Title of article :
Kinetic study of β-lactoglobulin thermal aggregation at low pH Original Research Article
Author/Authors :
P. Mudgal، نويسنده , , C.R. Daubert، نويسنده , , E.A. Foegeding، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2011
Pages :
7
From page :
159
To page :
165
Abstract :
Kinetics of β-lactoglobulin (β-lg) thermal aggregation at pH 3.35, 85 °C, and 2–8% w/w protein concentration was studied using high performance liquid chromatography (HPLC) coupled with multi-angle laser light scattering (MALS) and rheology. Rate of β-lg aggregation was found to be of first order with respect to the initial protein concentration, and the conversion of native-like β-lg monomers/dimers (<36 kDa) to aggregates increased with initial concentration and heating times. The size of the aggregates formed during heating was dependent on the initial protein concentration. A simple nucleation and growth model was described for the β-lg aggregation at pH 3.35, where nucleation was found to be a rate limiting step below the previously identified critical concentration, Cc ∼ 6.4% protein. Above the Cc, nucleation occurred quickly and was not rate limiting. Critical size of the nucleus varied with protein concentration, with larger critical size needed at lower protein concentrations.
Keywords :
Low pH , ?-Lactoglobulin , kinetics , aggregation , Model , Nucleation
Journal title :
Journal of Food Engineering
Serial Year :
2011
Journal title :
Journal of Food Engineering
Record number :
1169188
Link To Document :
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