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Ultrastructure of o/w emulsions stabilized by faba bean protein isolates

✍ Scribed by Krause, J.-P. ;Buchheim, W.


Publisher
John Wiley and Sons
Year
1994
Tongue
English
Weight
749 KB
Volume
38
Category
Article
ISSN
0027-769X

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✦ Synopsis


An ultrastructural comparison is given for dispersions of a protein isolate (FBPI) from faba beans (Viciu fubu L.) and its highly acetylated derivative (AFBPI) as well as for various o/w emulsions stabilized by FBPI and AFBPI. Both protein isolates contain substantial amounts of surface-active phospholipids (about 3%) which occur as vesicles (diameter 30 . . . 500 nm). Their membranes and cores contain protein. Interfacial protein layers of Triolein/Water-emulsion droplets possess smooth external surfaces and rather coarse internal surfaces with peculiar paracrystalline structured areas. Tangible differences are found in the droplet-size distribution and ultrastructure of sunflower-oil/water emulsions due to both the homogenization process (high pressure homogenizer or ultrasonic disintegrator) and the acetylation of the isolate. The modification by acetylation increases the emulsifying activity of the isolate and prevents the strong aggregation of oil droplets observed in FBPI-stabilized emulsions.

Zusammenfassung

Ultrastruktur von O/W-Emulsionen stabilisiert durch Proteinisolate der Ackerbohne

Ergebnisse vergleichender Untersuchungen der Ultrastruktur von Dispersionen aus einem nichtmodifizierten Proteinisolat (FBPI) und einem hochacetylierten Derivat (AFBPI) der Ackerbohne (Viciu fubu L.) sowie damit stabilisierter Emulsionen werden vorgestellt. Die in den Isolaten enthaltenen grenzflachenaktiven Phospholipide (ca. 3%) bilden im waBrigen Medium Vesikel mit Durchmessern zwischen 30 und 500 nm. Ihre Membranen und Kerne enthalten Protein. Die proteinstabilisierten Grenzfllchen von Triolein/Wasser-Emulsionen haben glatte AuBen-und rauhe Innenseiten mit zum Teil parakristallinen Bereichen. Unterschiedliche Homogenisierverfahren (Hochdruck und Ultraschall) als auch die Acetylierung des Proteinisolates fuhren zu deutlichen Unterschieden in der Tropfchen-groBen-Verteilung und in der Ultrastruktur von Sonnenblumenol in Wasser Emulsionen. Das acetylierte Isolate besitzt eine deutlich hohere Emulgieraktivitat und verhindert die in FBPIstabilisierten Emulsionen beobachtete starke Flockung der Tropfchen.


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