Hydrophobicity of Whey Protein Concentrates Measured by Fluorescence Quenching and Its Relation with Surface Functional Properties

Moro, Andrea; Gatti, Carlos A.; Delorenzi, Néstor J.

doi:10.1021/jf001132e

Cited by 131 publications

(85 citation statements)

References 26 publications

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“…Tryptophan residues are particularly valuable probes since the indole ring is very sensitive to its environment and there are often a limited number of tryptophan residues in a given protein. Extrinsic fluorescence materials, including hydrophobicity probes such as ANS, have been successfully used to determine the surface hydrophobicity of whey proteins (Moro et al 2001;Liu et al 2005). With extrinsic fluorescence, the probes undergo changes in one or more fluorescence properties as a result of noncovalent interaction with proteins (Semisotnov et al 1991).…”

Section: Introductionmentioning

confidence: 99%

Pulsed Electric Field-Induced Structural Modification of Whey Protein Isolate

Xiang

Ngadi

Ochoa-Martínez

et al. 2009

Food Bioprocess Technol

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Effects of pulsed electric fields (PEF) on structural modification and surface hydrophobicity were assessed for whey protein isolate (WPI) of protein concentrations (3% and 5%) using fluorescence spectroscopy. The effects of a factorial combination of electric field intensities (12, 16, and 20 kV cm −1 ) and number of pulses (10, 20, and 30) on the intrinsic tryptophan fluorescence intensity, extrinsic fluorescence intensity, and surface hydrophobicity of WPI were evaluated. PEF treatments of WPI resulted in increases in the intrinsic tryptophan fluorescence intensity and led to 2-4-nm red shifts in emission wavelengths, indicating changes in the polarity of tryptophan residues microenvironment in whey proteins from a less polar to a more polar environment. The extrinsic fluorescence intensity of WPI increased with PEF treatments, but with 2-4-nm blue shifts, indicating partial denaturation of WPI fractions and exposure of more hydrophobic regions under these PEF treatments. Thus, under the conditions studied, PEF treatments of WPI yielded increases in surface hydrophobicity. The study confirmed that PEF treatments resulted in whey protein structure modifications. These results suggested that controlled PEF could be applied to process liquids food including WPI ingredients and modify their structure and function in order to get desired food products.

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Section: Introductionmentioning

confidence: 99%

Pulsed Electric Field-Induced Structural Modification of Whey Protein Isolate

Xiang

Ngadi

Ochoa-Martínez

et al. 2009

Food Bioprocess Technol

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“…3). An increase in the surface hydrophobicity of β-lg indicates that more hydrophobic residues present in the inside of native structure of β-lg are exposed to aqueous environment during heat treatments since the hydrophobic residues on the protein surface can be attached by a fluorescence probe, ANS (Moro et al, 2001). Therefore, heat treatment from 60 to 70 o C resulted in a partial denaturation of β-lg, which could lead to enhancing the surface hydrophobicity of β-lg.…”

Section: Resultsmentioning

confidence: 99%

Production and Characterization of Beta-lactoglobulin/Alginate Nanoemulsion Containing Coenzyme Q₁₀: Impact of Heat Treatment and Alginate Concentrate

Lee¹,

Choi²,

Ha³

et al. 2013

Korean Journal for Food Science of Animal Resources

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The aims of this research were to produce oil-in-water β-lactoglobulin/alginate (β-lg/Al) nanoemulsions loaded with coenzyme Q 10 and to investigate the combined effects of heating temperature and alginate concentration on the physicochemical properties and encapsulation efficiency of β-lg/Al nanoemulsions. In β-lg/Al nanoemulsions production, various heating temperatures (60, 65, and 70 o C) and alginate concentrations (0, 0.01, 0.03, and 0.05%) were used. A transmission electron microscopy was used to observe morphologies of β-lg/Al nanoemulsions. Droplet size and zeta-potential values of β-lg/Al nanoemulsions and encapsulation efficiency of coenzyme Q 10 were determined by electrophoretic light scattering spectrophotometer and HPLC, respectively. The spherically shaped β-lg/Al nanoemulsions with the size of 169 to 220 nm were successfully formed. The heat treatments from 60 to 70 o C resulted in a significant (p<0.05) increase in droplet size, polydispersity, zeta-potential value of β-lg/Al nanoemulsions, and encapsulation efficiency of coenzyme Q 10 . As alginate concentration was increased from 0 to 0.05%, there was an increase in the polydispersity index of β-lg/Al nanoemulsions and encapsulation efficiency of coenzyme Q 10 . This study demonstrates that heating temperature and alginate concentration had a major impact on the size, polydispersity, zeta-potential value and encapsulation efficiency of coenzyme Q 10 in β-lg/ Al nanoemulsions.

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“…Por otra parte, el hecho de que no se observa diferencia en la extinción de la fluorescencia de la β-lg con acrilamida en ausencia y presencia de los PF indicaría que los PF se unirían a un sitio distinto al del bolsillo hidrofóbico sin producir cambios conformacionales evidentes (Moro, et al, 2001). Contrariamente, Kanakis et al (2011), quienes estudiaron la interacción de β-lg con PF del té, observaron que estos se unen débilmente a la proteína en solución por interacciones hidrofóbicas e hidrofílicas, produciendo notables cambios conformacionales.…”

Section: Discusión Y Conclusiónunclassified

Formación de nanocomplejos entre polifenoles de cáscaras de manzanas y beta-lactoglobulina para su potencial aplicación en alimentos funcionales

Llopart

Busti

Verdini

et al. 2018

INNOTEC

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ResumenLos polifenoles (PF) ejercen una importante influencia sobre la salud humana, principalmente por su capacidad antioxidante. Las manzanas poseen PF principalmente en su cáscara. La proteína mayoritaria del lactosuero, la beta-lactoglobulina (β-lg), puede unir compuestos anfifílicos, como PF, protegiéndolos de agentes externos. Se estudió la posibilidad de vehiculizar PF de cáscara de manzanas rojas (Red Delicious), formando nanocomplejos (NC) con β-lg. El contenido de PF de cáscara de manzana roja ensayada fue de 266 ± 2 mg AG/100 g. Por ultrafiltración se determinó que el 57% formó NC con β-lg. Por medidas de extinción de la fluorescencia de los PF sobre β-lg se confirmó la formación de un complejo estático entre PF y β-lg. Las experiencias de extinción de la fluorescencia con acrilamida no mostraron diferencia significativa ante la presencia de PF, indicando que los PF se unen a un sitio distinto al del bolsillo hidrofóbico de la proteína. El tamaño de partícula y el potencial ζ de β-lg no se modificaron por agregado de PF. Se observó que la mayor parte de los PF forman NC con β-lg. Son necesarios más estudios para caracterizar el complejo con la finalidad de utilizarlo para enriquecer alimentos. Palabras clave: Polifenoles, cáscaras de manzanas, beta-lactoglobulina, nanocomplejos. AbstractPolyphenols (PF) exert an important influence on human health, mainly due to their antioxidant capacity. Apples have PF mainly in their peel. The major whey protein, beta-lactoglobulin (β-lg), can bind amphiphilic compounds, such as PF, protecting them from the action of external agents. In this work, nanocomplexes (NC) of PF extracted from red apple peel (Red Delicious), and β-lg were studied. By ultrafiltration it was determined that 57% of the PF added bound to the protein. Fluorescence extinction of β-lg by PF addition performed at different temperatures confirmed the formation of a static complex. The fluorescence extinction of β-lg with acrylamide did not vary significantly in the presence of PF, indicating that PF bound to a site different from the hydrophobic pocket of the protein. Particle size and ζ potential measurements of β-lg were not significantly modified by the addition of PF. This fact pointed to a low number of PF bounded to the dimer of the protein. In conclusion, NC would allow PF vehiculization, their protection and use for enrichment functional foods.

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Hydrophobicity of Whey Protein Concentrates Measured by Fluorescence Quenching and Its Relation with Surface Functional Properties

Cited by 131 publications

References 26 publications

Pulsed Electric Field-Induced Structural Modification of Whey Protein Isolate

Pulsed Electric Field-Induced Structural Modification of Whey Protein Isolate

Production and Characterization of Beta-lactoglobulin/Alginate Nanoemulsion Containing Coenzyme Q₁₀: Impact of Heat Treatment and Alginate Concentrate

Formación de nanocomplejos entre polifenoles de cáscaras de manzanas y beta-lactoglobulina para su potencial aplicación en alimentos funcionales

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Hydrophobicity of Whey Protein Concentrates Measured by Fluorescence Quenching and Its Relation with Surface Functional Properties

Cited by 131 publications

References 26 publications

Pulsed Electric Field-Induced Structural Modification of Whey Protein Isolate

Pulsed Electric Field-Induced Structural Modification of Whey Protein Isolate

Production and Characterization of Beta-lactoglobulin/Alginate Nanoemulsion Containing Coenzyme Q10: Impact of Heat Treatment and Alginate Concentrate

Formación de nanocomplejos entre polifenoles de cáscaras de manzanas y beta-lactoglobulina para su potencial aplicación en alimentos funcionales

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Product

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Production and Characterization of Beta-lactoglobulin/Alginate Nanoemulsion Containing Coenzyme Q₁₀: Impact of Heat Treatment and Alginate Concentrate