Molecular characterization of β-lactoglobulin (βLG) gene in Indian buffalo (Bubalus bubalis)

The aim of the study was to characterized tha β-lactoglobulin gene and protein in indian buffalo. The β-lactoglobulin (Bu_βLG) is a major whey milk protein and cause an allergic reaction in infants and children. In the present study, the full open reading frame (ORF) of buffalo β-lactoglobulin (Bu_βLG) gene was characterized, which consisted of a 543 bp sequence with 180 amino acid residues. The phylogenetic tree showed that the cattle, yak, and buffalo βLG gene formed one cluster and buffalo is more closer (96%) to an exotic cow (Bos taurus). ProtParam analysis showed that Bu_βLG protein was acidic (pI, 4.93), thermo-tolerant, and hydrophobic. The Bu_βLG 3-D model was generated by I-TASSER, which revealed a more stabilized nature of the predicted structure. Further, the Ramachandran plot validated that the 3-D model of Bu_βLG protein, which was of good quality. The presence of four ligand-binding sites for retinoic acid, oleic acid, vitamin D3, and benziphenone in Bu_βLG suggests that this protein bind to several fatty acids and ions. IEDB analysis displayed the seven and six epitope sites in the Bu_βLG protein for B-cell and T-cell, respectively. Thus, the epitope sites in the βLG protein may have certain immunological roles, which can be used to reduce the allergenicity of βLG protein for improving the buffalo milk quality.