaccessibility in casein-stabilized emulsions is influenced by the free to acylated carotenoid ratio, but not by the casein aggregation state.

    Mantovani, Raphaela A / Xavier, Ana Augusta O / Tavares, Guilherme M / Mercadante, Adriana Z

    Food research international (Ottawa, Ont.)

    2022  Volume 161, Page(s) 111778

    Abstract: Considering that carotenoids are found acylated to fatty acids in most edible fruits, the influence of the ratio of free to acylated lutein on the hydrolysis extent and bioaccessibility was evaluated by in vitro digestion. For this purpose, for the first ...

    Abstract Considering that carotenoids are found acylated to fatty acids in most edible fruits, the influence of the ratio of free to acylated lutein on the hydrolysis extent and bioaccessibility was evaluated by in vitro digestion. For this purpose, for the first time, esterified, free, or a mixture of both carotenoid forms was used in the lipid phase of emulsions stabilized by sodium caseinate (NaCas) and native phosphocaseinate (PPCN). Marigold petals was used as a source of lutein-rich extracts. The emulsions were characterized and the extent of ester hydrolysis, carotenoid recovery, and bioaccessibility were evaluated by LC-DAD-MS/MS. Besides low polydispersity, NaCas and PPCN stabilized emulsions exhibited a constant mean droplet diameter of about 260 and 330 nm, respectively, after 7 days. Caseins were completely digested after the gastric digestion step. Moreover, casein supramolecular structure did not significantly affect carotenoid bioaccessibility. Lutein was majorly found in its free form in all bioaccessible fractions. The carotenoid bioaccessibility increased from 3% to 40% by increasing the percentage of free carotenoids from 0.5 to 100% in the emulsions; but the carotenoid recovery and hydrolysis extent of lutein esters were not affected. In conclusion, emulsion-based systems for carotenoid delivery stabilized either by NaCas or PPCN provided similar carotenoid bioaccessibility. Furthermore, bioaccessibility was inversely dependent on the overall hydrophobicity of the carotenoid extract. Our results suggest that the low bioaccessibility of esterified carotenoids was a consequence of their limited hydrolysis extent. This study provides information that may help design emulsion-based systems stabilized by food protein as a vehicle for carotenoids.
    MeSH term(s) Carotenoids/chemistry ; Caseins ; Emulsions/chemistry ; Esters ; Fatty Acids ; Lutein ; Plant Extracts/chemistry ; Tandem Mass Spectrometry
    Chemical Substances Caseins ; Emulsions ; Esters ; Fatty Acids ; Plant Extracts ; Carotenoids (36-88-4) ; Lutein (X72A60C9MT)
    Language English
    Publishing date 2022-08-19
    Publishing country Canada
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1111695-x
    ISSN 1873-7145 ; 0963-9969
    ISSN (online) 1873-7145
    ISSN 0963-9969
    DOI 10.1016/j.foodres.2022.111778
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Bonn / Germany

    Z 2972: Show issues

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  6. Article: Does the protein structure of Beta-lactoglobulin impact its complex coacervation with type A gelatin and the ability of the complexes to entrap lutein?

    Rodriguez, Martin Daniel Aya / Vidotto, Danilo C. / Xavier, Ana Augusta O. / Mantovani, Raphaela A. / Tavares, Guilherme M.

    Food hydrocolloids

    2023  Volume 140, Issue -, Page(s) 108651

    Language English
    Document type Article
    ZDB-ID 742742-6
    ISSN 0268-005X
    Database Current Contents Nutrition, Environment, Agriculture

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    In stock of ZB MED Bonn / Germany

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