Fluorescence Study of Bovine ÃÂ²-Lactoglobulin
Jihad René Albani*
Laboratory of Molecular Biophysics, University of Science and Technology of Lille, Building C6, 59655 Villeneuve d’Ascq Cedex, France
- *Corresponding Author:
- Jihad René Albani
Laboratory of Molecular Biophysics
University of Science and Technology of Lille
Building C6, 59655 Villeneuve d’Ascq Cedex, France
E-mail: [email protected]
Received date: November 03, 2015; Accepted date: December 07, 2015; Published date: December 10, 2015
Citation: Albani JR (2015) Fluorescence Study of Bovine β-Lactoglobulin. Pharm Anal Acta 6:452. doi:10.4172/2153-2435.1000452
Copyright: © 2015 Albani JR. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
β-Lactoglobulin consists of a single polypeptide of 162 amino acid residues (Mr=18,400). Tertiary structure of β-lactoglobulin possesses a pocket (calyx) where hydrophobic ligands can easily bind. The protein normally exists as a dimer, each monomer having one free cysteine and two disulphide bridges. Quaternary structure of the protein varies with the pH. For example, at pH 2, β-lactoglobulin is in a molten globule state, stable although partially unfolded, and at pH 12 the protein is denatured. At some pH, mixtures of both monomeric and dimeric forms are found.