Binding of Vitamin D and Cholesterol to β-Lactoglobulin

Wang, Qiwu; Allen, Jeffrey C.; Swaisgood, Harold E.

doi:10.3168/jds.s0022-0302(97)76030-2

Cited by 114 publications

(96 citation statements)

References 23 publications

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“…The amino acid sequence of β-LG along with its 3-dimensional structure reveals association with the lipocalin superfamily (Kontopidis et al 2004). Its ability to bind hydrophobic bioactive substances and amphiphilic molecules ranges from hexane to palmitic acid to retinol to vitamin D. Studies have revealed β-LG-pectin complexes as molecular nano-vehicles for delivering hydrophobic nutraceuticals such as ω-3 polyunsaturated fatty acids and vitamin D (Wang et al 1997;Kontopidis et al 2004;Zimet and Livney 2009;Ron et al 2010;Cui et al 2012). Other biological activities of β-LG include enzyme regulation, neonatal acquisition of passive immunity, a source of bioactive peptides, and antimicrobial activity against mastitis-causing bacteria.…”

Section: Introductionmentioning

confidence: 99%

Nucleotide sequencing and DNA polymorphism studies of beta-lactoglobulin gene in native Saudi goat breeds in relation to milk yield

et al. 2015

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β-Lactoglobulin (β-LG) is the dominant non-casein whey protein found in milk of bovine and of most ruminants. The amino acid sequence of β-LG along with its 3-dimensional structure illustrates linkage with the lipocalin superfamily. Preliminary studies in goats indicated that milk yield can be influenced by polymorphism in genes coding for whey proteins. The aim of this study is to identify and evaluate the incidence of functional polymorphisms in the exonic and intronic portions of β-LG gene in native Saudi goat breeds (Ardi, Habsi and Harri). Blood samples were collected from 300 animals (100 for each breed) and genomic DNA was extracted using QIAamp DNA extraction kit. A fragment of the β-LG gene from exon 7 to 3' flanking region was amplified with pairs of specific primers. Subsequent digestion with Sac II restriction endonuclease revealed two alleles (A and B) and three different banding patterns or genotypes, i.e. AA, AB, and BB. The statistical analysis showed that β-LG AA genotype had higher milk yield than β-LG AB and β-LG BB genotypes. Nucleotide sequencing of the selected β-LG fragments was done and submitted to GenBank NCBI (Accession Nos. KJ544248, KJ588275, KJ588276, KJ783455, KJ783456, KJ874959, and KP269078). Two already established SNPs in exon 7 (+4601 and +4603) and one fresh SNP in the 3' UTR region were detected in the β-LG fragments with designated AA genotype. The exonic SNPs, i.e. +4601 (G/A) and +4603 (G/C), were found within the Sac II restriction site and accountable for generating the AA genotypic patterns. Hence, the allele characterized by the substitution G>A has been sub-designated as AA A , while the one characterized by the substitution G>C as AA C . The polymorphisms in exon 7 did not produce any amino acid substitution.

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Section: Introductionmentioning

confidence: 99%

Nucleotide sequencing and DNA polymorphism studies of beta-lactoglobulin gene in native Saudi goat breeds in relation to milk yield

et al. 2015

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“…It is a globular protein with a monomeric molecular weight of 18.4 kDa, consisting of 162 amino acids (Kontopidis et al, 2004). βlg is a member of the lipocalin family, which are able to bind small hydrophobic molecules, including fatty acids (FA) and hydrophobic vitamins , Flower, 1996, Wang et al, 1997, Ragona et al, 2000, Kontopidis et al, 2002, 2004, Considine et al, 2007, Jiang and Liu, 2010. All members of the lipocalin family contain a β-barrel, shaped into a calyx, composed of eight antiparallel β-strands (Flower, 1996).…”

Section: Introductionmentioning

confidence: 99%

β-Lactoglobulin-linoleate complexes: In vitro digestion and the role of protein in fatty acid uptake

Maux¹,

Brodkorb²,

Croguennec³

et al. 2013

Journal of Dairy Science

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The dairy protein β-lactoglobulin (BLG) is known to bind fatty acids such as the salt of the essential longchain fatty acid linoleic acid (cis,cis-9,12-octadecadienoic acid, n-6, 18:2). The aim of the current study was to investigate how bovine BLG-linoleate complexes, of various stoichiometry, affect the enzymatic digestion of BLG and the intracellular transport of linoleate into enterocyte-like monolayers. Duodenal and gastric digestions of the complexes indicated that BLG was hydrolyzed more rapidly when complexed with linoleate. Digested as well as undigested BLG-linoleate complexes reduced intracellular linoleate transport as compared with free linoleate. To investigate whether enteroendocrine cells perceive linoleate differently when part of a complex, the ability of linoleate to increase production or secretion of the enteroendocrine satiety hormone, cholecystokinin, was measured. Cholecystokinin mRNA levels were different when linoleate was presented to the cells alone or as part of a protein complex. In conclusion, understanding interactions between linoleate and BLG could help to formulate foods with targeted fatty acid bioaccessibility and, therefore, aid in the development of food matrices with optimal bioactive efficacy

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“…LGB is probably involved in storage and transport through the calves gastric tract hydrophobic substances such as fatty acids and retinoids naturally present in bovine milk (Pé rez and Calvo, 1995;Wang et al, 1997;Kontopidis et al, 2002). Is has been also observed that this protein enhances pregastric lipase activity towards triglycerides hydrolysis (Perez et al, 1992).…”

Section: Introductionmentioning

confidence: 99%

Two modes of fatty acid binding to bovine β‐lactoglobulin—crystallographic and spectroscopic studies

Loch¹,

Polit²,

Górecki³

et al. 2010

J of Molecular Recognition

107

104

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Lactoglobulin is a natural protein present in bovine milk and common component of human diet, known for binding with high affinity wide range of hydrophobic compounds, among them fatty acids 12-20 carbon atoms long. Shorter fatty acids were reported as not binding to β-lactoglobulin. We used X-ray crystallography and fluorescence spectroscopy to show that lactoglobulin binds also 8- and 10-carbon caprylic and capric acids, however with lower affinity. The determined apparent association constant for lactoglobulin complex with caprylic acid is 10.8 ± 1.7 × 10(3) M(-1), while for capric acid is 6.0 ± 0.5 × 10(3) M(-1). In crystal structures determined with resolution 1.9 Å the caprylic acid is bound in upper part of central calyx near polar residues located at CD loop, while the capric acid is buried deeper in the calyx bottom and does not interact with polar residues at CD loop. In both structures, water molecule hydrogen-bonded to carboxyl group of fatty acid is observed. Different location of ligands in the binding site indicates that competition between polar and hydrophobic interactions is an important factor determining position of the ligand in β-barrel.

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Binding of Vitamin D and Cholesterol to β-Lactoglobulin

Cited by 114 publications

References 23 publications

Nucleotide sequencing and DNA polymorphism studies of beta-lactoglobulin gene in native Saudi goat breeds in relation to milk yield

Nucleotide sequencing and DNA polymorphism studies of beta-lactoglobulin gene in native Saudi goat breeds in relation to milk yield

β-Lactoglobulin-linoleate complexes: In vitro digestion and the role of protein in fatty acid uptake

Two modes of fatty acid binding to bovine β‐lactoglobulin—crystallographic and spectroscopic studies

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