Design improvements of β-lactoglobulin

Abstract The functional performance of the whey protein β-lactoglobulin has been improved by the application of a rational design strategy and the use of site-directed mutagenesis to implement it. Three functional properties of β-lactoglobulin have been investigated: its ability to bind retinol; its tendency to form aggregates upon heating; and its ability to form thermoset gel networks. Any improvements made to β-lactoglobulin that enhance its performance during food processing will have a profound effect on its economic value. Such improvements, coupled with the ability to express them in dairy cattle, will increase the food and other applications of this protein as an ingredient, and open new markets for the use of whey proteins.

[1]  C. Batt,et al.  Cloning and partial nucleotide sequence of the genomic bovine beta-lactoglobulin gene. , 1990, Nucleic acids research.

[2]  M. Bolognesi,et al.  Crystal structure of the trigonal form of bovine beta-lactoglobulin and of its complex with retinol at 2.5 A resolution. , 1987, Journal of molecular biology.

[3]  J. Brady,et al.  Molecular dynamics simulations of the whey protein ß-lactoglobulin , 1992 .

[4]  J. Horwitz,et al.  Properties of the chromophore binding site of retinol-binding protein from human plasma. , 1974, The Journal of biological chemistry.

[5]  C. Batt,et al.  Reducing Whey Syneresis in Yogurt by the Addition of a Thermolabile Variant of β-Lactoglobulin , 1994 .

[6]  C. Batt,et al.  Cloning and nucleotide sequence of the bovine -lactoglobulin gene , 1987 .

[7]  A. Clark,et al.  Alteration of the quality of milk by expression of sheep β-lactoglobulin in transgenic mice , 1987, Nature.

[8]  T. Richardson,et al.  Genetic engineering of CASEINS , 1985 .

[9]  E. M. Brown,et al.  Three-dimensional molecular modeling of bovine caseins: an energy-minimized beta-casein structure. , 1993, Journal of dairy science.

[10]  C. Batt,et al.  Thermostable variants of bovine β-lactoglobulin , 1994 .

[11]  P. Kraulis,et al.  The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein , 1986, Nature.

[12]  J. Knowles.  Tinkering with enzymes: what are we learning? , 1987, Science.

[13]  E. M. Brown,et al.  Three-Dimensional Molecular Modeling of Bovine Caseins: A Refined, Energy-Minimized κ-Casein Structure , 1993 .

[14]  C. Batt,et al.  Probing the retinol-binding site of bovine beta-lactoglobulin. , 1994, The Journal of biological chemistry.

[15]  T. Richardson,et al.  Polymerization and gelation of thiolated β-lactoglobulin at ambient temperature induced by oxidation by potassium iodate. , 1990 .

[16]  C. Batt,et al.  Enhancing the gelation of β-lactoglobulin , 1993 .