Premium
Interactions of (β‐Lactoglobulin and High‐methoxyl Pectins in Acidified Systems
Author(s) -
Kazmierski M.,
Wicker L.,
Corredig M.
Publication year - 2003
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.2003.tb12312.x
Subject(s) - pectin , chemistry , pectinesterase , mixing (physics) , chromatography , food science , pectinase , biochemistry , enzyme , physics , quantum mechanics
The interactions that occur when β‐lactoglobulin (β‐lg) is mixed with a high‐methoxyl pectin (HMP) and a modified pectin (mHMP, modified using plant pectinesterase) were examined at pH 3.8. Whereas soluble aggregates formed in β‐lg‐HMP, β‐lg‐mHMP precipitated upon mixing. β‐lg‐HMP mixtures showed soluble aggregates with larger hydrodynamic diameters when heated at 65°C than when heated at 90°C. β‐lg‐HMP mixtures adjusted to pH 6.0 after heating showed that the aggregates formed at 65°C could be dissociated, but the complexes were not reversible after heating at 90°C. A similar effect also was observed when resuspending the°‐lg‐mHMP precipitates at pH 6.0. The behavior of the 2 pectins was attributed to their differences in charge distribution.