Relation of β-Lactoglobulin – Sodium Polypectate Aggregation to Bulk Macromolecular Concentration |
| |
| Authors: | EMBOLA E. NDI B.G. SWANSON A.K. DUNKER L.O. LUEDECKE |
| |
| Affiliation: | Authors Ndi, Swanson, and Luedecke are with the Dept. of Food Science &Human Nutrition, and Author Dunker is with the Dept. of Biochemistry/Biophysics, Washington State Univ., Pullman, WA 99164-6376. |
| |
| Abstract: | Aggregation of β-Lactoglobulin β-Lg) solutions, with and without sodium polypectate (SPP), was investigated at pH 6.5 and 3.5 by turbidity measurements and gel permeation chromatography during heating at 1°C/min. The ratio of β-Lg:SPP was maintained at 10:1. At pH 6.5, the transition temperature of β-Lg aggregation decreased linearly with the logarithm of β-Lg concentration. Irrespective of β-Lg concentration, SPP did not affect the rate of β-Lg aggregation during heating at pH 6.5. However, SPP influenced the formation of high-molecular-weight (HMW) β-Lg aggregates during heating at pH 6.5 was related to bulk macromolecular concentration. No thermal aggregation transitions were detected for β-Lg solutions at pH 3.5. SPP interacted with β-Lg at pH 3.5 to form a complex that precipitated on heating. |
| |
| Keywords: | thermal aggregation β-lactoglobulin sodium polypectate transition temperature |
|
|
