메뉴 건너뛰기




Volumn 64, Issue , 2017, Pages 22-30

Mild thermal treatment and in-vitro digestion of three forms of bovine lactoferrin: Effects on functional properties

Author keywords

[No Author keywords available]

Indexed keywords

ANTIOXIDANTS; BINS; HYDROLYSIS; MAMMALS; PEPTIDES;

EID: 84992481955     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.idairyj.2016.09.001     Document Type: Article
Times cited : (46)

References (48)
  • 2
    • 3342963515 scopus 로고    scopus 로고
    • Lactoferrin and iron: Structural and dynamic aspects of binding and release
    • Baker, H.M., Baker, E.N., Lactoferrin and iron: Structural and dynamic aspects of binding and release. Biometals 17 (2004), 209–216.
    • (2004) Biometals , vol.17 , pp. 209-216
    • Baker, H.M.1    Baker, E.N.2
  • 4
    • 0032893748 scopus 로고    scopus 로고
    • Lactoferrin: A multifunctional glycoprotein involved in the modulation of the inflammatory process
    • Baveye, S., Elass, E., Mazurier, J., Spik, G., Legrand, D., Lactoferrin: A multifunctional glycoprotein involved in the modulation of the inflammatory process. Clinical Chemistry and Laboratory Medicine 37 (1999), 281–286.
    • (1999) Clinical Chemistry and Laboratory Medicine , vol.37 , pp. 281-286
    • Baveye, S.1    Elass, E.2    Mazurier, J.3    Spik, G.4    Legrand, D.5
  • 5
    • 84879486580 scopus 로고    scopus 로고
    • Physico-chemical properties of different forms of bovine lactoferrin
    • Bokkhim, H., Bansal, N., Grøndahl, L., Bhandari, B., Physico-chemical properties of different forms of bovine lactoferrin. Food Chemistry 141 (2013), 3007–3013.
    • (2013) Food Chemistry , vol.141 , pp. 3007-3013
    • Bokkhim, H.1    Bansal, N.2    Grøndahl, L.3    Bhandari, B.4
  • 6
    • 84937035270 scopus 로고    scopus 로고
    • In vitro digestion of different forms of bovine lactoferrin encapsulated in alginate micro-gel particles
    • Bokkhim, H., Bansal, N., Grøndahl, L., Bhandari, B., In vitro digestion of different forms of bovine lactoferrin encapsulated in alginate micro-gel particles. Food Hydrocolloids 52 (2016), 231–242.
    • (2016) Food Hydrocolloids , vol.52 , pp. 231-242
    • Bokkhim, H.1    Bansal, N.2    Grøndahl, L.3    Bhandari, B.4
  • 7
    • 33847380572 scopus 로고    scopus 로고
    • Impacts of thermal pre-treatments on the semi-continuous anaerobic digestion of waste activated sludge
    • Bougrier, C., Delgenes, J.P., Carrere, H., Impacts of thermal pre-treatments on the semi-continuous anaerobic digestion of waste activated sludge. Biochemical Engineering Journal 34 (2007), 20–27.
    • (2007) Biochemical Engineering Journal , vol.34 , pp. 20-27
    • Bougrier, C.1    Delgenes, J.P.2    Carrere, H.3
  • 9
    • 0028658413 scopus 로고
    • The role of lactoferrin as an anti-inflammatory molecule
    • H.T. William B. Lonnerdal V.S. Rumball Plenum Press New York, NY, USA
    • Britigan, B.E., Serody, J.S., Cohen, M.S., The role of lactoferrin as an anti-inflammatory molecule. William, H.T., Lonnerdal, B., Rumball, V.S., (eds.) Lactoferrin: Structure and function, 1994, Plenum Press, New York, NY, USA, 143–156.
    • (1994) Lactoferrin: Structure and function , pp. 143-156
    • Britigan, B.E.1    Serody, J.S.2    Cohen, M.S.3
  • 10
    • 84992531149 scopus 로고    scopus 로고
    • U.S. Patent No. 8,999,923
    • US Patent and Trademark Office Washington, DC
    • Cao, L., Maas, H., U.S. Patent No. 8,999,923. 2015, US Patent and Trademark Office, Washington, DC.
    • (2015)
    • Cao, L.1    Maas, H.2
  • 11
    • 84896830875 scopus 로고    scopus 로고
    • Microfluidic chip electrophoresis investigation of major milk proteins: Study of buffer effects and quantitative approaching
    • Costa, F.F., Brito, M.A.V.P., Furtado, M.A.M., Martins, M.F., de Oliveira, M.A.L., de Castro Barra, P.M., et al. Microfluidic chip electrophoresis investigation of major milk proteins: Study of buffer effects and quantitative approaching. Analytical Methods 6 (2014), 1666–1673.
    • (2014) Analytical Methods , vol.6 , pp. 1666-1673
    • Costa, F.F.1    Brito, M.A.V.P.2    Furtado, M.A.M.3    Martins, M.F.4    de Oliveira, M.A.L.5    de Castro Barra, P.M.6
  • 12
    • 84867593337 scopus 로고    scopus 로고
    • Impact of dietary fibers on the properties and proteolytic digestibility of lactoferrin nano-particles
    • David-Birman, T., Mackie, A., Lesmes, U., Impact of dietary fibers on the properties and proteolytic digestibility of lactoferrin nano-particles. Food Hydrocolloids 31 (2013), 33–41.
    • (2013) Food Hydrocolloids , vol.31 , pp. 33-41
    • David-Birman, T.1    Mackie, A.2    Lesmes, U.3
  • 13
    • 79958699963 scopus 로고    scopus 로고
    • Lactoferrin in relation to biological functions and applications: A review
    • EI-Loly, M.M., Mahfouz, M.B., Lactoferrin in relation to biological functions and applications: A review. International Journal of Dairy Science 6 (2011), 79–111.
    • (2011) International Journal of Dairy Science , vol.6 , pp. 79-111
    • EI-Loly, M.M.1    Mahfouz, M.B.2
  • 14
    • 0029399194 scopus 로고
    • Preparation of apo lactoferrin with a very low iron saturation
    • Feng, M., Van Der Does, L., Bantjes, A., Preparation of apo lactoferrin with a very low iron saturation. Journal of Dairy Science 78 (1995), 2352–2357.
    • (1995) Journal of Dairy Science , vol.78 , pp. 2352-2357
    • Feng, M.1    Van Der Does, L.2    Bantjes, A.3
  • 18
    • 48849088860 scopus 로고    scopus 로고
    • Studies of the structure of multiferric ion-bound lactoferrin: A new antianemic edible material
    • Hu, F., Pan, F., Sawano, Y., Makino, T., Kakehi, Y., Komiyama, M., et al. Studies of the structure of multiferric ion-bound lactoferrin: A new antianemic edible material. International Dairy Journal 18 (2008), 1051–1056.
    • (2008) International Dairy Journal , vol.18 , pp. 1051-1056
    • Hu, F.1    Pan, F.2    Sawano, Y.3    Makino, T.4    Kakehi, Y.5    Komiyama, M.6
  • 20
  • 21
    • 33747855587 scopus 로고    scopus 로고
    • A reference database for circular dichroism spectroscopy covering fold and secondary structure space
    • Lees, J.G., Miles, A.J., Wien, F., Wallace, B.A., A reference database for circular dichroism spectroscopy covering fold and secondary structure space. Bioinformatics 22 (2006), 1955–1962.
    • (2006) Bioinformatics , vol.22 , pp. 1955-1962
    • Lees, J.G.1    Miles, A.J.2    Wien, F.3    Wallace, B.A.4
  • 22
    • 0029126185 scopus 로고
    • Lactoferrin: A general review
    • Levay, P.F., Viljoen, M., Lactoferrin: A general review. Haematologica 80 (1995), 252–267.
    • (1995) Haematologica , vol.80 , pp. 252-267
    • Levay, P.F.1    Viljoen, M.2
  • 23
    • 0034456721 scopus 로고    scopus 로고
    • Oxidation of methionine in proteins: Roles in antioxidant defense and cellular regulation
    • Levine, R.L., Moskovitz, J., Stadtman, E.R., Oxidation of methionine in proteins: Roles in antioxidant defense and cellular regulation. IUBMB Life 50 (2000), 301–307.
    • (2000) IUBMB Life , vol.50 , pp. 301-307
    • Levine, R.L.1    Moskovitz, J.2    Stadtman, E.R.3
  • 24
    • 62749163083 scopus 로고    scopus 로고
    • Micronutrient transfer: Infant absorption
    • G.R. Goldberg A. Prentice A. Prentice S. Filteau K. Simondon Plenum Press New York, NY, USA
    • Lönnerdal, B., Kelleher, S.L., Micronutrient transfer: Infant absorption. Goldberg, G.R., Prentice, A., Prentice, A., Filteau, S., Simondon, K., (eds.) Breast-feeding: Early influences on later health, 2009, Plenum Press, New York, NY, USA, 29–40.
    • (2009) Breast-feeding: Early influences on later health , pp. 29-40
    • Lönnerdal, B.1    Kelleher, S.L.2
  • 27
  • 28
    • 0025674182 scopus 로고
    • cDNA and protein sequence of bovine lactoferrin
    • Mead, P.E., Tweedie, J.W., cDNA and protein sequence of bovine lactoferrin. Nucleic Acids Research, 18, 1990, 7167.
    • (1990) Nucleic Acids Research , vol.18 , pp. 7167
    • Mead, P.E.1    Tweedie, J.W.2
  • 29
    • 0037051529 scopus 로고    scopus 로고
    • Effects of natural phenolic compounds on the antioxidant activity of lactoferrin in liposomes and oil-in-water emulsions
    • Medina, I., Tombo, I., Satué-Gracia, M.T., German, J.B., Frankel, E.N., Effects of natural phenolic compounds on the antioxidant activity of lactoferrin in liposomes and oil-in-water emulsions. Journal of Agricultural and Food Chemistry 50:8 (2002), 2392–2399.
    • (2002) Journal of Agricultural and Food Chemistry , vol.50 , Issue.8 , pp. 2392-2399
    • Medina, I.1    Tombo, I.2    Satué-Gracia, M.T.3    German, J.B.4    Frankel, E.N.5
  • 30
    • 84901667773 scopus 로고    scopus 로고
    • A standardised static in vitro digestion method suitable for food–an international consensus
    • Minekus, M., Alminger, M., Alvito, P., Ballance, S., Bohn, T., Bourlieu, C., et al. A standardised static in vitro digestion method suitable for food–an international consensus. Food and Function 5 (2014), 1113–1124.
    • (2014) Food and Function , vol.5 , pp. 1113-1124
    • Minekus, M.1    Alminger, M.2    Alvito, P.3    Ballance, S.4    Bohn, T.5    Bourlieu, C.6
  • 31
    • 84931559936 scopus 로고    scopus 로고
    • Kinetic and thermodynamic parameters for thermal denaturation of ovine milk lactoferrin determined by its loss of immunoreactivity
    • Navarro, F., Harouna, S., Calvo, M., Pérez, M.D., Sánchez, L., Kinetic and thermodynamic parameters for thermal denaturation of ovine milk lactoferrin determined by its loss of immunoreactivity. Journal of Dairy Science 98 (2015), 4328–4337.
    • (2015) Journal of Dairy Science , vol.98 , pp. 4328-4337
    • Navarro, F.1    Harouna, S.2    Calvo, M.3    Pérez, M.D.4    Sánchez, L.5
  • 32
    • 84908507171 scopus 로고    scopus 로고
    • Optimized DPPH assay in a detergent-based buffer system for measuring antioxidant activity of proteins
    • Nicklisch, S.C., Waite, J.H., Optimized DPPH assay in a detergent-based buffer system for measuring antioxidant activity of proteins. MethodsX 1 (2014), 233–238.
    • (2014) MethodsX , vol.1 , pp. 233-238
    • Nicklisch, S.C.1    Waite, J.H.2
  • 35
    • 84924136005 scopus 로고    scopus 로고
    • Antibacterial activity of bovine milk lactoferrin and its hydrolysates prepared with pepsin, chymosin and microbial rennet against foodborne pathogen Listeria monocytogenes
    • Ripolles, D., Harouna, S., Parrón, J.A., Calvo, M., Pérez, M.D., Carramiñana, J.J., et al. Antibacterial activity of bovine milk lactoferrin and its hydrolysates prepared with pepsin, chymosin and microbial rennet against foodborne pathogen Listeria monocytogenes. International Dairy Journal 45 (2015), 15–22.
    • (2015) International Dairy Journal , vol.45 , pp. 15-22
    • Ripolles, D.1    Harouna, S.2    Parrón, J.A.3    Calvo, M.4    Pérez, M.D.5    Carramiñana, J.J.6
  • 36
    • 0028618546 scopus 로고
    • Physicochemical and antibacterial properties of lactoferrin and its hydrolysate produced by heat treatment at acidic pH
    • H.T. William B. Lonnerdal V.S. Rumball Plenum Press New York, NY, USA
    • Saito, H., Takase, M., Tamura, Y., Shimamura, S., Tomita, M., Physicochemical and antibacterial properties of lactoferrin and its hydrolysate produced by heat treatment at acidic pH. William, H.T., Lonnerdal, B., Rumball, V.S., (eds.) Lactoferrin: Structure and function, 1994, Plenum Press, New York, NY, USA, 219–226.
    • (1994) Lactoferrin: Structure and function , pp. 219-226
    • Saito, H.1    Takase, M.2    Tamura, Y.3    Shimamura, S.4    Tomita, M.5
  • 38
    • 78349309161 scopus 로고    scopus 로고
    • Structural characteristic, pH and thermal stabilities of apo and holo forms of caprine and bovine lactoferrins
    • Sreedhara, A., Flengsrud, R., Langsrud, T., Kaul, P., Prakash, V., Vegarud, G.E., Structural characteristic, pH and thermal stabilities of apo and holo forms of caprine and bovine lactoferrins. Biometals 23 (2010), 1159–1170.
    • (2010) Biometals , vol.23 , pp. 1159-1170
    • Sreedhara, A.1    Flengsrud, R.2    Langsrud, T.3    Kaul, P.4    Prakash, V.5    Vegarud, G.E.6
  • 42
    • 27744563101 scopus 로고    scopus 로고
    • Availability of lactoferrin as a natural solubilizer of iron for food products
    • Uchida, T., Oda, T., Sato, K., Kawakami, H., Availability of lactoferrin as a natural solubilizer of iron for food products. International Dairy Journal 16 (2006), 95–101.
    • (2006) International Dairy Journal , vol.16 , pp. 95-101
    • Uchida, T.1    Oda, T.2    Sato, K.3    Kawakami, H.4
  • 43
    • 0028875343 scopus 로고
    • Glycosylated and unglycosylated human lactoferrins both bind iron and show identical affinities towards human lysozyme and bacterial lipopolysaccharide, but differ in their susceptibilities towards tryptic proteolysis
    • Van Berkel, P.H.C., Geerts, M.E.J., van Veen, H.A., Kooiman, P.M., Pieper, F.R., de Boer, H.A., et al. Glycosylated and unglycosylated human lactoferrins both bind iron and show identical affinities towards human lysozyme and bacterial lipopolysaccharide, but differ in their susceptibilities towards tryptic proteolysis. Biochemical Journal 312 (1995), 107–114.
    • (1995) Biochemical Journal , vol.312 , pp. 107-114
    • Van Berkel, P.H.C.1    Geerts, M.E.J.2    van Veen, H.A.3    Kooiman, P.M.4    Pieper, F.R.5    de Boer, H.A.6
  • 45
    • 85013663962 scopus 로고    scopus 로고
    • Drying and denaturation characteristics of three forms of bovine lactoferrin
    • article in press
    • Wang, B., Timilsena, Y.P., Blanch, E., Adhikari, B., Drying and denaturation characteristics of three forms of bovine lactoferrin. Drying Technology, 2016, 10.1080/07373937.2016.1196699 article in press.
    • (2016) Drying Technology
    • Wang, B.1    Timilsena, Y.P.2    Blanch, E.3    Adhikari, B.4
  • 46
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases
    • Whitmore, L., Wallace, B.A., Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases. Biopolymers 89 (2008), 392–400.
    • (2008) Biopolymers , vol.89 , pp. 392-400
    • Whitmore, L.1    Wallace, B.A.2
  • 48
    • 84930199637 scopus 로고    scopus 로고
    • Influence of lipid type on gastrointestinal fate of oil-in-water emulsions: In vitro digestion study
    • Zhang, R., Zhang, Z., Zhang, H., Decker, E.A., McClements, D.J., Influence of lipid type on gastrointestinal fate of oil-in-water emulsions: In vitro digestion study. Food Research International 75 (2015), 71–78.
    • (2015) Food Research International , vol.75 , pp. 71-78
    • Zhang, R.1    Zhang, Z.2    Zhang, H.3    Decker, E.A.4    McClements, D.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.