Study of the stability of egg white protein-based foams: effect of heating protein solution

Hagolle, N.; Relkin, Perla; Popineau, Yves; Bertrand, Dominique

doi:10.1002/1097-0010(200006)80:8<1245::aid-jsfa631>3.0.co;2-4

Cited by 43 publications

(38 citation statements)

References 20 publications

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“…In earlier studies, it was shown that controlled mild heat treatment of globular proteins in controlled physico-chemical conditions can decrease their resistance to heat denaturation, with positive effects on their surface activity and stabilisation of protein-based foams [11,13,23]. In this work, we observed that despite a slight decrease in protein solubility and formation of a low proportion of covalentlybound aggregates, the decrease in whey proteins' conformational stability was accompanied by enhancement of their ability to stabilise foams.…”

Section: Resultsmentioning

confidence: 93%

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Production of whey protein aggregates with controlled end-use properties

Relkin¹,

Bernard²,

Meylheuc³

et al. 2007

Lait

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-We studied the structural behaviour and foaming properties of whey proteins under the effects of spray-drying in a co-current configuration. We used two different inlet/outlet air temperatures (170/85• C or 260/138• C, respectively), the other operating conditions being unchanged. Using different characterisation techniques, we showed that both whey proteins (WP-P 85 and WP-P 138 ) which were submitted to hydro-thermal treatments under mild and high air processing conditions behaved differently from untreated proteins (WP-L). As expected, WP-P 138 powder exhibited lower moisture and free lactose contents, a higher particle internal porosity, and a thinner particle wall thickness than the WP-P 85 powder. The conformational stability of whey proteins, obtained by dilution of untreated whey proteins (WP-L) and dispersions of the two spray-dried powders (WP-P 85 and WP-P 138 ), were compared. Whey proteins in the WP-P 138 powder showed a red-shift in the tryptophan emission wavelength, the appearance of a newly created fluorescent compound at 420 nm, contrary to untreated and WP-P 85 whey proteins. In addition, we observed formation of a higher proportion of covalently-bound aggregates (11% in WP-P 138 , instead of 5% in WP-P 85 ) and a decrease in conformational stability against re-heating (∼50% s in WP-P 138 , instead of ∼30% in WP-P 85 ) compared with untreated WP-L solution. Finally, combination of continuous measurements of foam volume (by an on-line video camera) and liquid (by conductivity) entrained in a column foam during its formation by air injection, in parallel with automatic acquisition of videofoam images during the destabilisation step, showed that solution of WP-P 138 spray-dried powder, obtained using the highest air temperature conditions, has higher foaming properties than WP-P 85 and WP-L solutions. • C et 260/138• C, respectivement), les autres conditions opératoires étant inchangées. Par application de différentes techniques de caractérisa-tion, nous avons montré que les protéines (WP-P 85 et WP-P 138 ) qui ont subi des traitements hydrothermiques à température d'air modérée et sévère, respectivement, se comportent différemment des protéines (WP-L) contenues dans les solutions avant séchage. Comme attendu, la poudre contenant les protéines WP-P 138 présente des taux d'humidité et de lactose libre plus faibles, un taux de porosité interne plus important, et une épaisseur de paroi plus faible. L'étude spectrofluorimétrique des protéines, contenues dans des dispersions dans l'eau distillée des poudres issues des deux conditions de séchage, indique que pour les protéines WP-P 138 , et contrairement aux protéines WP-L et WP-P 85 , la longueur d'onde maximum d'émission de fluorescence du tryptophane présente un déplacement vers le rouge, ainsi que l'apparition de nouveaux composés qui fluorescent avec une longueur d'onde maximum d'émission à 420 nm. D'autre part, nous avons observé une plus forte proportion d'agrégats covalents (11 % pour WP-P 138 au lieu de 5 % pour WP-P 85 ), ainsi qu'...

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Section: Resultsmentioning

confidence: 93%

“…Foaming properties of whey protein solutions were characterised using a foam analyser based on conductimetric measurements [10,11,13,23]. The foam was generated by sparging air (15 mL·min −1 ) into an initial volume of protein solution (12 mL) through a metallic porous disk (a sintered metal frit of 2 μm pore size).…”

Section: Foaming Propertiesmentioning

confidence: 99%

Production of whey protein aggregates with controlled end-use properties

Relkin¹,

Bernard²,

Meylheuc³

et al. 2007

Lait

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“…La primera técnica está basada en la textura aparente de la espuma. Un estudio sobre la estabilidad de espumas mediante la caracterización de textura fue realizado por Hagolle et al (2000). La caracterización de textura utiliza la transformada de Haar, según se presenta en los trabajos de Bertrand et al (1992).…”

Section: Procesamiento De Imágenesunclassified

“…Por el momento, los estudios se han centrado en la comprensión y el desarrollo de técnicas analíticas adecuadas para estos productos (Guillerme et al, 1993;Hagolle et al, 2000) pero la capacidad de interpretar sus mediciones en términos SOMENTA CIENCIA Y TECNOLOGÍA ALIMENTARIA Sociedad Mexicana de Nutrición y Tecnología de los Alimentos ISSN 1135-8122 ©2006 SOMENTA 148 del comportamiento de las burbujas y de su relación con la estructura del producto y su calidad están aún fuera del alcance de los tecnólogos en alimentos. Generalmente, los estudios realizados en burbujas se han dedicado a la caracterización básica de las propiedades físicas del proceso de espumado como el volumen, la densidad y el drenado (Relkin et al, 1999).…”

Section: Introductionunclassified

Cuantificación De La Persistencia Y Homogeneidad De Espumas Mediante Procesamiento De Imágenes Quantification of Foam's Stability and Homogeneity by Image Processing

Castillo-Castañeda

Courtois

Relkin

2006

Ciencia y Tecnologia Alimentaria

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“…Denatured proteins are characterised by less high-ordered structures, less initially buried amino-acid groups in the protein core, and a greater exposure to the solvent environment of hydrophobic and sulphydryl (SH) groups than proteins in their initial structure [10,14,27,33,35,36]. On the other hand, it is well established that due to their amphiphilic (polar/non-polar) nature and marginal conformational stability, whey proteins may adsorb from aqueous solutions to solid surfaces and fluid/fluid interfaces and act as surfactants by reducing the interfacial tension and forming a cohesive film [9,15,16,19,23,35]. For some time, efforts have been made to develop standardised methods to differentiate between stable and unstable surfactantand/or protein-based foams [17,30,42].…”

Section: Introductionmentioning

confidence: 99%

Enhancement of protein structure-forming properties in liquid foams by spray drying

Bernard

Broyart

Vasseur

et al. 2008

Dairy Sci. Technol.

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-In the first part of this study we used mathematical modelling for prediction of hydrothermal pathways (time evolution of temperature and water content) of a whey protein-rich product during its spray drying in a co-current configuration. The model was validated through drying assays, where the inlet/outlet air temperatures were fixed at 170/85• C, 217/107• C, 247/125• C or 260/138• C, the other spray-drying operation variables being unchanged. Then, the spray-dried powders were characterised before and after re-hydration for evaluation of a threshold air operating temperature value leading to changes in protein structure-functionality, in comparison with the nonspray-dried protein solution (WP-L). The predicted hydro-thermal pathways of the whey proteinrich product during its spray drying indicated that all of the operation variables used were accompanied by a product wet bulb temperature value lower than 60• C. However, the resulting powders presented different internal porosity and wall thickness, and the protein solutions obtained after the powders' re-hydration behaved differently from the non-spray-dried protein solution (WP-L). Particularly, it seemed that powders obtained at outlet air temperature and water content higher than 100• C and lower than 4%, respectively, presented a higher internal porosity and lower free lactose content. Furthermore, they were accompanied by lower protein solubility and conformation stability and by a slight development of hydroxymethylfurfural and covalently-bound protein aggregates. In addition, in situ evaluation of foam formation and stability after air injection into the re-hydrated powders showed that increasing spray-drying air temperatures led to powders with more and more enhanced foaming properties, relative to the whey protein-rich solution before spray drying. The powder characteristics obtained in the present study, added to those recently published [Relkin et al., Lait 87 (2007) 337-348] are presented and discussed in regards to effects of spray-drying operation variables on protein structural changes and enhancement of foaming properties without additional processing equipment. • C (les autres paramètres d'opération de séchage étant maintenus constants), nous avons caractérisé les poudres obtenues avant et après ré-hydratation. Nous avons observé que pour toutes les conditions opératoires testées, la température de thermomètre humide reste inférieure à 60• C, pendant une durée diminuant de 10 à 5 s pour une température de sortie d'air (produit) variant de 85• C (59. Cependant, les poudres sortant à une température supérieure à 100• C et un taux d'humidité inférieur à 4 %, semblent subir une montée en température beaucoup plus brutale après un palier à 60• C (température de thermomètre humide) d'une durée inférieure à 7 s. Ces poudres présentent une porosité interne qui augmente ( 40 %) et une épaisseur de paroi (visualisée par microscopie électronique à balayage) qui semble diminuer avec l'intensité du traitement thermique. Les solutions protéiques...

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Study of the stability of egg white protein-based foams: effect of heating protein solution

Cited by 43 publications

References 20 publications

Production of whey protein aggregates with controlled end-use properties

Production of whey protein aggregates with controlled end-use properties

Cuantificación De La Persistencia Y Homogeneidad De Espumas Mediante Procesamiento De Imágenes Quantification of Foam's Stability and Homogeneity by Image Processing

Enhancement of protein structure-forming properties in liquid foams by spray drying

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