Invited Review: β-Lactoglobulin: Binding Properties, Structure, and Function
نویسندگان
چکیده
منابع مشابه
Structure of bovine β-lactoglobulin-lactoferrin coacervates.
Lactoferrin (LF) and β-lactoglobulin (BLG) are among the protein pairs that exhibit heteroprotein coacervation, a unique and relatively unexamined type of liquid-liquid phase separation (LLPS). In prior work we found that LF and BLG undergo coacervation at highly constrained conditions of pH, ionic strength and protein stoichiometry. The molar stoichiometry in coacervate and supernatant is LF :...
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Ligand-binding properties of β-lactoglobulin (β-lg) are well documented, but the subsequent biological functions are still unclear. Focusing on fatty acids/β-lg complexes, the structure-function relationships are reviewed in the light of the structural state of the protein (native versus non-native aggregated proteins). After a brief description of β-lg native structure, the review takes an int...
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We have determined bulk rheology of β-lactoglobulin (BLG) foams and surface viscoelasticity of corresponding protein solutions by varying pH as well as type, valency and concentration of the added salt in a wide range. Foam rheology was characterized by the storage modulus G0, the apparent yield stress τy, and the critical strain γc,foam defining the cessation of the linear viscoelastic respons...
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Irregularities are inherent to virtually all fibers, including the conventional textile fibers, the high-performance brittle fibers and newly developed nano-fibers. These irregularities can fall into two main categories: dimensional or geometrical irregularity (external) and structural irregularity (internal). For natural fibers such as wool, diameter variation along fiber length is atypical ex...
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ژورنال
عنوان ژورنال: Journal of Dairy Science
سال: 2004
ISSN: 0022-0302
DOI: 10.3168/jds.s0022-0302(04)73222-1