Primary Information
BoMiProt ID	Bomi107
Protein Name	Beta-lactoglobulin
Organism	Bos taurus
Uniprot ID	P02754
Milk Fraction	Whey
Aminoacid Length	178
Molecular Weight	19883
FASTA Sequence	Download
Gene Name	LGB
Gene ID	280838
Protein Existence Status	Reviewed: Experimental evidence at protein level
Secondary Information
Endogenous/Bioactive peptides - Fragment - Sequence - Effect	ß-lactorphin - 102–105 - TLLF - Non-opioid ACE-inhibition Ref 142–148 - ALPMHIR - ACE-inhibition Ref lactotensin - 146–149 - HIRL - Ileum contraction, hypocholesterolemic activity Ref
Protein Function	Role in molecular transport or possibly some form of modulator; binds both fatty acids and retinol
Biochemical Properties	Initial denaturation of β-Lg led to the formation of small well defined clusters with a size independent to concentration, temperature and ionic strength; β-lactoglobulin dimers are resistant to boiling or denaturing and reducing conditions; potential lactosylation can occur in milk at an elevated temperature; increasing temperature up to 30°C the content of β- strands remains constant, decreases strongly between 30 and 40°C with approximately 8 to 10%, and decreases more gradually up to 22% at 95°C; α-helical content remains constant from 15 to 65°C and decreases to 7% at 75°C; the β-turn content remains constant throughout the temperature range
Significance in milk	Dominant bovine milk allergen;
PTMs	Disulfide bond formation
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation
SCOP	Class : All beta proteins Fold : Lipocalins Superfamily : Lipocalins Family : Retinol binding protein-like Domain Name : 1BEB A:5-160
CATH	Matched CATH superfamily 2.40.128.20
Predicted Disorder Regions	NA
DisProt Annotation
TM Helix Prediction	No TM helices
Significance of PTMs	Steric effects governing disulfide bond interchange during thermal aggregation in solutions of beta-lactoglobulin B and alpha-lactalbumin
PDB ID	1B0O, 1B8E, 1BEB, 1BSO, 1BSQ, 1BSY, 1CJ5, 1DV9, 1GX8, 1GX9, 1GXA, 1QG5, 1UZ2, 1YUP, 2AKQ, 2BLG, 2GJ5, 2Q2M, 2Q2P, 2Q39, 2R56, 3BLG, 3KZA, 3NPO, 3NQ3, 3NQ9, 3PH5, 3PH6, 3UEU, 3UEV, 3UEW, 3UEX, 4DQ3, 4DQ4, 4GNY, 4IB6, 4IB7, 4IB8, 4IB9, 4IBA, 4KII, 4LZU, 4LZV, 4Y0P, 4Y0Q, 4Y0R, 5EEE, 5HTD, 5HTE, 5IO5, 5IO7, 5K06, 5LKE, 5LKF, 5NUJ, 5NUK, 5NUM, 5NUN, 5Y5C, 6FXB, 6GE7, 6GF9, 6GFS, 6GHH, 6NKQ, 6QI6, 6QI7, 6QPD, 6QPE, 6RWP, 6RWQ, 6RWR, 6rys, 6ryt,
Bibliography	1. Duan, C., Li, A., Yang, L., Zhao, R., Fan, W., and Huo, G. (2014) Comparison of immunomodulating properties of Beta-lactoglobulin and its hydrolysates. Iran. J. Allergy. Asthma. Immunol. 13, 26–32. 2. de Jongh, H. H. J., Gröneveld, T., and de Groot, J. (2001) Mild Isolation Procedure Discloses New Protein Structural Properties of β-Lactoglobulin. J. Dairy Sci. 84, 562–571. 3. Prioult, G., Pecquet, S., and Fliss, I. (2005) Allergenicity of acidic peptides from bovine β-lactoglobulin is reduced by hydrolysis with Bifidobacterium lactis NCC362 enzymes. Int. Dairy J. 15, 439–448. 4. Kontopidis, G., Holt, C., and Sawyer, L. (2004) Invited Review: β-Lactoglobulin: Binding Properties, Structure, and Function. J. Dairy Sci. 87, 785–796. 5. Kontopidis, G., Holt, C., and Sawyer, L. (2002) The Ligand-binding Site of Bovine β-Lactoglobulin: Evidence for a Function? J. Mol. Biol. 318, 1043–1055. 6. Fogliano, V., Monti, S. M., Visconti, A., Randazzo, G., Facchiano, A. M., Colonna, G., and Ritieni, A. (1998) Identification of a beta-lactoglobulin lactosylation site. Biochim. Biophys. Acta 1388, 295–304. 7. Morgan, F., Léonil, J., Mollé, D., and Bouhallab, S. (1997) Nonenzymatic lactosylation of bovine beta-lactoglobulin under mild heat treatment leads to structural heterogeneity of the glycoforms. Biochem. Biophys. Res. Commun. 236, 413–417. 8.Livney YD, Verespej E, Dalgleish DG. Steric effects governing disulfide bond interchange during thermal aggregation in solutions of beta-lactoglobulin B and alpha-lactalbumin. J Agric Food Chem. 2003 Dec 31;51(27):8098-106. doi: 10.1021/jf034582q. PMID: 14690403.