Effect of the Bovine β-Lactoglobulin Phenotype on the Properties of β-Lactoglobulin, Milk Composition, and Dairy Products

Hill, J. P.; Boland, Mike; Creamer, Lawrence K.; Anema, Skelte G.; Otter, Don; Paterson, Geoff R.; Lowe, R.; Motion, Rose; Thresher, Wayne C.

doi:10.1021/bk-1996-0650.ch022

Cited by 47 publications

(23 citation statements)

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“…Taken from Manderson et al~1995! andHill et al 1996!. but distant from the EF loop: the closest contact of residue 64 with Ca atoms of the EF loop is ;25 Å for the open conformation of BLGA at pH 7.1 and ;19 Å for the closed conformation of BLGB at pH 7.1; the closest contact of any atom on loop CD with any atom on loop EF is ;9 Å for BLGA at pH 7.1~L87CB . .…”

Section: Conformation Of Loop Ef and The Tanford Transitionmentioning

confidence: 96%

“…There is a vast and somewhat confusing literature on the different chemical and physical properties of BLG, such as chemical reactivity of the free cysteine at position 121, thermal denaturation, Dannenberg & Kessler, 1988;Anema & McKenna, 1996;Hill et al, 1996!, and induces more readily the coagulation of milk at 140 8C~Rose, 1962; Feagan et al, 1972;McLean et al, 1987;van den Berg et al, 1992;Robitaille, 1995;Hill et al, 1996!-all undesirable properties for various heat treatments involved in standard milk processing~Hill et al, 1996!. Variant C is noticeably more stable than variant B to both thermal~Manderson et al, 1995thermal~Manderson et al, , 1998Hill et al, 1996!…”

Section: Functional Consequences Of Sequence Differences Of Blga and mentioning

confidence: 99%

“…Variant C has at position 59 at the end of strand b-C a histidine in place of the glutamine found for variants A and B. In general, variant C has enhanced thermal stability compared to variants A andB~Manderson et al, 1995, 1998;Hill et al, 1996!. For BLGA and BLGB a weak hydrogen bond between the side chains of Glu44 and Gln59 is probably replaced by a salt bridge~at neutral pH! between the side chains of Glu44 and His59, leading to enhanced rigidity in this region~Bewley et al, 1997!.…”

Section: Functional Consequences Of Sequence Differences Of Blga and mentioning

confidence: 99%

“…Of technological significance, bovine BLG variants have different effects on the industrial processing of milk and on the characteristics of milk products~Hill et al, 1996!. Thermal stability is in the order B Ͻ A Ͻ C, where B is most susceptible to thermal denaturatioñ Manderson et al, 1995;Hill et al, 1996!. These variants of bovine BLG have different self-association properties~Hill et al, 1996!.…”

Section: Introductionmentioning

confidence: 99%

“…These variants of bovine BLG have different self-association properties~Hill et al, 1996!. Variant A forms dimers and then octamers under increasingly acidic conditions, whereas variants B and C do not form octamers~Timasheff & Townend, 1961;Timasheff, 1964;Pessen et al, 1985!, but do form dimers, with dissociation constants in the micromolar range at pH ; 7 and stability constants in the order C Ͼ Ͼ B Ͼ A~Timasheff & Townend, 1961;McKenzie, 1971;McKenzie & Sawyer, 1972;Thresher et al, 1994;Hill et al, 1996;Thresher & Hill, 1997!. Both bovine BLG variants A and B undergo pH-dependent conformational changes in the range pH 6.5 to pH 7.5, the so called N ? R or Tanford transition~Tanford et al, 1959;Hambling et al, 1994!.…”

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confidence: 99%

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Functional implications of structural differences between variants A and B of bovine β‐lactoglobulin

Qin

Bewley

Creamer³

et al. 1999

Protein Science

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The structure of the trigonal crystal form of bovine b-lactoglobulin variant B at pH 7.1 has been determined by X-ray diffraction methods at a resolution of 2.22 Å and refined to values for R and R free of 0.239 and 0.286, respectively. By comparison with the structure of the trigonal crystal form of bovine b-lactoglobulin variant A at pH 7.1, which was determined previously @Qin BY et al., 1998, Biochemistry 37:14014-14023#, the structural consequences of the sequence differences D64G and V118A of variants A and B, respectively, have been investigated. Only minor differences in the core calyx structure occur. In the vicinity of the mutation site D64G on loop CD~residues 61-67!, there are small changes in main-chain conformation, whereas the substitution V118A on b-strand H is unaccompanied by changes in the surrounding structure, thereby creating a void volume and weakened hydrophobic interactions with a consequent loss of thermal stability relative to variant A. A conformational difference is found for the loop EF, implicated in the pH-dependent conformational change known as the Tanford transition, but it is not clear whether this reflects differences intrinsic to the variants in solution or differences in crystallization.Keywords: bovine b-lactoglobulin; crystal structure; genetic variants; hydrophobic stabilization Bovine b-lactoglobulin~BLG!, the major whey protein of cow's milk at a concentration of 0.3 g0100 mL~Bell & McKenzie, 1964!, was first isolated by Palmer~1934!. Mature bovine b-lactoglobulin has 162 residues, and is a member of the lipocalin protein superfamily~Flower, 1994, 1996!. Members of this family have a distinctive eight-stranded b-barrel structure, the central cavity of which binds a variety of hydrophobic molecules~Banaszak et al., 1994!. In the case of BLG, the primary site for fatty-acid binding has recently been established crystallographically to be inside this cavity~Qin et al., 1998b; Wu et al., 1999!. The structure of BLG is now reliably known following two independent redeterminations of the structure in the triclinic~lattice X!~Brownlow et al., 1997! and orthorhombic~lattice Y! forms~Bewley et al., 1997!. The latter structure has led to our redetermination of the structure in the trigonal~lattice Z! form~Qin et al., 1998a!. In lattice Z, in contrast to lattices X and Y, the entire molecule is well defined from electron density maps.Three variants of BLG, labeled as A, B, and C, commonly occur in cow's milk. Variants A and B~BLGA and BLGB! differ at two sites: Asp64 in A is changed to Gly in B, and Val118 in A is changed to Ala in B. Variants B and C differ at one site: Gln59 in B is changed to His in C. Thus, the isoelectric points for variants A, B, and C differ slightly: pI ϭ 5.26, 5.34, and 5.33, respectively, in 0.1 M KCl at room temperature~McKenzie, 1971!. Of technological significance, bovine BLG variants have different effects on the industrial processing of milk and on the characteristics of milk products~Hill et al., 1996!. Thermal stability is in the order B ...

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Section: Conformation Of Loop Ef and The Tanford Transitionmentioning

confidence: 96%

Section: Functional Consequences Of Sequence Differences Of Blga and mentioning

confidence: 99%

Section: Functional Consequences Of Sequence Differences Of Blga and mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

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Functional implications of structural differences between variants A and B of bovine β‐lactoglobulin

Qin

Bewley

Creamer³

et al. 1999

Protein Science

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134

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Milk Major and Minor Proteins, Polymorphisms and Non‐protein Nitrogen^*

Kukovics

Németh

2013

Milk and Dairy Products in Human Nutrition

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Isotopically Labeled Bovine β-Lactoglobulin for NMR Studies Expressed inPichia pastoris

Denton

Smith

Husi

et al. 1998

Protein Expression and Purification

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Effect of the Bovine β-Lactoglobulin Phenotype on the Properties of β-Lactoglobulin, Milk Composition, and Dairy Products

Cited by 47 publications

References 0 publications

Functional implications of structural differences between variants A and B of bovine β‐lactoglobulin

Functional implications of structural differences between variants A and B of bovine β‐lactoglobulin

Milk Major and Minor Proteins, Polymorphisms and Non‐protein Nitrogen^*

Isotopically Labeled Bovine β-Lactoglobulin for NMR Studies Expressed inPichia pastoris

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Effect of the Bovine β-Lactoglobulin Phenotype on the Properties of β-Lactoglobulin, Milk Composition, and Dairy Products

Cited by 47 publications

References 0 publications

Functional implications of structural differences between variants A and B of bovine β‐lactoglobulin

Functional implications of structural differences between variants A and B of bovine β‐lactoglobulin

Milk Major and Minor Proteins, Polymorphisms and Non‐protein Nitrogen*

Isotopically Labeled Bovine β-Lactoglobulin for NMR Studies Expressed inPichia pastoris

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Product

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Milk Major and Minor Proteins, Polymorphisms and Non‐protein Nitrogen^*