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Characterization and Comparison of Beta‐Lactoglobulin Orthologs
Author(s) -
Crowther Jennifer,
Jameson Geoffrey,
Hodgkinson Alison,
Dobson Renwick
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.895.13
Subject(s) - whey protein , beta lactoglobulin , dimer , ruminant , cow milk , function (biology) , chemistry , food science , characterization (materials science) , bovine milk , biology , biophysics , biochemistry , crystallography , microbiology and biotechnology , materials science , nanotechnology , pasture , ecology , organic chemistry
Beta‐lactoglobulin (Blg) is the most abundant whey protein in the milk of ruminant animals, yet its physiological function is yet to be confirmed. It is not present in human milk and has been identified as one of the main immunogenic proteins in cow milk. Goat milk appears to be less allergenic and more easily digested than cow milk. As Blg is the most abundant whey protein differences in its structural, physicochemical and dynamic properties may be responsible for some of the differences seen between these milks. An ultra‐high resolution crystal structure of caprine Blg, along with sedimentation velocity and small‐angle X‐ray scattering data, suggest the presence of subtle differences between bovine and caprine orthologs. While both are dimeric in solution and crystalline states, our data suggest a flexible arrangement of subunits within the dimer. These structural findings have directed further studies into the stability and dynamics of the protein and their binding behaviors with other components in milk, which may provide insight into the differences between these species' milks and potentially the physiological role of this enigmatic protein.