Premium
Stability of β‐lactoglobulin/micellar casein mixtures on heating in simulated milk ultrafiltrate at pH 6.0
Author(s) -
MOUNSEY JOHN S,
O’KENNEDY BRENDAN T
Publication year - 2009
Publication title -
international journal of dairy technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.061
H-Index - 53
eISSN - 1471-0307
pISSN - 1364-727X
DOI - 10.1111/j.1471-0307.2009.00522.x
Subject(s) - casein , chemistry , lactose , chromatography , beta lactoglobulin , whey protein , precipitation , heat stability , milk protein , food science , materials science , physics , meteorology , composite material
The stability of β‐lactoglobulin (β‐lg)/micellar casein (MC) mixtures was examined on heating at pH 6.0 in increasing levels of lactose‐free simulated milk ultrafiltrate (SMUF). Heated β‐lg associated with MC to form stable particles (up to 771 nm in size in SMUF × 0.5). Higher levels of SMUF induced reductions in the charge on particles, resulting in greater aggregation and precipitation. Results indicated that the nonthiol‐containing α s1 ‐ and β‐casein fractions showed greater interaction with β‐lg on heating than the thiol‐containing fractions (α s2 ‐casein and κ‐casein). Casein proteins and their fractions have potential application in the development of heat‐stable dairy‐based beverages.