Search by BoMiProt ID - Bomi107

Primary Information

BoMiProt ID Bomi107
Protein Name Beta-lactoglobulin
Organism Bos taurus
Uniprot IDP02754
Milk FractionWhey
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,
SCOP Class : All beta proteins
Fold : Lipocalins
Superfamily : Lipocalins
Family : Retinol binding protein-like
Domain Name : 1BEB A:5-160

CATH Matched CATH superfamily
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.