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Volumn 92, Issue 7, 2012, Pages 1432-1440

One-step method for isolation and purification of native β-lactoglobulin from bovine whey

Author keywords

Anion exchange chromatography; Isolation; Native lactoglobulin; Purification

Indexed keywords

ENZYME; ISOPROTEIN; LACTOGLOBULIN; MILK PROTEIN; WHEY PROTEIN;

EID: 84859419583     PISSN: 00225142     EISSN: 10970010     Source Type: Journal    
DOI: 10.1002/jsfa.4722     Document Type: Article
Times cited : (23)

References (34)
  • 1
    • 0022140116 scopus 로고
    • Functionality of heated milk proteins in dairy and related foods
    • Morr CV, Functionality of heated milk proteins in dairy and related foods. J Dairy Sci 68: 2773-2781 (1985).
    • (1985) J Dairy Sci , vol.68 , pp. 2773-2781
    • Morr, C.V.1
  • 4
    • 0034578634 scopus 로고    scopus 로고
    • Molecular differences in the formation and structure of fine-stranded and particulate beta-lactoglobulin gels
    • Lefevre T and Subirade M, Molecular differences in the formation and structure of fine-stranded and particulate beta-lactoglobulin gels. Biopolymers 54: 578-586 (2000).
    • (2000) Biopolymers , vol.54 , pp. 578-586
    • Lefevre, T.1    Subirade, M.2
  • 5
    • 0142229534 scopus 로고    scopus 로고
    • Effect of pre-heating on the foaming properties of whey protein isolate using a membrane foaming apparatus
    • Bals A and Kulozik U, Effect of pre-heating on the foaming properties of whey protein isolate using a membrane foaming apparatus. Int Dairy J 13: 903-908 (2003).
    • (2003) Int Dairy J , vol.13 , pp. 903-908
    • Bals, A.1    Kulozik, U.2
  • 6
    • 8644288237 scopus 로고    scopus 로고
    • Cold gelation of beta-lactoglobulin oil-in-water emulsions
    • Line VLS, Remondetto GE and Subirade M, Cold gelation of beta-lactoglobulin oil-in-water emulsions. Food Hydrocolloids 19: 269-278 (2005).
    • (2005) Food Hydrocolloids , vol.19 , pp. 269-278
    • Line, V.L.S.1    Remondetto, G.E.2    Subirade, M.3
  • 7
    • 20444486236 scopus 로고    scopus 로고
    • Humoral and cellular responses to cow's milk proteins in patients with milk-induced IgE-mediated and non-IgE-mediated disorders
    • Shek LPC, Bardina L, Castro R, Sampson HA and Beyer K, Humoral and cellular responses to cow's milk proteins in patients with milk-induced IgE-mediated and non-IgE-mediated disorders. Allergy 60: 912-919 (2005).
    • (2005) Allergy , vol.60 , pp. 912-919
    • Shek, L.P.C.1    Bardina, L.2    Castro, R.3    Sampson, H.A.4    Beyer, K.5
  • 8
    • 0030853218 scopus 로고    scopus 로고
    • Method for the isolation of bovine beta-lactoglobulin from a cheese whey protein fraction and physicochemical characterization of the purified product
    • Caessens PWJR, Visser S and Gruppen H, Method for the isolation of bovine beta-lactoglobulin from a cheese whey protein fraction and physicochemical characterization of the purified product. Int Dairy J 7: 229-235 (1997).
    • (1997) Int Dairy J , vol.7 , pp. 229-235
    • Caessens, P.W.J.R.1    Visser, S.2    Gruppen, H.3
  • 9
    • 0034467427 scopus 로고    scopus 로고
    • A large-scale isolation of native beta-lactoglobulin: characterization of physicochemical properties and comparison with other methods
    • Konrad G, Lieske B and Faber W, A large-scale isolation of native beta-lactoglobulin: characterization of physicochemical properties and comparison with other methods. Int Dairy J 10: 713-721 (2000).
    • (2000) Int Dairy J , vol.10 , pp. 713-721
    • Konrad, G.1    Lieske, B.2    Faber, W.3
  • 10
    • 1542680883 scopus 로고    scopus 로고
    • Separation and characterization of beta-lactoglobulin and alpha-lactalbumin from whey and whey protein preparations
    • Alomirah HF and Alli I, Separation and characterization of beta-lactoglobulin and alpha-lactalbumin from whey and whey protein preparations. Int Dairy J 14: 411-419 (2004).
    • (2004) Int Dairy J , vol.14 , pp. 411-419
    • Alomirah, H.F.1    Alli, I.2
  • 11
    • 36248952115 scopus 로고    scopus 로고
    • An improved method for isolation of beta-lactoglobulin
    • Lozano JM, Giraldo GI and Romero CM, An improved method for isolation of beta-lactoglobulin. Int Dairy J 18: 55-63 (2008).
    • (2008) Int Dairy J , vol.18 , pp. 55-63
    • Lozano, J.M.1    Giraldo, G.I.2    Romero, C.M.3
  • 12
    • 0038128669 scopus 로고    scopus 로고
    • Isolation of alpha-lactalbumin, beta-lactoglobulin, and bovine serum albumin from cow's milk using gel filtration and anion-exchange chromatography including evaluation of their antigenicity
    • Neyestani TR, Djalali M and Pezeshki M, Isolation of alpha-lactalbumin, beta-lactoglobulin, and bovine serum albumin from cow's milk using gel filtration and anion-exchange chromatography including evaluation of their antigenicity. Protein Expr Purif 29: 202-208 (2003).
    • (2003) Protein Expr Purif , vol.29 , pp. 202-208
    • Neyestani, T.R.1    Djalali, M.2    Pezeshki, M.3
  • 13
    • 0034536951 scopus 로고    scopus 로고
    • Isolation of lactoperoxidase, lactoferrin, alpha-lactalbumin, beta-lactoglobulin B and beta-lactoglobulin A from bovine rennet whey using ion exchange chromatography
    • Ye X, Yoshida S and Ng TB, Isolation of lactoperoxidase, lactoferrin, alpha-lactalbumin, beta-lactoglobulin B and beta-lactoglobulin A from bovine rennet whey using ion exchange chromatography. Int J Biochem Cell Biol 32: 1143-1150 (2000).
    • (2000) Int J Biochem Cell Biol , vol.32 , pp. 1143-1150
    • Ye, X.1    Yoshida, S.2    Ng, T.B.3
  • 14
    • 0036651792 scopus 로고    scopus 로고
    • Scale-up of native beta-lactoglobulin affinity separation process
    • Vyas HK, Izco JM and Jimenez-Flores R, Scale-up of native beta-lactoglobulin affinity separation process. J Dairy Sci 85: 1639-1645 (2002).
    • (2002) J Dairy Sci , vol.85 , pp. 1639-1645
    • Vyas, H.K.1    Izco, J.M.2    Jimenez-Flores, R.3
  • 15
    • 0022624246 scopus 로고
    • Allergen-specific IgE antibodies against antigenic components in cow's milk and milk substitutes
    • Gjesing B, Osterballe O, Schwartz B, Wahn U and Lowenstein H, Allergen-specific IgE antibodies against antigenic components in cow's milk and milk substitutes. Allergy 41: 51-56 (1986).
    • (1986) Allergy , vol.41 , pp. 51-56
    • Gjesing, B.1    Osterballe, O.2    Schwartz, B.3    Wahn, U.4    Lowenstein, H.5
  • 16
    • 0022307525 scopus 로고
    • Rapid separation of milk whey proteins by anion exchange chromatography
    • Manji B, Hill A, Kakuda Y and Irvine DM, Rapid separation of milk whey proteins by anion exchange chromatography. J Dairy Sci 68: 3176-3179 (1985).
    • (1985) J Dairy Sci , vol.68 , pp. 3176-3179
    • Manji, B.1    Hill, A.2    Kakuda, Y.3    Irvine, D.M.4
  • 17
    • 28444472469 scopus 로고    scopus 로고
    • Enzyme-aided modification of chicken-breast myofibril proteins: effect of laccase and transglutaminase on gelation and thermal stability
    • Lantto R, Puolanne E, Kalkkinen N, Buchert J and Autio K, Enzyme-aided modification of chicken-breast myofibril proteins: effect of laccase and transglutaminase on gelation and thermal stability. J Agric Food Chem 53: 9231-9237 (2005).
    • (2005) J Agric Food Chem , vol.53 , pp. 9231-9237
    • Lantto, R.1    Puolanne, E.2    Kalkkinen, N.3    Buchert, J.4    Autio, K.5
  • 18
    • 0037009169 scopus 로고    scopus 로고
    • Investigations on the laccase-catalyzed polymerization of lignin model compounds using size-exclusion HPLC
    • Rittstieg K, Suurnakki A, Suortti T, Kruus K, Guebitz G and Buchert J, Investigations on the laccase-catalyzed polymerization of lignin model compounds using size-exclusion HPLC. Enzyme Microb Technol 31: 403-410 (2002).
    • (2002) Enzyme Microb Technol , vol.31 , pp. 403-410
    • Rittstieg, K.1    Suurnakki, A.2    Suortti, T.3    Kruus, K.4    Guebitz, G.5    Buchert, J.6
  • 19
    • 33748327047 scopus 로고    scopus 로고
    • Production and characterization of a secreted, C-terminally processed tyrosinase from the filamentous fungus Trichoderma reesei
    • Selinheimo E, Saloheimo M, Ahola E, Westerholm-Parvinen A, Kalkkinen N, Buchert J, et al, Production and characterization of a secreted, C-terminally processed tyrosinase from the filamentous fungus Trichoderma reesei. FEBS J 273: 4322-4335 (2006).
    • (2006) FEBS J , vol.273 , pp. 4322-4335
    • Selinheimo, E.1    Saloheimo, M.2    Ahola, E.3    Westerholm-Parvinen, A.4    Kalkkinen, N.5    Buchert, J.6
  • 20
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace CN, Vajdos F, Fee L, Grimsley G and Gray T, How to measure and predict the molar absorption coefficient of a protein. Protein Sci 4: 2411-2423 (1995).
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK, Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0033562629 scopus 로고    scopus 로고
    • Analyzing protein circular dichroism spectra for accurate secondary structures
    • Johnson WC, Analyzing protein circular dichroism spectra for accurate secondary structures. Protein Struct Funct Genet 35: 307-312 (1999).
    • (1999) Protein Struct Funct Genet , vol.35 , pp. 307-312
    • Johnson, W.C.1
  • 24
    • 0015878020 scopus 로고
    • Immunization, isolation of immunoglobulins, estimation of antibody titre
    • Harboe N and Ingild A, Immunization, isolation of immunoglobulins, estimation of antibody titre. Scand J Immunol 2(Suppl. 1): 161-164 (1973).
    • (1973) Scand J Immunol , vol.2 , Issue.SUPPL. 1 , pp. 161-164
    • Harboe, N.1    Ingild, A.2
  • 25
    • 0016166178 scopus 로고
    • Transient state isoelectric focusing. Measurement of minimal focusing time
    • Catsimpoolas N, Campbell BE and Griffith AL, Transient state isoelectric focusing. Measurement of minimal focusing time. Biochim Biophys Acta 351: 196-204 (1974).
    • (1974) Biochim Biophys Acta , vol.351 , pp. 196-204
    • Catsimpoolas, N.1    Campbell, B.E.2    Griffith, A.L.3
  • 28
    • 44349164116 scopus 로고    scopus 로고
    • Formation of protein-oligosaccharide conjugates by laccase and tyrosinase
    • Selinheimo E, Lampila P, Mattinen ML and Buchert J, Formation of protein-oligosaccharide conjugates by laccase and tyrosinase. J Agric Food Chem 56: 3118-3128 (2008).
    • (2008) J Agric Food Chem , vol.56 , pp. 3118-3128
    • Selinheimo, E.1    Lampila, P.2    Mattinen, M.L.3    Buchert, J.4
  • 29
    • 0031033309 scopus 로고    scopus 로고
    • Effects of redox potential and hydroxide inhibition on the pH activity profile of fungal laccases
    • Xu F, Effects of redox potential and hydroxide inhibition on the pH activity profile of fungal laccases. J Biol Chem 272: 924-928 (1997).
    • (1997) J Biol Chem , vol.272 , pp. 924-928
    • Xu, F.1
  • 30
    • 0034684161 scopus 로고    scopus 로고
    • The core lipocalin, bovine beta-lactoglobulin
    • Sawyer L and Kontopidis G, The core lipocalin, bovine beta-lactoglobulin. Biochim Biophys Acta 1482: 136-148 (2000).
    • (2000) Biochim Biophys Acta , vol.1482 , pp. 136-148
    • Sawyer, L.1    Kontopidis, G.2
  • 31
    • 0001497241 scopus 로고
    • The reversible transformation of b-lactoglobulin at pH 7.5
    • Tanford C, Bunville LG and Nozaki YJ, The reversible transformation of b-lactoglobulin at pH 7.5. J Am Chem Soc 81: 4032-4036 (1959).
    • (1959) J Am Chem Soc , vol.81 , pp. 4032-4036
    • Tanford, C.1    Bunville, L.G.2    Nozaki, Y.J.3
  • 32
    • 0035290424 scopus 로고    scopus 로고
    • Mild isolation procedure discloses new protein structural properties of beta-lactoglobulin
    • De Jongh HH, Groneveld T and de Groot J, Mild isolation procedure discloses new protein structural properties of beta-lactoglobulin. J Dairy Sci 84: 562-571 (2001).
    • (2001) J Dairy Sci , vol.84 , pp. 562-571
    • De Jongh, H.H.1    Groneveld, T.2    de Groot, J.3
  • 33
    • 0031202714 scopus 로고    scopus 로고
    • Preparative-scale fractionation of bovine, caprine and ovine whey proteins by gel permeation chromatography
    • Felipe X and Law AJR, Preparative-scale fractionation of bovine, caprine and ovine whey proteins by gel permeation chromatography. J Dairy Res 64: 459-464 (1997).
    • (1997) J Dairy Res , vol.64 , pp. 459-464
    • Felipe, X.1    Law, A.J.R.2
  • 34
    • 0000808259 scopus 로고
    • Beta-lactoglobulin separation from whey protein isolate on a large scale
    • Mate JI and Krochta JM, Beta-lactoglobulin separation from whey protein isolate on a large scale. J Food Sci 59: 1111-1114 (1994).
    • (1994) J Food Sci , vol.59 , pp. 1111-1114
    • Mate, J.I.1    Krochta, J.M.2


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