Advertisement
Article| Volume 79, ISSUE 5, P791-799, May 1996

Download started.

Ok

Alterations of the Physical Characteristics of Milk from Transgenic Mice Producing Bovine κ-Casein

  • Author Footnotes
    1 Department of Animal Science.
    A. Gutiérrez-Adán
    Footnotes
    1 Department of Animal Science.
    Affiliations
    University of California, Davis 95616
    Search for articles by this author
  • Author Footnotes
    1 Department of Animal Science.
    E.A. Maga
    Footnotes
    1 Department of Animal Science.
    Affiliations
    University of California, Davis 95616
    Search for articles by this author
  • Author Footnotes
    2 Genzyme Corporation, One Mountain Road, Framingham, MA 01536.
    H. Meade
    Footnotes
    2 Genzyme Corporation, One Mountain Road, Framingham, MA 01536.
    Affiliations
    University of California, Davis 95616
    Search for articles by this author
  • Author Footnotes
    3 Department of Food Science and Technology.
    C.F. Shoemaker
    Footnotes
    3 Department of Food Science and Technology.
    Affiliations
    University of California, Davis 95616
    Search for articles by this author
  • Author Footnotes
    1 Department of Animal Science.
    J.F. Medrano
    Footnotes
    1 Department of Animal Science.
    Affiliations
    University of California, Davis 95616
    Search for articles by this author
  • Author Footnotes
    1 Department of Animal Science.
    G.B. Anderson
    Footnotes
    1 Department of Animal Science.
    Affiliations
    University of California, Davis 95616
    Search for articles by this author
  • Author Footnotes
    1 Department of Animal Science.
    ,
    Author Footnotes
    4 Department of Veterinary Medicine Population Health and Reproduction.
    ,
    Author Footnotes
    5 Reprint requests.
    J.D. Murray
    Footnotes
    1 Department of Animal Science.
    4 Department of Veterinary Medicine Population Health and Reproduction.
    5 Reprint requests.
    Affiliations
    University of California, Davis 95616
    Search for articles by this author
  • Author Footnotes
    1 Department of Animal Science.
    2 Genzyme Corporation, One Mountain Road, Framingham, MA 01536.
    3 Department of Food Science and Technology.
    4 Department of Veterinary Medicine Population Health and Reproduction.
    5 Reprint requests.
Open ArchiveDOI:https://doi.org/10.3168/jds.S0022-0302(96)76427-5
Alterations of the Physical Characteristics of Milk from Transgenic Mice Producing Bovine κ-Casein
Previous ArticleEffects of Limited Proteolysis on the Microstructure of Heat-Induced Whey Protein Gels at Varying pH
Next ArticleResponses of Dairy Cows Supplemented with Somatotropin During Weeks 5 Through 43 of Lactation1
      This paper is only available as a PDF. To read, Please Download here.

      Abstract

      κ-Casein is the protein fraction of milk that allows formation of micelles and determines micelle size and function, thus affecting many of the physical characteristics of milk. Several lines of transgenic mice were generated bearing the B allele of the bovine κ-CN gene under the control of the regulatory sequences of the caprine β-CN gene that specifically directed expression of bovine κ-CN to the lactating mammary tissue of these mice. High expression of bovine κ-CN protein was observed in the lines studied; the total level of protein in milk was not significantly affected. A high degree of conservation in the amino acids involved in the predicted three-dimensional structure exists between murine and bovine κ-CN. Milk from transgenic lines expressing high bovine κ-CN had a significantly smaller micelle size than did control milk. Therefore, bovine κ-CN appears to have effectively participated in assembly of murine casein micelles. There was no effect on the time of rennet coagulation, but the association was significant between the milk of transgenic lines and the production of a stronger curd in rennet-induced gels. We conclude that bovine κ-CN is an appropriate candidate for transgenic technology that would increase the ratio of κ-CN to the calcium-sensitive caseins, therefore affecting the physical properties of the colloidal casein suspension.

      Key words

      References

        • Barnes H.A.
        • Hutton J.F.
        • Walters K.
        An Introduction to Rheology.
        Elsevier Publ., New York, NY1989
        • Bawden W.S.
        • Passey R.J.
        • Mackinlay A.G.
        The genes encoding the major milk-specific proteins and their use in transgenic studies and protein engineering.
        Biotechnol. Genet. Eng. Rev. 1994; 12: 89
        • Bynum D.G.
        • Olson N.F.
        Standardization of a device to measure firmness of curd during clotting of milk.
        J. Dairy Sci. 1982; 65: 1321
        • Chaplin B.
        • Green M.L.
        Determination of the proportion of κ-casein hydrolysed by rennet on coagulation of milk.
        J. Dairy Res. 1980; 47: 351
        • Clark A.H.
        • Ross-Murphy S.B.
        Advances in Polymer Science. Vol. 83. Springer-Verlag, Berlin, Germany1987
        • Clark A.J.
        Prospects for the genetic engineering of milk.
        J. Cell Biochem. 1992; 49: 121
        • Dalgleish D.G.
        • Brinkhuis J.
        • Payens T.A.J.
        The coagulation of differently sized casein micelles by rennet.
        Eur. J. Biochem. 1981; 119: 257
        • Dalgleish D.G.
        • Horse D.S.
        • Law A.J.R.
        Size-related differences in bovine casein micelles.
        Biochim. Biophys. Acta. 1989; 991: 383
        • Davies D.T.
        • Law A.J.R.
        Variation of the protein composition of bovine casein micelles and serum caseins in relation to micellar size and temperature.
        J. Dairy Sci. 1983; 50: 67
        • Donnelly W.J.
        • MacNeill G.P.
        • Buchheim W.
        • McGann T.C.A.
        Comprehensive study of the relationship between size and protein composition in natural bovine casein micelles.
        Biochim. Biophys. Acta. 1984; 789: 136
        • Ekstrand B.
        • Larsson-Raznikiewicz M.
        • Perlamann C.
        Casein micelles size and composition related to the enzymatic coagulation process.
        Biochim. Biophys. Acta. 1980; 630: 361
        • Farrell H.M.
        Physical equilibrium: proteins.
        in: Wong N.P. Fundamentals of Dairy Chemistry. Van Nostrand Reinhold Co., New York, NY1988: 461
        • Fox P.F.
        Heat-induced coagulation of milk.
        in: Developments in Dairy Chemistry. Vol. I. Appl. Sci., New York, NY1982: 189
        • Goff H.D.
        • Hill A.R.
        Chemistry and physics.
        in: Dairy Science and Technology. Vol. I. VCH (Verlag Chemie) Publ., New York, NY1993: 1
        • Gutierrez A.
        • Meade H.M.
        • Jimenez-Flores R.
        • Anderson G.B.
        • Murray J.D.
        • Medrano J.F.
        Expression of a bovine kappa-CN cDNA in the mammary gland of transgenic mice utilizing a genomic milk protein gene as an expression cassette.
        Transgenic Res. 1996; 5: 1
        • Halim H.K.
        • Shoemaker C.F.
        Effect of addition of α-, β-, and κ-casein, and Na-caseinate on viscoelastic properties of skim milk curd.
        J. Texture Stud. 1990; 21: 323
        • Hashizume K.
        • Sato T.
        Gel-forming characteristics of milk proteins. 2. Roles of sulfhydryl groups and disulfide bonds.
        J. Dairy Sci. 1988; 71: 1447
        • Holt C.
        The size distribution of bovine casein micelles: a review.
        Food Microstruct. 1985; 4: 1
        • Holt C.
        • Sawyer L.
        Primary and predicted secondary structures of the caseins in relation to their biological functions.
        Protein Eng. 1988; 2: 251
        • Jimenez-Flores R.
        • Richardson T.
        Genetic engineering of the caseins to modify the behavior of milk during processing: a review.
        J. Dairy Sci. 1988; 71: 2640
        • Kang Y.
        • Richardson T.
        Genetic engineering of caseins.
        Food Technol. 1985; 39: 89
        • Kumar S.
        • Clarke A.R.
        • Hooper M.L.
        • Home D.S.
        • Law A.J.R.
        • Leaver J.
        • Springbett A.
        • Stevenson E.
        • Simons J.P.
        Milk composition and lactation of β-casein-deficient mice.
        Proc. Natl. Acad. Sci. USA. 1994; 91: 6138
        • Kumosinski T.F.
        • Brown E.M.
        • Farrell Jr, H.M.
        Three-dimensional molecular modeling of bovine caseins: a refined, energy-minimized κ-casein structure.
        J. Dairy Sci. 1993; 76: 2507
        • Maga E.A.
        • Anderson G.B.
        • Murray J.D.
        The effect of mammary gland expression of human lysozyme on the properties of milk in transgenic mice.
        J. Dairy Sci. 1995; 78: 2645
        • Marziali A.S.
        • Ng-Kwai-Hang K.F.
        Effect of milk composition and genetic polymorphism on coagulating properties of milk.
        J. Dairy Sci. 1986; 69: 1793
        • McGann T.C.A.
        • Donnelly W.J.
        • Dearney R.D.
        • Buchheim W.
        Composition and size distribution of bovine casein micelles.
        Biochim. Biophys. Acta. 1980; 630: 261
        • McLean D.M.
        • Graham E.R.B.
        • Ponzoni R.W.
        • McKenzie H.A.
        Effects of milk protein genetic variants on milk yield and composition.
        J. Dairy Res. 1984; 51: 531
        • Mercier J.C.
        • Chobert J.-M.
        Comparative study of the amino acid sequences of the caseinomacropeptides from seven species.
        FEBS (Fed. Eur. Biol Soc.) Lett. 1976; 72: 208
        • Mercier J.C.
        • Gaye P.
        • Soulier S.
        • Hue-Delahaie D.
        • Vilotte J.L.
        Construction and identification of recombinant plasmids carrying cDNAs coding for ovine αs1-, αs2-,β-, κ-casein and β-lactoglobulin. Nucleotide sequence of αs1-casein Cdna.
        Biochimie. 1985; 67: 959
        • Morini D.
        • Losi G.
        • Castagnetti G.B.
        • Benevelli M.
        • Resmini P.
        • Volontenio G.
        L’influenza delle varianti genetiche della κ-caseina sulla dimensions delle micelle caseiniche.
        Sci. Tech. Latt. Cas. 1975; 26: 437
        • Muysson D.J.
        • Gibbins A.M.V.
        The alteration of milk content by genetic engineering and recombinant DNA-mediated selection techniques.
        Can. J. Anim. Sci. 1989; 69: 517
        • Ng-Kwai-Hang K.F.
        • Grosclaude F.
        Genetic poly- morphism of milk protein.
        in: Advanced Dairy Chemistry. Vol. I. Appl. Sci., New York, NY1992: 405
        • Ng-Kwai-Hang K.F.
        • Hayes J.F.
        • Moxley J.E.
        • Monardes H.G.
        Variation in milk protein concentrations associated with genetic polymorphism and environmental factors.
        J. Dairy Sci. 1987; 70: 563
        • Rasmussen L.K.
        • Hojrup P.
        • Petersen T.E.
        The multimeric structure and disulfide-bonding pattern of bovine κ-casein.
        Eur. J. Biochem. 1992; 207: 215

      35. Renner-Nantz, J. 1994. The effect of various processing conditions on the rheological properties of milk gels. M.S. Thesis, Univ. California, Davis.

        • Rollema H.S.
        Casein association and micelle formation.
        in: Advanced Dairy Chemistry. Vol. I. Appl. Sci., New York, NY1992: 110
        • Schaar J.
        Casein stability and cheesemaking. Properties of milk: effects of handling, mastitis and genetic variation.
        Swed. Univ. Agric. Sci., Uppsala, Sweden1981 (Rep 52)
        • Schaar J.
        Effect of κ-casein genetic variants and lactation number on the renneting properties of individual milks.
        J. Dairy Res. 1984; 51: 397
        • Schmidt D.G.
        Properties of artificial casein micelles.
        J. Dairy Res. 1979; 46: 351
        • Schmidt D.G.
        Association of caseins and casein micelle structure.
        in: Developments in Dairy Chemistry. Vol. I. Appl. Sci., New York, NY1982: 61
        • Shoemaker C.F.
        • Nantz J.
        • Bonnans S.
        • Noble A.C.
        Rheological characterization of dairy products.
        Food Technol. 1992; 1: 98
        • Sullivan R.A.
        • Fitzpatrick M.M.
        • Stanton E.K.
        Distribution of kappa-casein in skim milk.
        Nature (Lond.). 1959; 183: 616
        • Thompson M.D.
        • Dave J.R.
        • Nakhasi H.L.
        Molecular cloning of mouse mammary gland κ-casein: comparison with rat κ-casein and rat and human γ-fibrinogen.
        DNA (New York). 1985; 4: 263
        • Van Eenennaam A.L.
        • Medrano J.F.
        Differences in allelic protein expression in the milk of heterozygous κ-casein cows.
        J. Dairy Sci. 1991; 74: 1491
        • Walstra P.
        • Jenness R.
        Dairy Chemistry and Physics.
        John Wiley & Sons, ed., New York, NY1984
        • Wilde C.J.
        • Clark A.J.
        • Kerr M.A.
        • Knight C.H.
        • McClena-ghan M.
        • Simons J.P.
        Mammary development and milk secretion in transgenic mice expressing the beta-lactoglobulin gene.
        Biochem. J. 1992; 284: 717

      Article info

      Publication history

      Accepted: January 17, 1996
      Received: August 28, 1995

      Identification

      DOI: https://doi.org/10.3168/jds.S0022-0302(96)76427-5

      Copyright

      © 1996 American Dairy Science Association. Published by Elsevier Inc.

      User license

      Elsevier user license |
      How you can reuse Information Icon
      Elsevier user license

      Permitted

      For non-commercial purposes:

      • Read, print & download
      • Text & data mine
      • Translate the article

      Not Permitted

      • Reuse portions or extracts from the article in other works
      • Redistribute or republish the final article
      • Sell or re-use for commercial purposes

      Elsevier's open access license policy

      ScienceDirect

      Access this article on ScienceDirect

      The content on this site is intended for healthcare professionals.


      We use cookies to help provide and enhance our service and tailor content. To update your cookie settings, please visit the Cookie Preference Center for this site.
      Copyright © 2023 Elsevier Inc. except certain content provided by third parties.


      RELX