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Key Documents

L8005

Sigma-Aldrich

β-Lactoglobulin B from bovine milk

≥90% (PAGE)

Sinónimos:

β-LG, Bos d 5, beta-LG

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About This Item

Número de CAS:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.61

biological source

bovine milk

Quality Level

assay

≥90% (PAGE)

form

powder

mol wt

18,276 Da by calculation

technique(s)

HPLC: suitable
electrophoresis: suitable

UniProt accession no.

storage temp.

2-8°C

Gene Information

bovine ... LGB(280838)

General description

β-Lactoglobulin B (β-LG B), a isoform of β-Lactoglobulin, is a small protein of 162 amino acids with a molecular mass of 18.2 kDa and optimum pH of 5.2. It is present in high level in casein and is relatively low in raw bovine milk. β-LG has eight-stranded β-barrel (strands A-H) succeeded by a three-turn α-helix and a final β-strand (strand I), that forms part of the dimerization interface.
Milk from dairy cows contains the protein β-lactoglobulin (BLG). It naturally occurs in a number of genetic variants, and the most prevalent bovine variants are known as BLG A and BLG B.

Application

β-Lactoglobulin B from bovine milk has been used as:
  • a protein standard in SDS-polyacrylamide electrophoresis for quantification of milk protein fractions
  • in the calibration of reversed phase- high-performance liquid chromatography (HPLC) for caseins quantification
  • for immobilization on the biosensor surface and a calibration standards in biosensor assay

β-Lactoglobulin was used in the identification of the genetic variants of κ-casein in milk by isoelectric focusing electrophoresis.

Biochem/physiol Actions

β-Lactoglobulin B (β-LG B) show less inhibitory effect on the Staphylaococcus sp compared to β-LG A.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Milk protein fractions strongly affect the patterns of coagulation, curd firming, and syneresis
Amalfitano N, et al.
Journal of Dairy Science, 102(4), 2903-2917 (2019)
Casein polymorphism heterogeneity influences casein micelle size in milk of individual cows
Day L, et al.
Journal of Dairy Science, 98(6), 3633-3644 (2015)
Invited review: beta-lactoglobulin: binding properties, structure, and function
Kontopidis G, et al.
Journal of Dairy Science, 87(4), 785-796 (2004)
Huaying Zhao et al.
Current protocols in protein science, 101(1), e109-e109 (2020-07-03)
Sedimentation velocity analytical ultracentrifugation is a powerful classical method to study protein self-association processes in solution based on the size-dependent macromolecular migration in the centrifugal field. This technique can elucidate the assembly scheme, measure affinities ranging from picomolar to millimolar
Antimicrobial activity of bovine beta-lactoglobulin against mastitis-causing bacteria
Chaneton L, et al.
Journal of Dairy Science, 94(1), 138-145 (2011)

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