Alkali cold gelation of whey proteins. Part I : sol-gel-sol(-gel) transitions

The cold gelation of preheated whey protein isolate (WPI) solutions at alkaline conditions (pH>10) has been studied to better understand the effect of NaOH in the formation and destruction of whey protein aggregates and gels. Oscillatory rheology has been used to follow the gelation process, resu...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 25(2009), 10 vom: 19. Mai, Seite 5785-92
1. Verfasser: Mercadé-Prieto, Ruben (VerfasserIn)
Weitere Verfasser: Gunasekaran, Sundaram
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2009
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Gels Milk Proteins Whey Proteins Sodium Hydroxide 55X04QC32I Gold 7440-57-5
Beschreibung
Zusammenfassung:The cold gelation of preheated whey protein isolate (WPI) solutions at alkaline conditions (pH>10) has been studied to better understand the effect of NaOH in the formation and destruction of whey protein aggregates and gels. Oscillatory rheology has been used to follow the gelation process, resulting in novel and different gelation profiles with the gelation pH. At low alkaline pH, typical sol-gel transitions are observed, as in many other biopolymers. At pH>11.5, the system gels quickly, after approximately 300 s, followed by a slow degelation step that transforms the gel to a viscous solution. Finally, there is a second gelation step. This results in a surprising sol-gel-sol-gel transition in time at constant gelation conditions. At very high pH (>12.5), the degelation step is very severe, and the second gelation step is not observed, resulting in a sol-gel-sol transition. The first quick gelation step is related to the quick swelling of the WPI aggregates in alkali, as observed from light scattering, which enables the formation of new noncovalent interactions to form a gel network. These interactions are argued to be destroyed in the subsequent degelation step. Disulfide cross-linking is observed only in the second gelation step, not in the first step
Beschreibung:Date Completed 23.07.2009
Date Revised 19.11.2015
published: Print
Citation Status MEDLINE
ISSN:1520-5827
DOI:10.1021/la804093d