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Volumn 31, Issue 2, 2013, Pages 111-116

Antibacterial effect and hydrophobicity of yak κ-casein hydrolysate and its fractions

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBACTERIAL EFFECTS; CASEIN HYDROLYSATE; GEL FILTRATION; MONOCYTE-MACROPHAGES; POTENTIAL INHIBITORS; RAW 264.7 CELLS; SEPHADEX; SURFACE HYDROPHOBICITY;

EID: 84876869276     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.idairyj.2012.12.004     Document Type: Article
Times cited : (27)

References (42)
  • 1
    • 0018536145 scopus 로고
    • Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid
    • Adler-Nissen J. Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid. Journal of Agricultural and Food Chemistry 1979, 27:1256-1262.
    • (1979) Journal of Agricultural and Food Chemistry , vol.27 , pp. 1256-1262
    • Adler-Nissen, J.1
  • 2
    • 51249100844 scopus 로고    scopus 로고
    • Degradation of whey from caprine milk by human proteolytic enzymes, and the resulting antibacterial effect against Listeria monocytogenes
    • Almaas H., Berner V., Holm H., Langsrud T., Vegarud G.E. Degradation of whey from caprine milk by human proteolytic enzymes, and the resulting antibacterial effect against Listeria monocytogenes. Small Ruminant Research 2008, 79:11-15.
    • (2008) Small Ruminant Research , vol.79 , pp. 11-15
    • Almaas, H.1    Berner, V.2    Holm, H.3    Langsrud, T.4    Vegarud, G.E.5
  • 4
    • 1842434455 scopus 로고    scopus 로고
    • Optimization study for the production of an opioid-like preparation from bovine casein by mild acidic hydrolysis
    • Bitri L. Optimization study for the production of an opioid-like preparation from bovine casein by mild acidic hydrolysis. International Dairy Journal 2004, 14:535-539.
    • (2004) International Dairy Journal , vol.14 , pp. 535-539
    • Bitri, L.1
  • 5
    • 0342804403 scopus 로고    scopus 로고
    • Enzymatic hydrolysis and synthesis of soy protein to improve its amino acid composition and functional properties
    • Calderón de la Barca A.M., Ruiz-Salazar R.A., Jara-Marini M.E. Enzymatic hydrolysis and synthesis of soy protein to improve its amino acid composition and functional properties. Journal of Food Science 2000, 65:246-253.
    • (2000) Journal of Food Science , vol.65 , pp. 246-253
    • Calderón de la Barca, A.M.1    Ruiz-Salazar, R.A.2    Jara-Marini, M.E.3
  • 7
    • 16844373772 scopus 로고    scopus 로고
    • Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index
    • Chen Y., Mant C.T., Farmer S.W., Hancock R.E., Vasil M.L., Hodges R.S. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. Journal of Biological Chemistry 2005, 280:12316-12329.
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 12316-12329
    • Chen, Y.1    Mant, C.T.2    Farmer, S.W.3    Hancock, R.E.4    Vasil, M.L.5    Hodges, R.S.6
  • 8
    • 0042430615 scopus 로고    scopus 로고
    • In vitro and in vivo activity of an antibacterial peptide analog against uropathogens
    • Cudic M., Lockatell C.V., Johnson D.E., Otvos L. In vitro and in vivo activity of an antibacterial peptide analog against uropathogens. Peptides 2003, 24:807-820.
    • (2003) Peptides , vol.24 , pp. 807-820
    • Cudic, M.1    Lockatell, C.V.2    Johnson, D.E.3    Otvos, L.4
  • 10
    • 33645737243 scopus 로고    scopus 로고
    • Membrane lipid composition and the interaction of pardaxin: the role of cholesterol
    • Epand R.F., Ramamoorthy A., Epand R.M. Membrane lipid composition and the interaction of pardaxin: the role of cholesterol. Protein and Peptide Letters 2006, 13:1-5.
    • (2006) Protein and Peptide Letters , vol.13 , pp. 1-5
    • Epand, R.F.1    Ramamoorthy, A.2    Epand, R.M.3
  • 11
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • Epand R.M., Vogel H.J. Diversity of antimicrobial peptides and their mechanisms of action. Biochimica et Biophysica Acta 1999, 1462:11-28.
    • (1999) Biochimica et Biophysica Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 12
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: antimicrobial peptides of innate immunity
    • Ganz T. Defensins: antimicrobial peptides of innate immunity. Nature Reviews Immunology 2003, 3:710-720.
    • (2003) Nature Reviews Immunology , vol.3 , pp. 710-720
    • Ganz, T.1
  • 13
    • 26644469527 scopus 로고    scopus 로고
    • Basis for selectivity of cationic antimicrobial peptides for bacterial versus mammalian membranes
    • Glukhov E., Stark M., Burrows L.L., Deber C.M. Basis for selectivity of cationic antimicrobial peptides for bacterial versus mammalian membranes. Journal of Biological Chemistry 2005, 280:33960-33967.
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 33960-33967
    • Glukhov, E.1    Stark, M.2    Burrows, L.L.3    Deber, C.M.4
  • 15
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: a new source of antibiotics
    • Hancock R.E., Lehrer R. Cationic peptides: a new source of antibiotics. Trends in Biotechnology 1998, 16:82-88.
    • (1998) Trends in Biotechnology , vol.16 , pp. 82-88
    • Hancock, R.E.1    Lehrer, R.2
  • 16
    • 27744532776 scopus 로고    scopus 로고
    • Relationships between antimicrobial use and antimicrobial resistance in Gram-negative bacteria causing nosocomial infections from 1991-2003 at a university hospital in Taiwan
    • Hsueh P.R., Chen W.H., Luh K.T. Relationships between antimicrobial use and antimicrobial resistance in Gram-negative bacteria causing nosocomial infections from 1991-2003 at a university hospital in Taiwan. International Journal of Antimicrobial Agents 2005, 26:463-472.
    • (2005) International Journal of Antimicrobial Agents , vol.26 , pp. 463-472
    • Hsueh, P.R.1    Chen, W.H.2    Luh, K.T.3
  • 17
    • 0029860472 scopus 로고    scopus 로고
    • Structure-biological activity relationships of 11-residue highly basic peptide segment of bovine lactoferrin
    • Kang J.H., Lee M.K., Kim K.L., Hahm K.S. Structure-biological activity relationships of 11-residue highly basic peptide segment of bovine lactoferrin. International Journal of Peptide and Protein Research 1996, 48:357-363.
    • (1996) International Journal of Peptide and Protein Research , vol.48 , pp. 357-363
    • Kang, J.H.1    Lee, M.K.2    Kim, K.L.3    Hahm, K.S.4
  • 18
    • 0019331914 scopus 로고
    • Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins
    • Kato A., Nakai S. Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. Biochimica et Biophysica Acta - Protein Structure 1980, 624:13-20.
    • (1980) Biochimica et Biophysica Acta - Protein Structure , vol.624 , pp. 13-20
    • Kato, A.1    Nakai, S.2
  • 19
    • 0030041615 scopus 로고    scopus 로고
    • Antibacterial and immunostimulating casein-derived substances from milk: casecidin, isracidin peptides
    • Lahov E., Regelson W. Antibacterial and immunostimulating casein-derived substances from milk: casecidin, isracidin peptides. Food and Chemical Toxicology 1996, 34:131-145.
    • (1996) Food and Chemical Toxicology , vol.34 , pp. 131-145
    • Lahov, E.1    Regelson, W.2
  • 20
    • 69249206712 scopus 로고    scopus 로고
    • Antioxidant activity and functional properties of porcine plasma protein hydrolysate as influenced by the degree of hydrolysis
    • Liu Q., Kong B.H., Xiong Y.L., Xia X.F. Antioxidant activity and functional properties of porcine plasma protein hydrolysate as influenced by the degree of hydrolysis. Food Chemistry 2010, 118:403-410.
    • (2010) Food Chemistry , vol.118 , pp. 403-410
    • Liu, Q.1    Kong, B.H.2    Xiong, Y.L.3    Xia, X.F.4
  • 24
    • 84869884616 scopus 로고    scopus 로고
    • Science of camel and yak milks: human nutrition and health perspectives
    • Nikkhah A. Science of camel and yak milks: human nutrition and health perspectives. Food and Nutrition Sciences 2011, 2:667-673.
    • (2011) Food and Nutrition Sciences , vol.2 , pp. 667-673
    • Nikkhah, A.1
  • 25
    • 0021701491 scopus 로고
    • Biochemical and antibacterial properties of bovine mammary secretion during mammary involution and at parturition
    • Nonnecke B.J., Smith K.L. Biochemical and antibacterial properties of bovine mammary secretion during mammary involution and at parturition. Journal of Dairy Science 1984, 67:2863-2872.
    • (1984) Journal of Dairy Science , vol.67 , pp. 2863-2872
    • Nonnecke, B.J.1    Smith, K.L.2
  • 26
    • 0031527044 scopus 로고    scopus 로고
    • Characterization of caseins from Mongolian yak, khainak, and Bactrian camel
    • Ochirkhuyag B., Chobert J.M., Dalgalarrondo M., Choiset Y., Haertle T. Characterization of caseins from Mongolian yak, khainak, and Bactrian camel. Lait 1997, 77:601-613.
    • (1997) Lait , vol.77 , pp. 601-613
    • Ochirkhuyag, B.1    Chobert, J.M.2    Dalgalarrondo, M.3    Choiset, Y.4    Haertle, T.5
  • 28
    • 0029069628 scopus 로고
    • Comparison of the effects of hydrophobicity, amphiphilicity, and alpha-helicity on the activities of antimicrobial peptides
    • Pathak N., Salas-Auvert R., Ruche G., Janna M.H., McCarthy D., Harrison R.G. Comparison of the effects of hydrophobicity, amphiphilicity, and alpha-helicity on the activities of antimicrobial peptides. Proteins 1995, 22:182-186.
    • (1995) Proteins , vol.22 , pp. 182-186
    • Pathak, N.1    Salas-Auvert, R.2    Ruche, G.3    Janna, M.H.4    McCarthy, D.5    Harrison, R.G.6
  • 29
    • 0035799705 scopus 로고    scopus 로고
    • Isolation and characterization of four bactericidal domains in the bovine beta-lactoglobulin
    • Pellegrini A., Dettling C., Thomas U., Hunziker P. Isolation and characterization of four bactericidal domains in the bovine beta-lactoglobulin. Biochimica et Biophysica Acta 2001, 1526:131-140.
    • (2001) Biochimica et Biophysica Acta , vol.1526 , pp. 131-140
    • Pellegrini, A.1    Dettling, C.2    Thomas, U.3    Hunziker, P.4
  • 33
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai Y. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochimica et Biophysica Acta - Biomembranes 1999, 1462:55-70.
    • (1999) Biochimica et Biophysica Acta - Biomembranes , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 34
    • 25144472273 scopus 로고    scopus 로고
    • The threat of antibiotic resistance in Gram-negative pathogenic bacteria: β-lactams in peril!
    • Thomson J.M., Bonomo R.A. The threat of antibiotic resistance in Gram-negative pathogenic bacteria: β-lactams in peril!. Current Opinion in Microbiology 2005, 8:518-524.
    • (2005) Current Opinion in Microbiology , vol.8 , pp. 518-524
    • Thomson, J.M.1    Bonomo, R.A.2
  • 35
    • 78049440079 scopus 로고    scopus 로고
    • Antioxidant, cytoprotective and antibacterial effects of Sea buckthorn (Hippophae rhamnoides L.) leaves
    • Upadhyay N.K., Yogendra Kumar M.S., Gupta A. Antioxidant, cytoprotective and antibacterial effects of Sea buckthorn (Hippophae rhamnoides L.) leaves. Food and Chemical Toxicology 2010, 48:3443-3448.
    • (2010) Food and Chemical Toxicology , vol.48 , pp. 3443-3448
    • Upadhyay, N.K.1    Yogendra Kumar, M.S.2    Gupta, A.3
  • 36
    • 79956266692 scopus 로고    scopus 로고
    • Zinc-binding capacity of yak casein hydrolysate and the zinc-releasing characteristics of casein hydrolysate-zinc complexes
    • Wang X., Zhou J., Tong P.S., Mao X.Y. Zinc-binding capacity of yak casein hydrolysate and the zinc-releasing characteristics of casein hydrolysate-zinc complexes. Journal of Dairy Science 2011, 94:2731-2740.
    • (2011) Journal of Dairy Science , vol.94 , pp. 2731-2740
    • Wang, X.1    Zhou, J.2    Tong, P.S.3    Mao, X.Y.4
  • 37
    • 0018786922 scopus 로고
    • Synthesis and spectral properties of a hydrophobic fluorescent probe: 6-propionyl-2-(dimethylamino)naphthalene
    • Weber G., Farris F.J. Synthesis and spectral properties of a hydrophobic fluorescent probe: 6-propionyl-2-(dimethylamino)naphthalene. Biochemistry 1979, 18:3075-3078.
    • (1979) Biochemistry , vol.18 , pp. 3075-3078
    • Weber, G.1    Farris, F.J.2
  • 38
    • 0030957876 scopus 로고    scopus 로고
    • Peptide hydrophobicity controls the activity and selectivity of magainin 2 amide in interaction with membranes
    • Wieprecht T., Dathe M., Beyermann M., Krause E., Maloy W.L., MacDonald D.L., et al. Peptide hydrophobicity controls the activity and selectivity of magainin 2 amide in interaction with membranes. Biochemistry 1997, 36:6124-6132.
    • (1997) Biochemistry , vol.36 , pp. 6124-6132
    • Wieprecht, T.1    Dathe, M.2    Beyermann, M.3    Krause, E.4    Maloy, W.L.5    MacDonald, D.L.6
  • 39
    • 78751698027 scopus 로고    scopus 로고
    • Attenuating effect of casein glycomacropeptide on proliferation, differentiation, and lipid accumulation of in vitro Sprague-Dawley rat preadipocytes
    • Xu S.P., Mao X.Y., Ren F.Z., Che H.L. Attenuating effect of casein glycomacropeptide on proliferation, differentiation, and lipid accumulation of in vitro Sprague-Dawley rat preadipocytes. Journal of Dairy Science 2011, 94:676-683.
    • (2011) Journal of Dairy Science , vol.94 , pp. 676-683
    • Xu, S.P.1    Mao, X.Y.2    Ren, F.Z.3    Che, H.L.4
  • 40
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • Yeaman M.R., Yount N.Y. Mechanisms of antimicrobial peptide action and resistance. Pharmacological Reviews 2003, 55:27-55.
    • (2003) Pharmacological Reviews , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.