메뉴 건너뛰기




Volumn , Issue , 2001, Pages 271-334

Milk proteins: Biological and food aspects of structure and function

Author keywords

[No Author keywords available]

Indexed keywords

DAIRY FARMS; FOOD ASPECTS; HIGH WATER; LARGE-SCALE MANUFACTURING; MILK PROTEIN; NEUTRAL PH; SPONTANEOUS FERMENTATION;

EID: 0141601842     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (13)

References (135)
  • 1
    • 0032240057 scopus 로고    scopus 로고
    • Structural analysis of new antihypertensive peptides derived from cheese whey protein by proteinase k digestion
    • Abubakar, A., Saito, T., Kitazawa, H., Kawai. Y., and Itoh, T. 1998. “Structural analysis of new antihypertensive peptides derived from cheese whey protein by proteinase K digestion.” J. Dairy Sci. 81:3131-3138.
    • (1998) J. Dairy Sci , vol.81 , pp. 3131-3138
    • Abubakar, A.1    Saito, T.2    Kitazawa, H.Y.T.3
  • 2
    • 34548560769 scopus 로고
    • The characteristics and concentration of lactoferrin in finnish bovine milk
    • Ahonen, T., Korhonen, H., and Antila, M. 1978. “The characteristics and concentration of lactoferrin in Finnish bovine milk.” Meijeritieteellinen Aikakauskirja. 36:68-89.
    • (1978) Meijeritieteellinen Aikakauskirja , vol.36 , pp. 68-89
    • Ahonen, T.1    Korhonen, H.2    Antila, M.3
  • 3
    • 0022156350 scopus 로고
    • Effect of the lactoperoxidase system on lipoprotein lipase activity and lipolysis in milk
    • Ahrne, L. and Bjorck, L. 1985. “Effect of the lactoperoxidase system on lipoprotein lipase activity and lipolysis in milk.” J. Dairy Res. 52:513-520.
    • (1985) J. Dairy Res , vol.52 , pp. 513-520
    • Ahrne, L.1    Bjorck, L.2
  • 4
    • 0015528159 scopus 로고
    • Lactoferrin and transferrin: A comparative study
    • Aisen, P. and Leibman, A. 1972. “Lactoferrin and transferrin: a comparative study.” Biochim. Biophys. Acta. 257:314-323.
    • (1972) Biochim. Biophys. Acta , vol.257 , pp. 314-323
    • Aisen, P.1    Leibman, A.2
  • 5
    • 0024044319 scopus 로고
    • Separation of immunoglobulins and lactoferrin from cheese whey by chelating chromatography
    • Al-Mashikhi, S. A., Li-Chan, E., and Nakai, S. 1988. “Separation of immunoglobulins and lactoferrin from cheese whey by chelating chromatography.” J. Dairy Sci. 71:1747-1755.
    • (1988) J. Dairy Sci , vol.71 , pp. 1747-1755
    • Al-Mashikhi, S.A.1    Li-Chan, E.2    Nakai, S.3
  • 6
    • 0018463651 scopus 로고
    • The formation and structure of some proteose-peptone components
    • Andrews, A. T. 1979. “The formation and structure of some proteose-peptone components.” J. Dairy Res. 46:215-218.
    • (1979) J. Dairy Res , vol.46 , pp. 215-218
    • Andrews, A.T.1
  • 7
    • 0000145787 scopus 로고
    • Formation of soluble casein in whey protein-free milk heated at high temperature
    • Aoki, T, Suzuki, H., and Imamura, T. 1974. “Formation of soluble casein in whey protein-free milk heated at high temperature.” Milchwissenschaft. 29:589-594.
    • (1974) Milchwissenschaft , vol.29 , pp. 589-594
    • Aoki, T.1    Suzuki, H.2    Imamura, T.3
  • 8
    • 0026847631 scopus 로고
    • The least number of phosphate groups for crosslinking of casein by colloidal calcium phosphate
    • Aoki, T., Umeda, T., and Kako, Y. 1992. “The least number of phosphate groups for crosslinking of casein by colloidal calcium phosphate.” J. Dairy Sci. 75:971-975.
    • (1992) J. Dairy Sci , vol.75 , pp. 971-975
    • Aoki, T.1    Umeda, T.2    Kako, Y.3
  • 9
    • 0030133373 scopus 로고    scopus 로고
    • Effects of somatic cell count and stage of lactation on raw milk composition and the yield and quality of cheddar cheese
    • Auldist, M. J., Coats, S. T., Sutherland, B. J., Mayes, J. J., McDowell, G. H., and Rogers, G. L. 1996a. “Effects of somatic cell count and stage of lactation on raw milk composition and the yield and quality of cheddar cheese.” J. Dairy Res. 63:269-280.
    • (1996) J. Dairy Res , vol.63 , pp. 269-280
    • Auldist, M.J.1    Coats, S.T.2    Sutherland, B.J.3    Mayes, J.J.4    Mc Dowell, G.H.5    Rogers, G.L.6
  • 10
    • 0030209232 scopus 로고    scopus 로고
    • Effects of somatic cell count and stage of lactation on the quality and storage life of ultra high temperature milk
    • Auldist, M. J., Coats, S. T., Sutherland, B. J., Hardham, J. F., McDowell, G. H., and Rogers, G. L. 1996b. “Effects of somatic cell count and stage of lactation on the quality and storage life of ultra high temperature milk.” J. Dairy Res. 63:377-386.
    • (1996) J. Dairy Res , vol.63 , pp. 377-386
    • Auldist, M.J.1    Coats, S.T.2    Sutherland, B.J.3    Hardham, J.F.4    Mc Dowell, G.H.5    Rogers, G.L.6
  • 13
    • 0027691873 scopus 로고
    • Inhibition of plasmin by β-lactoglobulin using casein and a synthetic substrate
    • Bastian, E. D., Hansen, K. G., and Brown, R. J. 1993. “Inhibition of plasmin by β-lactoglobulin using casein and a synthetic substrate.” J. Dairy Sci. 76:3354-3361.
    • (1993) J. Dairy Sci , vol.76 , pp. 3354-3361
    • Bastian, E.D.1    Hansen, K.G.2    Brown, R.J.3
  • 14
    • 0033464236 scopus 로고    scopus 로고
    • Heat-induced gelation of whey protein at high ph studied by combined uv spectroscopy and refractive index measurements after size exclusion chromatography and by
    • Bauer, R., Rischel, C., Hansen, S., and 0gendal, L. 1999. “Heat-induced gelation of whey protein at high pH studied by combined UV spectroscopy and refractive index measurements after size exclusion chromatography and by in situ dynamic light scattering.” Int. J. Food Sci. Technol. 34:557-564.
    • (1999) Int. J. Food Sci. Technol , vol.34 , pp. 557-564
    • Bauer, R.1    Rischel, C.2    Hansen, S.3    Øgendal, L.4
  • 15
    • 84974095168 scopus 로고
    • Study of calcium binding to phosphoserine residues of β-casein and its phosphopeptide (1-25) by 31p nmr
    • Baumy, J. J., Guenot, P., Sinbandhit, S., and Brule, G. 1989. “Study of calcium binding to phosphoserine residues of β-casein and its phosphopeptide (1-25) by 31P NMR.” J. Dairy Res. 56:403-409.
    • (1989) J. Dairy Res , vol.56 , pp. 403-409
    • Baumy, J.J.1    Guenot, P.2    Sinbandhit, S.3    Brule, G.4
  • 16
    • 0014937614 scopus 로고
    • Peroxidase-mediated virucidal systems
    • Belding, M. I. and Klebanoff, S. J. 1970. “Peroxidase-mediated virucidal systems.” Science. 167:195-196.
    • (1970) Science , vol.167 , pp. 195-196
    • Belding, M.I.1    Klebanoff, S.J.2
  • 17
    • 0033091317 scopus 로고    scopus 로고
    • Proposing sequences for peptides derived from whey fermentation with potential bioactive sites
    • Belem, M. A. F., Gibbs, B. F., and Lee, B. H. 1999. “Proposing sequences for peptides derived from whey fermentation with potential bioactive sites.” J. Dairy Sci. 82:486-493.
    • (1999) J. Dairy Sci , vol.82 , pp. 486-493
    • Belem, M.A.F.1    Gibbs, B.F.2    Lee, B.H.3
  • 20
    • 0032016257 scopus 로고    scopus 로고
    • Inhibitory activity against plasmin, trypsin and elastase in rennet whey and in cheese fortified with whey proteins
    • Benfeldt, C., Sprensen, J., and Petersen, T. E. 1998. “Inhibitory activity against plasmin, trypsin and elastase in rennet whey and in cheese fortified with whey proteins.” J. Dairy Sci. 81:615-620.
    • (1998) J. Dairy Sci , vol.81 , pp. 615-620
    • Benfeldt, C.1    Sprensen, J.2    Petersen, T.E.3
  • 21
    • 0024347869 scopus 로고
    • Lactoferrin from human breast milk and from neutrophil granulocytes. Comparative studies of isolation, quantitation, characterization and iron binding properties
    • Bezwoda, W. R. and Mansoor, N. 1989. “Lactoferrin from human breast milk and from neutrophil granulocytes. Comparative studies of isolation, quantitation, characterization and iron binding properties.” Biomed. Chromatography. 3:121-126.
    • (1989) Biomed. Chromatography , vol.3 , pp. 121-126
    • Bezwoda, W.R.1    Mansoor, N.2
  • 22
    • 0000561063 scopus 로고
    • Xanthine oxidase as a source of hydrogen peroxide for the lactoperoxidase system in milk
    • Bjorck, L. and Claesson, O. 1979. “Xanthine oxidase as a source of hydrogen peroxide for the lactoperoxidase system in milk.” J. Dairy Sci. 62:1211—1215.
    • (1979) J. Dairy Sci , vol.62 , pp. 1211-1215
    • Bjorck, L.1    Claesson, O.2
  • 24
    • 0001447396 scopus 로고
    • α-lactalbumin
    • P. F. Fox, London and New York: Elsevier Applied Science
    • Brew, K. and Grobler, J. A. 1992. “α-Lactalbumin,” in Advanced Dairy Chemistry— 1: Proteins, ed. P. F. Fox, London and New York: Elsevier Applied Science, pp. 191-229.
    • (1992) Advanced Dairy Chemistry , pp. 191-229
    • Brew, K.1    Grobler, J.A.2
  • 25
    • 0010519790 scopus 로고    scopus 로고
    • Lactoferrin structure-function relationships: An overview
    • T. W. Hutchens, and B. Lonnerdal, Totowa, New Jersey: Humana Press
    • Brock, J. H. 1997. “Lactoferrin structure-function relationships: an overview,” in Lactoferrin— Interactions and Biological Functions, eds. T. W. Hutchens, and B. Lonnerdal, Totowa, New Jersey: Humana Press.
    • (1997) Lactoferrin— Interactions and Biological Functions
    • Brock, J.H.1
  • 26
    • 0032375531 scopus 로고    scopus 로고
    • Low-concentration-ratio ultrafiltration for cheddar cheese manufacture
    • Broome, M. C., Tan, S. E., Alexander, M. A., and Manser, B. 1998. “Low-concentration-ratio ultrafiltration for cheddar cheese manufacture.” Aust. J. Dairy Technol. 53:5-10.
    • (1998) Aust. J. Dairy Technol , vol.53 , pp. 5-10
    • Broome, M.C.1    Tan, S.E.2    Alexander, M.A.3    Manser, B.4
  • 27
    • 0026166365 scopus 로고
    • Ovine lactoferin: Isolation from colostrum and characterisation
    • Buchta, R. 1991. “Ovine lactoferin: isolation from colostrum and characterisation.” J. Dairy Res. 58:211-218.
    • (1991) J. Dairy Res , vol.58 , pp. 211-218
    • Buchta, R.1
  • 28
    • 0004219868 scopus 로고
    • Lund: Tetra Pak Processing Systems AB
    • Bylund, G. 1995. Dairy Processing Handbook. Lund: Tetra Pak Processing Systems AB, p. 339.
    • (1995) Dairy Processing Handbook , pp. 339
    • Bylund, G.1
  • 30
    • 0030507601 scopus 로고    scopus 로고
    • The effects of refrigerated storage on the quality of raw milk
    • Celestino, E. L., Iyer, M., and Roginski, H. 1996. “The effects of refrigerated storage on the quality of raw milk.” Aust. J. Dairy Technol. 51:59-63.
    • (1996) Aust. J. Dairy Technol , vol.51 , pp. 59-63
    • Celestino, E.L.1    Iyer, M.2    Roginski, H.3
  • 31
    • 0024372610 scopus 로고
    • Opioid antagonist peptides derived from k-casein
    • Chiba, H., Tani, F., and Yoshikawa, M. 1989. “Opioid antagonist peptides derived from K-casein.” J. Dairy Res. 56:363-366.
    • (1989) J. Dairy Res , vol.56 , pp. 363-366
    • Chiba, H.1    Tani, F.2    Yoshikawa, M.3
  • 32
    • 0034199281 scopus 로고    scopus 로고
    • Bioactive milk peptides: A prospectus
    • Clare, D. A. and Swaisgood, H. E. 2000. “Bioactive milk peptides: a prospectus.” J. Dairy Sci. 83:1187-1195.
    • (2000) J. Dairy Sci , vol.83 , pp. 1187-1195
    • Clare, D.A.1    Swaisgood, H.E.2
  • 33
    • 0343033897 scopus 로고
    • Heat resistant lipases and proteinases and the quality of dairy products
    • Cogan, T. M. 1980. “Heat resistant lipases and proteinases and the quality of dairy products.” Int. Dairy Fed. Bulletin, Doc. 118, pp. 26-32.
    • (1980) Int. Dairy Fed. Bulletin, Doc , vol.118 , pp. 26-32
    • Cogan, T.M.1
  • 34
    • 0029935514 scopus 로고    scopus 로고
    • Production of proteins in the milk of transgenic livestock: Problems, solutions and successes
    • Colman, A. 1996. “Production of proteins in the milk of transgenic livestock: problems, solutions and successes.” Am. J. Clin. Nutr. 63:639S-645S.
    • (1996) Am. J. Clin. Nutr , vol.63 , pp. 639S-645S
    • Colman, A.1
  • 35
    • 0033563952 scopus 로고    scopus 로고
    • Adsorption dynamics of a-lactalbumin and p-lactoglobulin at air-water interfaces
    • Comec, M., Cho, D., and Narsimhan, G. 1999. “Adsorption dynamics of a-lactalbumin and p-lactoglobulin at air-water interfaces.” J. Colloid Interface Sci. 214:129-142.
    • (1999) J. Colloid Interface Sci , vol.214 , pp. 129-142
    • Comec, M.1    Cho, D.2    Narsimhan, G.3
  • 36
    • 0008290589 scopus 로고
    • Physical and biochemical effects on milk components
    • R.C. McKellar, Boca Raton, Florida:, CRC Press, Inc
    • Cousin, M.A. 1989. “Physical and biochemical effects on milk components,” in Enzymes of Psychrotrophs in Raw Food, ed. R.C. McKellar, Boca Raton, Florida: CRC Press, Inc., pp. 205-225.
    • (1989) Enzymes of Psychrotrophs in Raw Food , pp. 205-225
    • Cousin, M.A.1
  • 37
    • 0002882021 scopus 로고
    • A study of the dissociation of p-casein from the bovine casein micelle at low temperature
    • Creamer, L. K., Berry, G. P., and Mills, O. E. 1977. “A study of the dissociation of P-casein from the bovine casein micelle at low temperature.” New Zealand J. Dairy Sci. Technol. 12:58-66.
    • (1977) Dairy Sci. Technol , vol.12 , pp. 58-66
    • Creamer, L.K.1    Berry, G.P.2    Mills, O.E.3
  • 38
    • 0000599870 scopus 로고
    • The enzymatic coagulation of milk
    • P. F. Fox, Barking, Essex: Elsevier Applied Science
    • Dalgleish, D. G. 1992. “The enzymatic coagulation of milk,” in Advanced Dairy Chemistry, Volume 1, ed. P. F. Fox, Barking, Essex: Elsevier Applied Science, pp. 579-620.
    • (1992) Advanced Dairy Chemistry, Volume 1 , pp. 579-620
    • Dalgleish, D.G.1
  • 39
    • 84865450762 scopus 로고    scopus 로고
    • Structure-function relationships of caseins
    • S. Damodaran and A. Paraf, New York-Basel-Hong, Kong: Marcel Dekker, Inc
    • Dalgleish, D. G. 1997. “Structure-function relationships of caseins,” in Food Proteins and Their Applications, eds., S. Damodaran and A. Paraf, New York-Basel-Hong Kong: Marcel Dekker, Inc., pp. 199-223.
    • (1997) Food Proteins and Their Applications , pp. 199-223
    • Dalgleish, D.G.1
  • 40
    • 0023730583 scopus 로고
    • Enhanced antimicrobial activity of lactoferrin by binding to the bacterial surface
    • Dalmastri, C., Valenti, P., Visca, P., Vittorioso, P., and Orsi, N. 1988. “Enhanced antimicrobial activity of lactoferrin by binding to the bacterial surface.” Microbiologica. 11:225-230.
    • (1988) Microbiologica , vol.11 , pp. 225-230
    • Dalmastri, C.1    Valenti, P.2    Visca, P.3    Vittorioso, P.4    Orsi, N.5
  • 41
    • 85032069769 scopus 로고
    • The composition of whole casein from the milk of ayrshire cows
    • Davies, D. T. and Law, A. J. R. 1977. “The composition of whole casein from the milk of Ayrshire cows.” J. Dairy Res. 44:447-454.
    • (1977) J. Dairy Res , vol.44 , pp. 447-454
    • Davies, D.T.1    Law, A.J.R.2
  • 42
    • 84974325077 scopus 로고
    • Variation in the protein composition of casein micelles and serum casein in relation to micellar size and milk temperature
    • Davies, D. T. and Law, A. J. R. 1983. “Variation in the protein composition of casein micelles and serum casein in relation to micellar size and milk temperature.” J. Dairy Res. 50:67-75.
    • (1983) J. Dairy Res , vol.50 , pp. 67-75
    • Davies, D.T.1    Law, A.J.R.2
  • 43
    • 0011394111 scopus 로고
    • Some features of the heat stability of concentrated milk. III. Seasonal effects on the amounts of casein, individual whey proteins and npn and their relation to variations in heat stability
    • de Koning, P. J., Koops, J., and van Rooijen, P. J. 1974. “Some features of the heat stability of concentrated milk. III. Seasonal effects on the amounts of casein, individual whey proteins and NPN and their relation to variations in heat stability.” Netherlands Milk and Dairy J. 28:186-202.
    • (1974) Netherlands Milk and Dairy J , vol.28 , pp. 186-202
    • De Koning, P.J.1    Koops, J.2    Van Rooijen, P.J.3
  • 44
    • 0026998049 scopus 로고
    • Casein micelles: Diffusivity as a function of renneting time
    • de Kruif, C. G. 1992. “Casein micelles: diffusivity as a function of renneting time.” Fangmuir. 8:2932-2937.
    • (1992) Fangmuir , vol.8 , pp. 2932-2937
    • De Kruif, C.G.1
  • 45
    • 85057417204 scopus 로고    scopus 로고
    • Whey protein fractionation using membranes
    • de Kruif, C. 1997. “Whey protein fractionation using membranes.” Food Sci. Technol. Today. 11:213-214.
    • (1997) Food Sci. Technol. Today , vol.11 , pp. 213-214
    • De Kruif, C.1
  • 46
    • 0348114294 scopus 로고    scopus 로고
    • Casein micelle structure substructure and interactions
    • P. F. Fox and P. Mc-Sweeney, 3rd edition, Gaithersburg, MD: Aspen Publications
    • de Kruif, C. G. and Holt, C. 2001. “Casein micelle structure substructure and interactions,” in Advanced Dairy Chemistry, Vol. 1: Proteins, eds. P. F. Fox and P. Mc-Sweeney, 3rd edition, Gaithersburg, MD: Aspen Publications.
    • (2001) Advanced Dairy Chemistry, Vol. 1: Proteins
    • De Kruif, C.G.1    Holt, C.2
  • 47
    • 0030588089 scopus 로고    scopus 로고
    • K-casein as a polyelectrolyte brush on the surface of casein micelles
    • de Kruif, C. G. and Zhulina, E. B. 1996. “K-Casein as a polyelectrolyte brush on the surface of casein micelles.” Colloids and Surfaces. 117:151-159.
    • (1996) Colloids and Surfaces , vol.117 , pp. 151-159
    • De Kruif, C.G.1    Zhulina, E.B.2
  • 48
    • 0002939524 scopus 로고
    • Functional properties of whey proteins
    • P. F. Fox, London and New, York: Elsevier Applied Science
    • de Wit, J. N. 1989a. “Functional properties of whey proteins,” in Developments in Dairy Chemistry— 4: Functional Milk Proteins, ed. P. F. Fox, London and New York: Elsevier Applied Science, pp. 285-321.
    • (1989) Developments in Dairy Chemistry , pp. 285-321
    • De Wit, J.N.1
  • 49
    • 0011439802 scopus 로고
    • The use of whey protein products
    • P. F. Fox, London and New York:, Elsevier Applied Science
    • de Wit, J. N. 1989b. “The use of whey protein products,” in Developments in Dairy Chemistry— 4: Functional Milk Proteins, ed. P. F. Fox, London and New York: Elsevier Applied Science, pp. 323-345.
    • (1989) Developments in Dairy Chemistry , pp. 323-345
    • De Wit, J.N.1
  • 50
    • 0032794189 scopus 로고    scopus 로고
    • Fourier-transform infrared spectroscopy study of the pressure-induced changes in the structure of the bovine a-lactalbumin: The stabilizing role of calcium ion
    • Dzwolak, W., Kato M., Shimizu, A., and Taniguchi, Y. 1999. “Fourier-transform infrared spectroscopy study of the pressure-induced changes in the structure of the bovine a-lactalbumin: the stabilizing role of calcium ion.” Biochim. Biophys. Acta, Prot. Structure Mol. Enzymol. 1433:45-55.
    • (1999) Prot. Structure Mol. Enzymol , vol.1433 , pp. 45-55
    • Dzwolak, W.1    Kato, M.2    Shimizu, A.3    Taniguchi, Y.4
  • 52
    • 84985175619 scopus 로고
    • Heat interactions between α-lactalbumin, β-lactoglobulin and casein in bovine milk
    • Elfagm, A. A. and Wheelock, J. V. 1978. “Heat interactions between α-lactalbumin, β-lactoglobulin and casein in bovine milk.” J. Dairy Sci. 61:159-163.
    • (1978) J. Dairy Sci , vol.61 , pp. 159-163
    • Elfagm, A.A.1    Wheelock, J.V.2
  • 53
    • 0032038921 scopus 로고    scopus 로고
    • Effect of psychrotrophic microorganisms on the plasmin system in milk
    • Fajardo-Lira, C. E. and Nielsen, S. S. 1998. “Effect of psychrotrophic microorganisms on the plasmin system in milk.” J. Dairy Sci. 81:901-908.
    • (1998) J. Dairy Sci , vol.81 , pp. 901-908
    • Fajardo-Lira, C.E.1    Nielsen, S.S.2
  • 54
    • 0001701660 scopus 로고    scopus 로고
    • The conformation of α-lactalbumin as a function of ph, heat treatment and adsorption at hydrophobic surfaces studied by ftir
    • Fang, Y. and Dalgleish, D. G. 1998. “The conformation of α-lactalbumin as a function of pH, heat treatment and adsorption at hydrophobic surfaces studied by FTIR.” Food Hydrocolloids. 12:121-126.
    • (1998) Food Hydrocolloids , vol.12 , pp. 121-126
    • Fang, Y.1    Dalgleish, D.G.2
  • 56
    • 0004168670 scopus 로고
    • Fox, R F., ed., Fondon and New York: Applied Science Publishers
    • Fox, R F., ed. 1982. Developments in Dairy Chemistry— 1. Proteins. Fondon and New York: Applied Science Publishers.
    • (1982) Developments in Dairy Chemistry
    • Fox, R.F.1
  • 57
    • 0004187143 scopus 로고
    • Fox, P. F., ed., Fondon and New York: Elsevier Applied Science
    • Fox, P. F., ed. 1992a. Advanced Dairy Chemistry— F. Proteins. Fondon and New York: Elsevier Applied Science.
    • (1992) Advanced Dairy Chemistry
    • Fox, P.F.1
  • 58
    • 0011542909 scopus 로고
    • Proteinases
    • K. M. Pruitt and J. O. Tenovuo, New York and Basel: Marcel Dekker Inc
    • Paul, K.-G. and Ohlsson, P.-I. 1985. “The chemical structure of lactoperoxidase,” in The Lactoperoxidase System—Chemistry and Biological Significance, eds. K. M. Pruitt and J. O. Tenovuo, New York and Basel: Marcel Dekker Inc., pp. 15-29.
    • (1992) Advanced Dairy Chemistry , pp. 310-321
    • Fox, P.F.1
  • 59
    • 0001345475 scopus 로고
    • Thermal separation of β-lactoglobulin and α-lactalbumin in bovine cheddar cheese whey
    • Pearce, R. J. 1983. “Thermal separation of β-lactoglobulin and α-lactalbumin in bovine cheddar cheese whey.” Aust. J. Dairy Technol. 38:144-149.
    • (1983) Aust. J. Dairy Technol , vol.38 , pp. 144-149
    • Pearce, R.J.1
  • 61
    • 85057435113 scopus 로고
    • Infection and antibody production in the udder
    • Petersen, W. E. 1955. “Infection and antibody production in the udder.” Aust. J. Dairy Technol. 10:117-122.
    • (1955) Aust. J. Dairy Technol , vol.10 , pp. 117-122
    • Petersen, W.E.1
  • 64
    • 0031201392 scopus 로고    scopus 로고
    • Presence in bovine milk of two protease inhibitors of the plasmin system
    • Precetti, A. S., Oria, M. P., and Nielsen, S. S. 1997. “Presence in bovine milk of two protease inhibitors of the plasmin system.” J. Dairy Sci. 80:1490-1496.
    • (1997) J. Dairy Sci , vol.80 , pp. 1490-1496
    • Precetti, A.S.1    Oria, M.P.2    Nielsen, S.S.3
  • 66
    • 0031762646 scopus 로고    scopus 로고
    • Antiviral effect of bovine lactoferrin saturated with metal ions on early steps of human immunodeficiency virus type 1 infection
    • Puddu, P., Borghi, P., Gessani, S., Valenti, P., Belardelli, F., and Seganti, F. 1998. “Antiviral effect of bovine lactoferrin saturated with metal ions on early steps of human immunodeficiency virus type 1 infection.” Int. J. Biochem. Cell Biol. 30:1055-1062.
    • (1998) Int. J. Biochem. Cell Biol , vol.30 , pp. 1055-1062
    • Puddu, P.1    Borghi, P.2    Gessani, S.3    Valenti, P.4    Belardelli, F.5    Seganti, F.6
  • 67
    • 0242590199 scopus 로고    scopus 로고
    • Introduction to the subject
    • Brussels: International Dairy Federation
    • Puhan, Z. 1997. “Introduction to the subject,” in Milk Protein Polymorphism, S.I. 9702, Brussels: International Dairy Federation, pp. 12-21.
    • (1997) Milk Protein Polymorphism, S.I , vol.9702 , pp. 12-21
    • Puhan, Z.1
  • 68
    • 0041033250 scopus 로고    scopus 로고
    • Rheological properties of commercial whey protein samples from the
    • Puyol, P., Perez, M. D., and Calvo, M. 1999. “Rheological properties of commercial whey protein samples from the MADGELAS survey.” Int. J. Food Sci. Technol. 34:565-572.
    • (1999) Int. J. Food Sci. Technol , vol.34 , pp. 565-572
    • Puyol, P.1    Perez, M.D.2    Calvo, M.3
  • 69
    • 0030993642 scopus 로고    scopus 로고
    • Effect of temperature on the secondary structure of β-lactoglobulin at ph 6.7, as determined by circular dichroism and infrared spectroscopy: A test of the molten
    • Qi, X. F., Holt, C., McNulty, D., Clarke, D. T., Brownlow, S., and Jones, G. R. 1997. “Effect of temperature on the secondary structure of y-lactoglobulin at pH 6.7, as determined by circular dichroism and infrared spectroscopy: A test of the molten globule hypothesis.” Biochem. J. 324:341-346.
    • (1997) Biochem. J , vol.324 , pp. 341-346
    • Qi, X.F.1    Holt, C.2    Mc Nulty, D.3    Clarke, D.T.4    Brownlow, S.5    Jones, G.R.6
  • 70
    • 0015219737 scopus 로고
    • Molecular weight, single-chain structure, and amino-acid composition of human lactoferrin
    • Querinjean, P., Masson, P., and Heremans, J. F. 1971. “Molecular weight, single-chain structure, and amino-acid composition of human lactoferrin.” Fur. J. Biochem. 20:420-425.
    • (1971) Fur. J. Biochem , vol.20 , pp. 420-425
    • Querinjean, P.1    Masson, P.2    Heremans, J.F.3
  • 71
    • 0024919787 scopus 로고
    • Milk product protects against rotavirus
    • Ragg, M. 1989. “Milk product protects against rotavirus.” Today’s Fife Science. 1:57-59.
    • (1989) Today’s Fife Science , vol.1 , pp. 57-59
    • Ragg, M.1
  • 72
    • 0030635208 scopus 로고    scopus 로고
    • Identification of a conserved hydrophobic cluster in partially folded bovine β-lactoglobulin at ph 2
    • Ragona, F., Pusterla, F., Zetta, F., Monaco, H., and Molinari, H. 1997. “Identification of a conserved hydrophobic cluster in partially folded bovine β-lactoglobulin at pH 2.” Folding and Design. 2:281-290.
    • (1997) Folding and Design , vol.2 , pp. 281-290
    • Ragona, F.1    Pusterla, F.2    Zetta, F.3    Monaco, H.4    Molinari, H.5
  • 73
    • 0000420026 scopus 로고
    • Seasonal changes in the β-lactoglobulin and a-lactalbumin, glycomacropeptide, and casein content of whey protein concentrate
    • Regester, G.O. and Smithers, G.W. 1991. “Seasonal changes in the β-lactoglobulin and α-lactalbumin, glycomacropeptide, and casein content of whey protein concentrate.” Journal of Dairy Science. 74:796-802.
    • (1991) Journal of Dairy Science , vol.74 , pp. 796-802
    • Regester, G.O.1    Smithers, G.W.2
  • 74
    • 21144484329 scopus 로고
    • Seasonal changes in the physical and functional properties of whey protein concentrates
    • Regester, G. O., Smithers, G. W., Mangino. M. E., and Pearce, R. J. 1992. “Seasonal changes in the physical and functional properties of whey protein concentrates.” Journal of Dairy Science. 75:2928-2936.
    • (1992) Journal of Dairy Science , vol.75 , pp. 2928-2936
    • Regester, G.O.1    Smithers, G.W.M.E.R.J.2
  • 75
    • 85057394917 scopus 로고
    • The impact of the lactoperoxidase system on the psychrotrophic microflora in milk
    • G. Hobbs, J. H. B. Christian and N. Skovgaard, Fondon and New York: Academic Press
    • Reiter, B. 1981. “The impact of the lactoperoxidase system on the psychrotrophic microflora in milk,” in Psychrotrophic Microorganisms in Spoilage and Pathogenicity, eds. G. Hobbs, J. H. B. Christian and N. Skovgaard, Fondon and New York: Academic Press, pp. 73-85.
    • (1981) Psychrotrophic Microorganisms in Spoilage and Pathogenicity , pp. 73-85
    • Reiter, B.1
  • 76
    • 33749850670 scopus 로고
    • The biological significance and exploitation of the nonimmunoglobulin protective proteins in milk: Lysozyme, lactoferrin, lactoperoxidase, xanthine oxidase
    • Bull
    • Reiter, B. 1985. “The biological significance and exploitation of the nonimmunoglobulin protective proteins in milk: Lysozyme, lactoferrin, lactoperoxidase, xanthine oxidase.” International Dairy Federation, Bull. 191.
    • (1985) International Dairy Federation , pp. 191
    • Reiter, B.1
  • 77
    • 0016658221 scopus 로고
    • Inhibition of Escherichia coli by bovine colostrum and post-colostral milk. II. The bacteriostatic effect of lactoferrin on a serum susceptible and serum resistant strain of E. Coli
    • Reiter, B., Brock, J. H., and Steel, E. D. 1975. “Inhibition of Escherichia coli by bovine colostrum and post-colostral milk. II. The bacteriostatic effect of lactoferrin on a serum susceptible and serum resistant strain of E. coli.” Immunology. 28:83-95.
    • (1975) Immunology , vol.28 , pp. 83-95
    • Reiter, B.1    Brock, J.H.2    Steel, E.D.3
  • 78
    • 0032924742 scopus 로고    scopus 로고
    • Construction and synthesis of lactoferricin derivatives with enhanced antibacterial activity
    • Rekdal, 0., Andersen, J., Vorland, L. H., and Svendsen, J. S. 1999. “Construction and synthesis of lactoferricin derivatives with enhanced antibacterial activity.” J. Pept. Sci. 5:32-45.
    • (1999) J. Pept , vol.5 , pp. 32-45
    • Rekdal, O.1    Andersen, J.2    Vorland, L.H.3    Svendsen, J.S.4
  • 79
    • 0023359760 scopus 로고
    • The prevention of sub-surface demineralization of bovine enamel and change in plaque composition by casein in an intra-oral model
    • Reynolds, E. 1987. “The prevention of sub-surface demineralization of bovine enamel and change in plaque composition by casein in an intra-oral model.” J. Dental Res. 66:1120-1127.
    • (1987) J. Dental , vol.66 , pp. 1120-1127
    • Reynolds, E.1
  • 80
    • 0028218041 scopus 로고
    • A selective precipitation purification procedure for multiple phosphoseryl-containing peptides and methods for their identification
    • Reynolds, E. C., Riley, R F., and Adamson, N. J. 1994. “A selective precipitation purification procedure for multiple phosphoseryl-containing peptides and methods for their identification.” Anal. Biochem. 217:277-284.
    • (1994) Anal. Biochem , vol.217 , pp. 277-284
    • Reynolds, E.C.1    Riley, R.F.2    Adamson, N.J.3
  • 81
    • 0028567981 scopus 로고
    • A model for the denaturation and aggregation of β-lactoglobulin
    • Roefs, S. P. F. M. and de Kruif, C. G. 1994. “A model for the denaturation and aggregation of y-lactoglobulin.” Eur. J. Biochemistry. 226:883-889.
    • (1994) Eur. J. Biochemistry , vol.226 , pp. 883-889
    • Roefs, S.P.F.M.1    De Kruif, C.G.2
  • 82
    • 0040215006 scopus 로고
    • Non-phage inhibition of group n streptococci in milk. 1. The incidence of inhibition in bulk milk
    • Roginski, H., Broome, M. C., and Hickey, M. W. 1984. “Non-phage inhibition of group N streptococci in milk. 1. The incidence of inhibition in bulk milk.” Aust. J. Dairy Technol. 39:23-27.
    • (1984) Aust. J. Dairy , vol.39 , pp. 23-27
    • Roginski, H.1    Broome, M.C.2    Hickey, M.W.3
  • 83
    • 0000529133 scopus 로고
    • Casein association and micelle formation
    • P. F. Fox, Fondon and New York: Elsevier Applied, Science
    • Rollema, H. S. 1992. “Casein association and micelle formation,” in Advanced Dairy Chemistry— 1: Proteins, ed. P. F. Fox, Fondon and New York: Elsevier Applied Science, pp. 111-140.
    • (1992) Advanced Dairy Chemistry , pp. 111-140
    • Rollema, H.S.1
  • 85
    • 0024345058 scopus 로고
    • 1H-NMR study of bovine casein micelles; influence of ph, temperature and calcium ions on micellar structure
    • 1H-NMR study of bovine casein micelles; influence of pH, temperature and calcium ions on micellar structure.” J. Dairy Res. 56:417-425.
    • (1989) J. Dairy Res , vol.56 , pp. 417-425
    • Rollema, H.S.1    Brinkhuis, J.A.2
  • 86
    • 84976113450 scopus 로고
    • A calorimetric study of the thermal denaturation of whey proteins in simulated milk ultrafiltrate
    • Riiegg, M., Moor, U., and Blanc, B. 1977. “A calorimetric study of the thermal denaturation of whey proteins in simulated milk ultrafiltrate.” J. Dairy Res. 44:509-520.
    • (1977) J. Dairy Res , vol.44 , pp. 509-520
    • Riiegg, M.1    Moor, U.2    Blanc, B.3
  • 87
    • 0034221181 scopus 로고    scopus 로고
    • Isolation and structural analysis of antihypertensive peptides that exist naturally in gouda cheese
    • Saito, T., Nakamura, T., Kitazawa, Y., Kawai, Y., and Itoh. T. 2000. “Isolation and structural analysis of antihypertensive peptides that exist naturally in Gouda cheese.” J. Dairy Sci. 83:1434-1440.
    • (2000) J. Dairy Sci , vol.83 , pp. 1434-1440
    • Saito, T.1    Nakamura, T.2    Kitazawa, Y.3    Kawai, Y.4
  • 89
    • 4644298225 scopus 로고    scopus 로고
    • Direct transfection of the mammary gland: Opportunities for modification of mammary function and the production, composition and qualities of milk
    • R.A.S. Welch, D. J. W. Burns, S. R. Davis, A. I. Popay and C. G. Prosser, Wallingford: CAB International
    • Schanbacher, F. F. and Amstutz, M. D. 1997. “Direct transfection of the mammary gland: Opportunities for modification of mammary function and the production, composition and qualities of milk,” in Milk Composition, Production and Biotechnology, eds. R.A.S. Welch, D. J. W. Burns, S. R. Davis, A. I. Popay and C. G. Prosser, Wallingford: CAB International, pp. 243-264.
    • (1997) Milk Composition, Production and Biotechnology , pp. 243-264
    • Schanbacher, F.F.1    Amstutz, M.D.2
  • 90
    • 84984458687 scopus 로고
    • Bioactive peptides derived from milk proteins. Structural, physiological and analytical aspects
    • Schlimme, E. and Meisel, H. 1995. “Bioactive peptides derived from milk proteins. Structural, physiological and analytical aspects.” Die Nahrung. 39:1-20.
    • (1995) Die Nahrung , vol.39 , pp. 1-20
    • Schlimme, E.1    Meisel, H.2
  • 91
    • 0002429127 scopus 로고
    • Association of caseins and casein micelle structure
    • P. F. Fox, ed, Applied Science Publishers, Barking, UK
    • Schmidt, D. G. 1982. “Association of caseins and casein micelle structure,” in Developments in Dairy Chemistry (P. F. Fox, ed.), Applied Science Publishers, Barking, UK: pp. 61-86.
    • (1982) Developments in Dairy Chemistry , pp. 61-86
    • Schmidt, D.G.1
  • 92
    • 17144389124 scopus 로고
    • Thermischer abbau von a-factalbumin. I. Zerstorung von zystinresten
    • Schnack, U. and Klostermayer, H. 1980. “Thermischer Abbau von a-Factalbumin. I. Zerstorung von Zystinresten.” Milchwissenschaft. 35:206-208.
    • (1980) Milchwissenschaft , vol.35 , pp. 206-208
    • Schnack, U.1    Klostermayer, H.2
  • 95
    • 0001353383 scopus 로고
    • Heat stability of milk
    • P. F. Fox, London and New York: Elsevier Applied Science
    • Singh, H. and Creamer, L. K. 1992. “Heat stability of milk,” in Advanced Dairy Chemistry— 1: Proteins, ed. P. F. Fox, London and New York: Elsevier Applied Science, pp. 621-656.
    • (1992) Advanced Dairy Chemistry , pp. 621-656
    • Singh, H.1    Creamer, L.K.2
  • 96
    • 0033230075 scopus 로고    scopus 로고
    • Use of mass spectrometry to rapidly characterize the heterogeneity of bovine a-lactalbumin
    • Slangen, C. J. and S. Visser. 1999. “Use of mass spectrometry to rapidly characterize the heterogeneity of bovine a-lactalbumin.” J. Agric. Food Chem. 47:4549-4556.
    • (1999) J. Agric. Food Chem , vol.47 , pp. 4549-4556
    • Slangen, C.J.1    Visser, S.2
  • 98
    • 0035144719 scopus 로고    scopus 로고
    • Solution structure of native proteins with irregular folds from raman optical activity
    • Smyth, E., Syme, C. D., Blanch, E. W., Hecht, L., Vasak, M., and Barron, L. D. 2000. “Solution structure of native proteins with irregular folds from Raman optical activity.” Biopolymers. 58:138-151.
    • (2000) Biopolymers , vol.58 , pp. 138-151
    • Smyth, E.1    Syme, C.D.2    Blanch, E.W.3    Hecht, L.4    Vasak, M.5    Barron, L.D.6
  • 101
    • 85057365302 scopus 로고
    • Production of foreign protein in the mammary gland of transgenic mammals
    • Stranzinger, G. F. 1993. “Production of foreign protein in the mammary gland of transgenic mammals.” International Dairy Federation, Bull. 279, 55-58.
    • (1993) International Dairy Federation, Bull , vol.279 , pp. 55-58
    • Stranzinger, G.F.1
  • 103
    • 0343469579 scopus 로고
    • Occurrence and levels of heat-resistant proteinases and their effects on uht-treated dairy products
    • Suhren, G. 1983. “Occurrence and levels of heat-resistant proteinases and their effects on UHT-treated dairy products.” Int. Dairy Fed. Bull. 157, pp. 17-25.
    • (1983) Int. Dairy Fed. Bull , vol.157 , pp. 17-25
    • Suhren, G.1
  • 104
    • 0030661831 scopus 로고    scopus 로고
    • Antirotaviral activity of milk proteins: Lactoferrin prevents rotavirus infection in the enterocytelike cell line ht-29
    • Superti, F., Ammendolia, M. G., Valenti, P., and Seganti, L. 1997. “Antirotaviral activity of milk proteins: Lactoferrin prevents rotavirus infection in the enterocytelike cell line HT-29.” Med. Microbiol. Immunol. 186:83-91.
    • (1997) Med. Microbiol. Immunol , vol.186 , pp. 83-91
    • Superti, F.1    Ammendolia, M.G.2    Valenti, P.3    Seganti, L.4
  • 105
    • 0002772383 scopus 로고
    • Chemistry of the caseins
    • P. F. Fox, London and New York: Elsevier Applied Science
    • Swaisgood, H. E. 1992. “Chemistry of the caseins,” in Advanced Dairy Chemistry— 1: Proteins, ed. P. F. Fox, London and New York: Elsevier Applied Science, pp. 63-110.
    • (1992) Advanced Dairy Chemistry , pp. 63-110
    • Swaisgood, H.E.1
  • 106
    • 0002692649 scopus 로고
    • Protein and amino acid composition of bovine milk
    • R. G. Jensen, San Diego: Academic Press
    • Swaisgood, H. E. 1995. “Protein and amino acid composition of bovine milk,” in Handbook of Milk Composition, ed. R. G. Jensen, San Diego: Academic Press, pp. 464-468.
    • (1995) Handbook of Milk Composition , pp. 464-468
    • Swaisgood, H.E.1
  • 107
    • 0029892820 scopus 로고    scopus 로고
    • Antiviral effects of milk proteins: Acylation results in polyanionic compounds with potent activity against human immunodeficiency
    • Swart P. J., Kuipers, M. E., Smit, C., Pauwels, R., de Bethune, M.-P, De Clercq, E., Meijer, D. K. F., and Huisman, J. G. 1996. “Antiviral effects of milk proteins: Acylation results in polyanionic compounds with potent activity against Human Immunodeficiency Vims types 1 and 2 in vitro." AIDS Res. Hum. Retroviruses. 12:769-775.
    • (1996) AIDS Res. Hum. Retroviruses , vol.12 , pp. 769-775
    • Swart, P.J.1    Kuipers, M.E.2    Smit, C.3    Pauwels, R.4    De Bethune, M.-P.5    De Clercq, E.6    Meijer, D.K.F.7    Huisman, J.G.8
  • 109
    • 0023891820 scopus 로고
    • Protection by milk immunoglobulin concentrate against oral challenge with enterotoxigenic
    • Tacket, C., Losonsky, G., Link, H., Hoang, Y., Guesry, P., Hilpert, H., and Levine, M. M. 1988. “Protection by milk immunoglobulin concentrate against oral challenge with enterotoxigenic Escherichia coli." New England J. Med. 318:1240-1243.
    • (1988) New England J. Med , vol.318 , pp. 1240-1243
    • Tacket, C.1    Losonsky, G.2    Link, H.3    Hoang, Y.4    Guesry, P.5    Hilpert, H.6    Levine, M.M.7
  • 110
    • 0032076816 scopus 로고    scopus 로고
    • Milk derived peptides and hypertension reduction
    • Takano, T. 1998. “Milk derived peptides and hypertension reduction.” Int. Dairy Journal. 8:375-381.
    • (1998) Int. Dairy Journal , vol.8 , pp. 375-381
    • Takano, T.1
  • 112
    • 0000519535 scopus 로고
    • Immunologic and allergic properties of cows milk proteins in humans
    • Taylor, S. L. 1986. “Immunologic and allergic properties of cow’s milk proteins in humans.” J. Food Prot. 49:239-250.
    • (1986) J. Food Prot , vol.49 , pp. 239-250
    • Taylor, S.L.1
  • 113
    • 0002291190 scopus 로고
    • Milk protein-derived atypical opioid peptides and related compounds with opioid antagonist activity (Review)
    • V. Brand, and H. Teschemacher, Weinheim: VCH Verlagsgesellschaft mbH
    • Teschemacher, H., Koch, G., and Brand, V. 1994. “Milk protein-derived atypical opioid peptides and related compounds with opioid antagonist activity (review),” in | Z-Casomorphins and Related Peptides: Recent Developments, eds. V. Brand, and H. Teschemacher, Weinheim: VCH Verlagsgesellschaft mbH., pp. 3-17.
    • (1994) Z-Casomorphins and Related Peptides: Recent Developments , pp. 3-17
    • Teschemacher, H.1    Koch, G.2    Brand, V.3
  • 114
    • 0018099284 scopus 로고
    • Lactoperoxidase, peroxide, thiocyanate antimicrobial system: Correlation of sulfhydryl oxidation with antimicrobial action
    • Thomas, E. L. and Aune, T. M. 1977. Lactoperoxidase, peroxide, thiocyanate antimicrobial system: Correlation of sulfhydryl oxidation with antimicrobial action. Infect. Immun. 20:456-463.
    • (1977) Infect , vol.20 , pp. 456-463
    • Thomas, E.L.1    Aune, T.M.2
  • 115
    • 33847488702 scopus 로고
    • Composition of milk on the atherton tableland. 4. Milk constituents
    • Tucker, V. C. 1969. “Composition of milk on the Atherton tableland. 4. Milk constituents.” Aust. J. Dairy Technol. 24:123-126.
    • (1969) Aust. J. Dairy Technol , vol.24 , pp. 123-126
    • Tucker, V.C.1
  • 116
    • 0000323810 scopus 로고
    • Cyanogenic glycosides and glucosinolates (Mustard oil glucosides)
    • G. W. Butler and R. W. Bailey, London and New York: Academic Press
    • Tupper, B. A. and Reay, P. F. 1973. “Cyanogenic glycosides and glucosinolates (mustard oil glucosides),” in Chemistry and Biochemistry of Herbage, Vol. I, eds. G. W. Butler and R. W. Bailey, London and New York: Academic Press, pp. 447-473.
    • (1973) Chemistry and Biochemistry of Herbage, Vol. I , pp. 447-473
    • Tupper, B.A.1    Reay, P.F.2
  • 117
    • 0032840576 scopus 로고    scopus 로고
    • The role of a sl-casein in the structure of caprine casein micelles
    • Tziboula, A. and Horne, D. S. 1999. The role of a sl-casein in the structure of caprine casein micelles. Int. Dairy J. 9:173-178.
    • (1999) Int. Dairy J , vol.9 , pp. 173-178
    • Tziboula, A.1    Horne, D.S.2
  • 118
    • 0039842514 scopus 로고    scopus 로고
    • Structural changes accompanying ph-induced dissociation of the β-lactoglobulin dimer
    • Uhrinova, S., Smith, M. H., Jameson, G. B., Uhrin, D., Sawyer, L., and Barlow, P. N. 2000. “Structural changes accompanying pH-induced dissociation of the β-lactoglobulin dimer.” Biochemistry. 39:3565-3574.
    • (2000) Biochemistry , vol.39 , pp. 3565-3574
    • Uhrinova, S.1    Smith, M.H.2    Jameson, G.B.3    Uhrin, D.4    Sawyer, L.5    Barlow, P.N.6
  • 120
    • 0346719554 scopus 로고    scopus 로고
    • Inactivation of heat-resistant lipase and protease from
    • Vercet, A., Lopez, P., and Burgos, J. 1997. “Inactivation of heat-resistant lipase and protease from Pseudomonas fluorescens by manothermosonication.” J. Dairy Sci. 80:29-36.
    • (1997) J. Dairy Sci , vol.80 , pp. 29-36
    • Vercet, A.1    Lopez, P.2    Burgos, J.3
  • 121
    • 0040176748 scopus 로고    scopus 로고
    • Application of transgenesis to modifying milk protein composition
    • R. A. S. Welch, D. J. W. Burns, S. R. Davis, A. I. Popay and C. G. Prosser, Wallingford: CAB International
    • Vilotte, J.-L., Soulier, S., Persuy, M.-A., Lepourry, L., Legrain, S., Printz, C., Stinnakre, M.-G., L’Huillier, P., and Mercier, J.-C. 1997. “Application of transgenesis to modifying milk protein composition,” in Milk Composition, Production and Biotechnology, eds. R. A. S. Welch, D. J. W. Burns, S. R. Davis, A. I. Popay and C. G. Prosser, Wallingford: CAB International, pp. 231-242.
    • (1997) Milk Composition, Production And , pp. 231-242
    • Vilotte, J.-L.1    Soulier, S.2    Persuy, M.-A.3    Lepourry, L.4    Legrain, S.5    Printz, C.6    Stinnakre, M.-G.7    L’ Huillier, P.8    Mercier, J.-C.9
  • 122
    • 0032855955 scopus 로고    scopus 로고
    • Antibacterial effects of lactoferricin b
    • Vorland, L. H., Ulvatne, H., Andersen, J., Haukland, H. H., Rekdal, 0., Svendsen, J. S., and Gutteberg, T. J. 1999. “Antibacterial effects of Lactoferricin B.” Scand. J. Infect. Dis. 31:179-184.
    • (1999) J. Infect. Dis , vol.31 , pp. 179-184
    • Vorland, L.H.1    Ulvatne, H.2    Ersen, J.3    Haukland, H.H.4
  • 123
    • 0011655357 scopus 로고
    • Variations in the chemical composition of milk with particular reference to the solids-non-fat. 1. The effect of stage of lactation, season of year and age of cow
    • Waite, R., White, J. C. D., and Robertson, A. 1956. “Variations in the chemical composition of milk with particular reference to the solids-non-fat. 1. The effect of stage of lactation, season of year and age of cow.” J. Dairy Res. 23:65-81.
    • (1956) J. Dairy Res , vol.23 , pp. 65-81
    • Waite, R.1    White, J.C.D.2    Robertson, A.3
  • 124
    • 0039625329 scopus 로고
    • Protein content of skim milk powder varies throughout the year
    • Walley, B. and O’Connor, C. B. 1980. “Protein content of skim milk powder varies throughout the year.” Farm Food Res. 11:82-83.
    • (1980) Farm Food Res , vol.11 , pp. 82-83
    • Walley, B.1    O’ Connor, C.B.2
  • 125
    • 0032818601 scopus 로고    scopus 로고
    • Casein sub-micelles: Do they exist?
    • Walstra, P. 1999. “Casein sub-micelles: Do they exist?” Int. Dairy J. 9:189-192.
    • (1999) Int. Dairy J , vol.9 , pp. 189-192
    • Walstra, P.1
  • 127
    • 0019890187 scopus 로고
    • Effect of chymosin action on the hydrodynamic diameter of casein micelles
    • Walstra, P., Bloomfield, V. A., Wei, G. J., and Jenness, R. 1981. “Effect of chymosin action on the hydrodynamic diameter of casein micelles.” Biochim. Biophys. Acta. 669:258-259.
    • (1981) Biochim. Biophys. Acta , vol.669 , pp. 258-259
    • Walstra, P.1    Bloomfield, V.A.2    Wei, G.J.3    Jenness, R.4
  • 128
    • 0006263578 scopus 로고
    • Proteins of milk
    • N. P. Wong, R. Jenness, M. Keeney, and E. H. Marth, New York: Van Nostrand Reinhold
    • Whitney, R. McL. 1988. “Proteins of milk,” in Fundamentals of Dairy Chemistry, eds. N. P. Wong, R. Jenness, M. Keeney, and E. H. Marth, New York: Van Nostrand Reinhold, pp. 81-169.
    • (1988) Fundamentals of Dairy Chemistry , pp. 81-169
    • Whitney, R.M.1
  • 129
    • 0032114248 scopus 로고    scopus 로고
    • Immunostimulation of murine spleen cells by materials associated with bovine milk protein fractions
    • Wong, K. F., Middleton, N., Montgomery, M., Dey, M., and Carr, R. I. 1998. “Immunostimulation of murine spleen cells by materials associated with bovine milk protein fractions.” J. Dairy Sci. 81:1825-1832.
    • (1998) J. Dairy Sci , vol.81 , pp. 1825-1832
    • Wong, K.F.1    Middleton, N.2    Montgomery, M.3    Dey, M.4    Carr, R.I.5
  • 130
    • 0032479440 scopus 로고    scopus 로고
    • A specific hydrophobic core in the a-lactalbumin molten globule
    • Wu, L. C. and Kim, P. S. 1998. “A specific hydrophobic core in the a-lactalbumin molten globule.” J. Mol. Biology. 280:175-182.
    • (1998) J. Mol. Biology , vol.280 , pp. 175-182
    • Wu, L.C.1    Kim, P.S.2
  • 131
    • 0345313659 scopus 로고    scopus 로고
    • β-factoglobulin binds palmitate within its central cavity
    • Wu, S. Y, Perez, M. D., Puyol, P., and Sawyer, L. 1999. “β-Factoglobulin binds palmitate within its central cavity.” J. Biol. Chem. 274:170-174.
    • (1999) J. Biol. Chem , vol.274 , pp. 170-174
    • Wu, S.Y.1    Perez, M.D.2    Puyol, P.3    Sawyer, L.4
  • 132
    • 0033161658 scopus 로고    scopus 로고
    • Purification and characterization of an antihypertensive peptide from a yogurt-like product fermented by
    • Yamamoto, N., Maeno, M., and Takano, T. 1999. “Purification and characterization of an antihypertensive peptide from a yogurt-like product fermented by Lactobacillus helveticus CPN-4.” J. Dairy Sci. 82:1388-1393.
    • (1999) J. Dairy Sci , vol.82 , pp. 1388-1393
    • Yamamoto, N.1    Maeno, M.2    Takano, T.3
  • 133
    • 0019023470 scopus 로고
    • Activity of xanthine oxidase in dairy products
    • Zikakis, J. P. and Wooters, S. C. 1980. “Activity of xanthine oxidase in dairy products.” J. Dairy Sci. 63:893-904.
    • (1980) J. Dairy Sci , vol.63 , pp. 893-904
    • Zikakis, J.P.1    Wooters, S.C.2
  • 134
    • 0028980267 scopus 로고
    • Casocidin-i: A casein a s2 derived peptide exhibits antibacterial activity
    • Zucht, H.-D., Raida, M., Adermann, K., Magert, H.-J., and Forsmann, W.-G. 1995. “Casocidin-I: a casein a s2 derived peptide exhibits antibacterial activity.” FEBS Letters 372:185-188.
    • (1995) FEBS Letters , vol.372 , pp. 185-188
    • Zucht, H.-D.1    Raida, M.2    Adermann, K.3    Magert, H.-J.4    Forsmann, W.-G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.