메뉴 건너뛰기




Volumn 95, Issue 2, 2012, Pages 549-557

Effect of high-pressure treatment on denaturation of bovine lactoferrin and lactoperoxidase

Author keywords

Denaturation kinetics; High pressure; Lactoferrin; Lactoperoxidase

Indexed keywords

ANTIBODY; LACTOFERRIN; LACTOPEROXIDASE;

EID: 84856158157     PISSN: 00220302     EISSN: 15253198     Source Type: Journal    
DOI: 10.3168/jds.2011-4665     Document Type: Article
Times cited : (38)

References (37)
  • 1
    • 0001430290 scopus 로고    scopus 로고
    • Reaction kinetics of thermal denaturation of whey proteins in heated reconstituted whole milk
    • Anema S.G., McKenna A.B. Reaction kinetics of thermal denaturation of whey proteins in heated reconstituted whole milk. J. Agric. Food Chem. 1996, 44:422-428.
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 422-428
    • Anema, S.G.1    McKenna, A.B.2
  • 2
    • 27144474946 scopus 로고    scopus 로고
    • Denaturation of β-lactoglobulin in pressure-treated skim milk
    • Anema S.G., Stockmann R., Lowe E.K. Denaturation of β-lactoglobulin in pressure-treated skim milk. J. Agric. Food Chem. 2005, 53:7783-7791.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 7783-7791
    • Anema, S.G.1    Stockmann, R.2    Lowe, E.K.3
  • 3
    • 0002507772 scopus 로고
    • ELISA and related enzyme immunoassays
    • IRL Press, Oxford, UK
    • Catty D., Raykundalia C. ELISA and related enzyme immunoassays. Antibodies: A Practical Approach 1989, Vol 2:97-154. IRL Press, Oxford, UK.
    • (1989) Antibodies: A Practical Approach , vol.2 , pp. 97-154
    • Catty, D.1    Raykundalia, C.2
  • 4
    • 0037334653 scopus 로고    scopus 로고
    • Review: Are intrinsic TTIs for thermally processed milk applicable for high-pressure process assessment?
    • Claeys W.L., Indrawati O., Van Loey A.M., Hendrickx M.E. Review: Are intrinsic TTIs for thermally processed milk applicable for high-pressure process assessment?. Innov. Food Sci. Emerg. Technol. 2003, 4:1-14.
    • (2003) Innov. Food Sci. Emerg. Technol. , vol.4 , pp. 1-14
    • Claeys, W.L.1    Indrawati, O.2    Van Loey, A.M.3    Hendrickx, M.E.4
  • 5
    • 0001652476 scopus 로고
    • Thermodynamic approach to kinetics of β-lactoglobulin denaturation in heated skim milk and sweet whey
    • Dannenberg F., Kessler H.G. Thermodynamic approach to kinetics of β-lactoglobulin denaturation in heated skim milk and sweet whey. Milchwissenschaft 1988, 43:139-142.
    • (1988) Milchwissenschaft , vol.43 , pp. 139-142
    • Dannenberg, F.1    Kessler, H.G.2
  • 6
    • 41549152615 scopus 로고    scopus 로고
    • Lactoferrin: The conductor of the immunological system?
    • Nova Science Publishers, New York, NY, B.A. Veskler (Ed.)
    • Farnaud S., Evans R.W. Lactoferrin: The conductor of the immunological system?. New Research on Immunology 2005, 47-76. Nova Science Publishers, New York, NY. B.A. Veskler (Ed.).
    • (2005) New Research on Immunology , pp. 47-76
    • Farnaud, S.1    Evans, R.W.2
  • 7
    • 77956835933 scopus 로고    scopus 로고
    • Effect of bovine lactoferrin addition to milk in yogurt manufacturing
    • Franco I., Castillo E., Pérez M.D., Calvo M., Sánchez L. Effect of bovine lactoferrin addition to milk in yogurt manufacturing. J. Dairy Sci. 2010, 93:4480-4489.
    • (2010) J. Dairy Sci. , vol.93 , pp. 4480-4489
    • Franco, I.1    Castillo, E.2    Pérez, M.D.3    Calvo, M.4    Sánchez, L.5
  • 8
    • 0037465606 scopus 로고    scopus 로고
    • The lactoperoxidase system increases efficacy of high-pressure inactivation of foodborne bacteria
    • García-Graells C., Van Opstal I., Vanmuysen S.C.M., Michiels C.W. The lactoperoxidase system increases efficacy of high-pressure inactivation of foodborne bacteria. Int. J. Food Microbiol. 2003, 81:211-221.
    • (2003) Int. J. Food Microbiol. , vol.81 , pp. 211-221
    • García-Graells, C.1    Van Opstal, I.2    Vanmuysen, S.C.M.3    Michiels, C.W.4
  • 9
    • 0030521681 scopus 로고    scopus 로고
    • Reaction kinetics of pressure-induced denaturation of whey proteins
    • Hinrichs J., Rademacher B., Kessler H.G. Reaction kinetics of pressure-induced denaturation of whey proteins. Milchwissenschaft 1996, 51:504-509.
    • (1996) Milchwissenschaft , vol.51 , pp. 504-509
    • Hinrichs, J.1    Rademacher, B.2    Kessler, H.G.3
  • 10
    • 10044295812 scopus 로고    scopus 로고
    • High pressure-induced denaturation of α-lactalbumin and β-lactoglobulin in bovine milk and whey: A possible mechanism
    • Huppertz T., Fox P.F., Kelly A.L. High pressure-induced denaturation of α-lactalbumin and β-lactoglobulin in bovine milk and whey: A possible mechanism. J. Dairy Res. 2004, 71:489-495.
    • (2004) J. Dairy Res. , vol.71 , pp. 489-495
    • Huppertz, T.1    Fox, P.F.2    Kelly, A.L.3
  • 11
    • 0036066607 scopus 로고    scopus 로고
    • Effects of high-pressure on constituents and properties of milk
    • Huppertz T., Kelly A.L., Fox P.F. Effects of high-pressure on constituents and properties of milk. Int. Dairy J. 2002, 12:561-572.
    • (2002) Int. Dairy J. , vol.12 , pp. 561-572
    • Huppertz, T.1    Kelly, A.L.2    Fox, P.F.3
  • 12
    • 39149126312 scopus 로고    scopus 로고
    • Analysis of denaturation of bovine IgG by heat and high pressure using an optical biosensor
    • Indyk H.E., Williams J.W., Patel H.A. Analysis of denaturation of bovine IgG by heat and high pressure using an optical biosensor. Int. Dairy J. 2008, 18:359-366.
    • (2008) Int. Dairy J. , vol.18 , pp. 359-366
    • Indyk, H.E.1    Williams, J.W.2    Patel, H.A.3
  • 13
    • 0006253440 scopus 로고
    • Retardation of protein denaturation by high pressure
    • Johnson F.H., Campbell D.H. Retardation of protein denaturation by high pressure. J. Cell. Comp. Physiol. 1945, 26:43-46.
    • (1945) J. Cell. Comp. Physiol. , vol.26 , pp. 43-46
    • Johnson, F.H.1    Campbell, D.H.2
  • 14
    • 33646345878 scopus 로고    scopus 로고
    • Functional improvement of milk whey proteins induced by high hydrostatic pressure
    • López-Fandiño R. Functional improvement of milk whey proteins induced by high hydrostatic pressure. Crit. Rev. Food Sci. Nutr. 2006, 46:351-363.
    • (2006) Crit. Rev. Food Sci. Nutr. , vol.46 , pp. 351-363
    • López-Fandiño, R.1
  • 15
    • 0035524079 scopus 로고    scopus 로고
    • Effect of temperature and/or pressure on lactoperoxidase activity in bovine milk and acid whey
    • Ludikhuyze L., Claeys W., Hendrickx M. Effect of temperature and/or pressure on lactoperoxidase activity in bovine milk and acid whey. J. Dairy Res. 2001, 68:625-637.
    • (2001) J. Dairy Res. , vol.68 , pp. 625-637
    • Ludikhuyze, L.1    Claeys, W.2    Hendrickx, M.3
  • 16
    • 0030706011 scopus 로고    scopus 로고
    • Kinetic and thermodynamic parameters for heat denaturation of bovine milk IgG, IgA and IgM
    • Mainer G., Sánchez L., Ena J.M., Calvo M. Kinetic and thermodynamic parameters for heat denaturation of bovine milk IgG, IgA and IgM. J. Food Sci. 1997, 62:1034-1038.
    • (1997) J. Food Sci. , vol.62 , pp. 1034-1038
    • Mainer, G.1    Sánchez, L.2    Ena, J.M.3    Calvo, M.4
  • 17
    • 0037286903 scopus 로고    scopus 로고
    • Effect of heat treatment on bovine lactoperoxidase activity in skim milk: kinetic and thermodynamic analysis
    • Marín E., Sánchez L., Pérez M.D., Puyol P., Calvo M. Effect of heat treatment on bovine lactoperoxidase activity in skim milk: kinetic and thermodynamic analysis. J. Food Sci. 2003, 68:89-93.
    • (2003) J. Food Sci. , vol.68 , pp. 89-93
    • Marín, E.1    Sánchez, L.2    Pérez, M.D.3    Puyol, P.4    Calvo, M.5
  • 18
    • 0035916960 scopus 로고    scopus 로고
    • High pressure increases bactericidal activity and spectrum of lactoferrin, lactoferricin and nisin
    • Masschalck B., Van Houdt R., Michiels C.W. High pressure increases bactericidal activity and spectrum of lactoferrin, lactoferricin and nisin. Int. J. Food Microbiol. 2001, 64:325-332.
    • (2001) Int. J. Food Microbiol. , vol.64 , pp. 325-332
    • Masschalck, B.1    Van Houdt, R.2    Michiels, C.W.3
  • 19
    • 1842723360 scopus 로고    scopus 로고
    • Lactoperoxidase
    • CRC Press, Boca Raton, FL, S. Naidu (Ed.)
    • Naidu A.S. Lactoperoxidase. Natural Food Antimicrobial Systems A 2000, 103-132. CRC Press, Boca Raton, FL. S. Naidu (Ed.).
    • (2000) Natural Food Antimicrobial Systems A , pp. 103-132
    • Naidu, A.S.1
  • 20
    • 0030456545 scopus 로고    scopus 로고
    • Lactoperoxidase suppresses acid production in yoghurt during storage under refrigeration
    • Nakada M., Dosako S., Hirano R., Oooka M., Nakajima I. Lactoperoxidase suppresses acid production in yoghurt during storage under refrigeration. Int. Dairy J. 1996, 6:33-42.
    • (1996) Int. Dairy J. , vol.6 , pp. 33-42
    • Nakada, M.1    Dosako, S.2    Hirano, R.3    Oooka, M.4    Nakajima, I.5
  • 21
    • 17444399413 scopus 로고    scopus 로고
    • Effects of heat and high-hydrostatic pressure on the aggregarion of whey proteins concentrate solutions
    • Patel H.A., Singh H., Anema S.G., Creamer L.K. Effects of heat and high-hydrostatic pressure on the aggregarion of whey proteins concentrate solutions. Food New Zealand 2004, 4:29-35.
    • (2004) Food New Zealand , vol.4 , pp. 29-35
    • Patel, H.A.1    Singh, H.2    Anema, S.G.3    Creamer, L.K.4
  • 22
    • 0038039639 scopus 로고
    • The lactoperoxidase system of bovine and human milk
    • Elsevier Applied Science, London, UK, D.S. Robinson, N.A.M. Eskin (Eds.)
    • Pruitt K.M., Kamau D.N. The lactoperoxidase system of bovine and human milk. Oxidative Enzymes in Foods 1991, 133-174. Elsevier Applied Science, London, UK. D.S. Robinson, N.A.M. Eskin (Eds.).
    • (1991) Oxidative Enzymes in Foods , pp. 133-174
    • Pruitt, K.M.1    Kamau, D.N.2
  • 23
    • 0001761268 scopus 로고    scopus 로고
    • High pressure inactivation of microorganisms and enzymes in milk and milk products
    • Leuven University Press, Leuven, Belgium, K. Heremans (Ed.)
    • Rademacher B., Kessler H.G. High pressure inactivation of microorganisms and enzymes in milk and milk products. High Pressure Research in the Biosciences and Biotechnology 1997, 291-293. Leuven University Press, Leuven, Belgium. K. Heremans (Ed.).
    • (1997) High Pressure Research in the Biosciences and Biotechnology , pp. 291-293
    • Rademacher, B.1    Kessler, H.G.2
  • 25
    • 0037171140 scopus 로고    scopus 로고
    • Revisiting volume changes in pressure-induced protein unfolding
    • Royer C.A. Revisiting volume changes in pressure-induced protein unfolding. Biochim. Biophys. Acta 2002, 1595:201-209.
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 201-209
    • Royer, C.A.1
  • 27
    • 16244397401 scopus 로고    scopus 로고
    • Significance of the lactoperoxidase system in the dairy industry and its potential applications: A review
    • Seifu E., Buysb E.M., Donkin E.F. Significance of the lactoperoxidase system in the dairy industry and its potential applications: A review. Trends Food Sci. Technol. 2005, 16:137-154.
    • (2005) Trends Food Sci. Technol. , vol.16 , pp. 137-154
    • Seifu, E.1    Buysb, E.M.2    Donkin, E.F.3
  • 28
    • 29344466959 scopus 로고    scopus 로고
    • Milk biologically active components as nutraceuticals: A review
    • Severin S., Wenshui X. Milk biologically active components as nutraceuticals: A review. Crit. Rev. Food Sci. Nutr. 2005, 45:645-656.
    • (2005) Crit. Rev. Food Sci. Nutr. , vol.45 , pp. 645-656
    • Severin, S.1    Wenshui, X.2
  • 30
    • 0035516988 scopus 로고    scopus 로고
    • Functional foods, probiotics and prebiotics
    • Shah N. Functional foods, probiotics and prebiotics. Food Technol. 2001, 55:46-53.
    • (2001) Food Technol. , vol.55 , pp. 46-53
    • Shah, N.1
  • 31
    • 2442688971 scopus 로고    scopus 로고
    • Heat stability of milk
    • Singh H. Heat stability of milk. Int. J. Dairy Technol. 2004, 57:111-119.
    • (2004) Int. J. Dairy Technol. , vol.57 , pp. 111-119
    • Singh, H.1
  • 34
    • 33748325910 scopus 로고    scopus 로고
    • Lactoferrin research, technology and applications
    • Wakabayashi H., Yamauchi K., Takase M. Lactoferrin research, technology and applications. Int. Dairy J. 2006, 16:1241-1251.
    • (2006) Int. Dairy J. , vol.16 , pp. 1241-1251
    • Wakabayashi, H.1    Yamauchi, K.2    Takase, M.3
  • 35
    • 11144234506 scopus 로고    scopus 로고
    • Effects of high-pressure processing at low temperature on the molecular structure and surface properties of β-lactoglobulin
    • Walker M.K., Farkas D.F., Anderson S.R., Meunier-Goddik L. Effects of high-pressure processing at low temperature on the molecular structure and surface properties of β-lactoglobulin. J. Agric. Food Chem. 2004, 52:8230-8235.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 8230-8235
    • Walker, M.K.1    Farkas, D.F.2    Anderson, S.R.3    Meunier-Goddik, L.4
  • 36
    • 28344447990 scopus 로고    scopus 로고
    • Multifunctional roles of lactoferrin: A critical overview
    • Ward P.P., Paz E., Conneely O.M. Multifunctional roles of lactoferrin: A critical overview. Cell. Mol. Life Sci. 2005, 62:2540-2548.
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 2540-2548
    • Ward, P.P.1    Paz, E.2    Conneely, O.M.3
  • 37
    • 29744433465 scopus 로고    scopus 로고
    • Effect of heat treatment on denaturation of bovine alpha-lactalbumin: Determination of kinetic and thermodynamic parameters
    • Wehbi Z., Pérez M.D., Sanchez L., Pocovi C., Barbana C., Calvo M. Effect of heat treatment on denaturation of bovine alpha-lactalbumin: Determination of kinetic and thermodynamic parameters. J. Agric. Food Chem. 2005, 53:9730-9736.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 9730-9736
    • Wehbi, Z.1    Pérez, M.D.2    Sanchez, L.3    Pocovi, C.4    Barbana, C.5    Calvo, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.