Ca2+-Induced Cold-Set Gelation of Whey Protein Isolate Fibrils
نویسندگان
چکیده
In this paper we describe the rheological behaviour of Ca2+-induced cold-set gels of whey protein mixtures. Coldset gels are important applications for products with a low thermal stability. In previous work [1], we determined the state diagram for whey protein mixtures that were heated for 10 h at pH 2 at 80°C. Under these conditions, the major whey protein, b-lactoglobulin (b-lg), forms fibrils. When whey protein mixtures are heated at protein concentrations in the liquid solution regime of the state diagram, cold-set gels can be formed by adding Ca2+ ions at pH 7. We studied the rheological behaviour of cold-set gels for various sample compositions for whey protein mixtures. When keeping the total whey protein concentration constant, the elastic modulus, G’, for the cold-set gels decreased for increasing a-lactalbumin and bovine serum albumin ratios, because less material (blg fibrils) was available to form a gel network. In the cold-set gels the interactions between the b-lg fibrils induced by the calcium ions are dominant. The b-lg fibrils are forming the cold-set gel network and therefore determine the gel strength. a-Lactalbumin and bovine serum albumin are not incorporated in the stress-bearing structure of the gels. Zusammenfassung: In diesem Artikel wird das rheologische Verhalten von Ca2+-induzierten, kaltgehärteten Gelen aus Mischungen von Molke-Protein beschrieben. Kaltgehärtete Gele sind wichtige Anwendungen für Produkte mit einer geringen thermischen Stabilität. Schon in früheren Arbeiten wurde von uns das Zustandsdiagramm von Molke-Protein-Mischungen, die für 10 Stunden bei einem pH 2 auf 80°C erhitzt wurden, erstellt [1]. Unter diesen Bedingungen formt das häufigste und daher wichtigste Molke-Protein, b-Lactoglobulin (b-lg), Fibrillen. Die flüssige Phase des Zustandsdiagramms von Molke-Protein kann, bei einem pH-Wert von 7, durch Erhitzten und Zugabe von Ca2+-Ionen kaltgehärtete Gele bilden. Dies wird für verschiedene Mischungen von Molke-Proteinen untersucht. Bei gleich bleibender totaler Proteinkonzentration und bei steigendem a-Lactalbumin Gehalt und Bovin Serum Albumin Gehalt wird der elastische Modul für kaltgehärtete-Gele kleiner, da weniger Material (b-Lactoglobulin Fibrillen) zur Formung eines Gelnetzwerkes vorhanden ist. In kaltgehärteten Gelen sind die durch Kalziumionen induzierten Wechselwirkungen zwischen den b-lg Fibrillen dominant. Die b-lg Fibrillen formen das kaltgehärtete Gel-Netzwerk und bestimmen daher die Gelstärke. a-Lactalbumin und BSA wurden nicht in diese Strukturen eingebaut. Résumé: Dans cet article, nous décrivons le comportement rhéologique de gels formés à partir de mixtures de protéines du petit lait, et induits à froid par l’addition de Ca2+. Les gels formés à froid sont utilisés de façon importante dans les produits montrant une faible stabilité thermique. Dans un travail précédent [1], nous avons déterminé le diagramme de phase pour les mixtures de petit lait qui ont été chauffées durant 10 heures à 80°C et à pH 2. Sous ces conditions, la protéine majoritaire, la b-lactoglobuline (b-lg), forme des fibrilles. Quand les mixtures sont chauffées avec des concentrations en protéines correspondant au régime de solution liquide du diagramme de phase, des gels peuvent être formés à froid par addition d’ions Ca2+ à pH 7. Nous avons étudié le comportement rhéologique des gels formés à froid pour des échantillons comprenant des compositions variées de mixtures de protéines. Lorsque la concentration totale en protéines est maintenue constante, le module élastique G’ des gels formés à froid décroît avec l’augmentation des ratios de a-lactalbumine et de d’albumine de sérum bovin, parce que moins de matériau (fibrilles de b-lg) est disponible pour former un réseau de gel. Dans les gels formés à froid, les interactions entre les fibrilles de b-lg forment le réseau du gel et donc déterminent la rigidité du gel. L’a-lactalbumine et l’albumine de sérum bovin ne sont pas incorporées dans la structure du gel qui supporte la contrainte.
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