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Volumn 120, Issue 1, 2010, Pages 66-73

Antimicrobial activity of native and esterified legume proteins against Gram-negative and Gram-positive bacteria

Author keywords

Antibacterial activity; Disc assay; Legume proteins; Protein esterification; Protein modification

Indexed keywords

CHICKPEA PROTEIN; HYDROCHLORIC ACID; SOYBEAN PROTEIN; UNCLASSIFIED DRUG; VEGETABLE PROTEIN; VICIA FABA PROTEIN;

EID: 71349088604     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2009.09.071     Document Type: Article
Times cited : (63)

References (31)
  • 1
    • 0038197386 scopus 로고    scopus 로고
    • Crude protein-micro Kjeldhelmethod
    • AACC , 10th ed, AACC method 46-13
    • AACC (2000). Crude protein-micro Kjeldhelmethod. In Approved methods of the AACC (Vol. II, 10th ed.). AACC method 46-13.
    • (2000) Approved methods of the AACC , vol.2
  • 2
    • 0000090990 scopus 로고
    • Purification and characterization of the storage proteins of Phaseolous vulgaris seeds, and their intracellular and cotyledonary distribution
    • Barker R.D.J., Derbyshire E., Yarwood A., and Boulter D. Purification and characterization of the storage proteins of Phaseolous vulgaris seeds, and their intracellular and cotyledonary distribution. Phytochemistry 15 (1976) 751-757
    • (1976) Phytochemistry , vol.15 , pp. 751-757
    • Barker, R.D.J.1    Derbyshire, E.2    Yarwood, A.3    Boulter, D.4
  • 3
    • 0001704077 scopus 로고
    • Esterification of food proteins: Characterization of the derivatives by a colorimetric method and by electrophoresis
    • Bertrand-Harb C., Chobert J.-M., Dufour E., and Haertlé T. Esterification of food proteins: Characterization of the derivatives by a colorimetric method and by electrophoresis. Sciences des Aliments 11 (1991) 641-652
    • (1991) Sciences des Aliments , vol.11 , pp. 641-652
    • Bertrand-Harb, C.1    Chobert, J.-M.2    Dufour, E.3    Haertlé, T.4
  • 4
    • 0033962266 scopus 로고    scopus 로고
    • Innate immunity and the normal microflora
    • Boman H.G. Innate immunity and the normal microflora. Immunology Reviews 173 (2000) 5-16
    • (2000) Immunology Reviews , vol.173 , pp. 5-16
    • Boman, H.G.1
  • 5
    • 0042830450 scopus 로고    scopus 로고
    • Antibacterial peptides: Basic facts and emerging concepts
    • Boman H.G. Antibacterial peptides: Basic facts and emerging concepts. Journal of Internal Medicine 254 (2003) 197-215
    • (2003) Journal of Internal Medicine , vol.254 , pp. 197-215
    • Boman, H.G.1
  • 6
    • 0016231216 scopus 로고
    • Insect immunity. I: Characteristics of an inducible cell-free antibacterial reaction in haemolymph of Samia cynthia pupae
    • Boman H.G., Nilson-Faye I.P.K., and Rasmuson T. Insect immunity. I: Characteristics of an inducible cell-free antibacterial reaction in haemolymph of Samia cynthia pupae. Infection and Immunity 10 (1974) 136-145
    • (1974) Infection and Immunity , vol.10 , pp. 136-145
    • Boman, H.G.1    Nilson-Faye, I.P.K.2    Rasmuson, T.3
  • 7
    • 0033579207 scopus 로고    scopus 로고
    • Use of the cell wall precursor lipid II by a pore-Forming peptide antibiotic
    • Breuking E., Wiedemann I., Van Kraaij C., Kuipers O.P., Sahl H., and Kruijff B. Use of the cell wall precursor lipid II by a pore-Forming peptide antibiotic. Science 286 (1999) 2361-2364
    • (1999) Science , vol.286 , pp. 2361-2364
    • Breuking, E.1    Wiedemann, I.2    Van Kraaij, C.3    Kuipers, O.P.4    Sahl, H.5    Kruijff, B.6
  • 8
    • 0037337245 scopus 로고    scopus 로고
    • Distinguishing between different pathways of bilayer disruption by the related antimicrobial peptides cecropin B, B1 and B3
    • Chen H.M., Leung K.W., Thakur N.N., Tan A., and Jack R.W. Distinguishing between different pathways of bilayer disruption by the related antimicrobial peptides cecropin B, B1 and B3. European Journal of Biochemistry 270 (2003) 911-920
    • (2003) European Journal of Biochemistry , vol.270 , pp. 911-920
    • Chen, H.M.1    Leung, K.W.2    Thakur, N.N.3    Tan, A.4    Jack, R.W.5
  • 10
    • 49349130487 scopus 로고
    • Legumin and vicilin, storage proteins of legume seeds
    • Derbyshire E., Wright D.J., and Boulter D. Legumin and vicilin, storage proteins of legume seeds. Phytochemistry 15 (1976) 3-24
    • (1976) Phytochemistry , vol.15 , pp. 3-24
    • Derbyshire, E.1    Wright, D.J.2    Boulter, D.3
  • 11
    • 4243270821 scopus 로고    scopus 로고
    • Lupin seed proteins
    • Doxastakis G., and Kiosseoglou V. (Eds), Elsevier, Amesterdam
    • Doxastakis G. Lupin seed proteins. In: Doxastakis G., and Kiosseoglou V. (Eds). Novel macromolecules in food systems (2000), Elsevier, Amesterdam 7-38
    • (2000) Novel macromolecules in food systems , pp. 7-38
    • Doxastakis, G.1
  • 12
  • 13
    • 0022292466 scopus 로고
    • Elected functionality changes of beta-lacto globulin upon esterification of side chain carboxyl groups
    • Halpin M.I., and Richardson T. Elected functionality changes of beta-lacto globulin upon esterification of side chain carboxyl groups. Journal of Dairy Science 68 (1985) 3189-3198
    • (1985) Journal of Dairy Science , vol.68 , pp. 3189-3198
    • Halpin, M.I.1    Richardson, T.2
  • 14
    • 4444235406 scopus 로고    scopus 로고
    • Bacterial structure and physiology: Influence on susceptibility to cationic antimicrobial peptides
    • Devine D.A., and Hancock R.E.W. (Eds), Cambridge University Press, Cambridge,UK
    • Hancock R.E.W. Bacterial structure and physiology: Influence on susceptibility to cationic antimicrobial peptides. In: Devine D.A., and Hancock R.E.W. (Eds). Mammalian host defense peptides (2004), Cambridge University Press, Cambridge,UK 229-244
    • (2004) Mammalian host defense peptides , pp. 229-244
    • Hancock, R.E.W.1
  • 16
    • 0000316158 scopus 로고
    • Electrophoretic analysis of whey proteins present in soybean globulin fractions
    • Iwabuchi S., and Yamauchi F. Electrophoretic analysis of whey proteins present in soybean globulin fractions. Journal of Agricultural and Food Chemistry 35 (1987) 205-209
    • (1987) Journal of Agricultural and Food Chemistry , vol.35 , pp. 205-209
    • Iwabuchi, S.1    Yamauchi, F.2
  • 17
    • 0001716538 scopus 로고
    • Functional properties of acylated pea protein isolates
    • Johnson E.A., and Brekke J. Functional properties of acylated pea protein isolates. Journal of Food Science 48 (1983) 722-725
    • (1983) Journal of Food Science , vol.48 , pp. 722-725
    • Johnson, E.A.1    Brekke, J.2
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 33847235357 scopus 로고    scopus 로고
    • The antimicrobial activity and molecular characterization of amidated bovine lactoferrin
    • Pan Y., Shiell B., Wan J., Coventry M.J., Roginski H., and Lee A. The antimicrobial activity and molecular characterization of amidated bovine lactoferrin. International Dairy Journal 17 (2007) 606-616
    • (2007) International Dairy Journal , vol.17 , pp. 606-616
    • Pan, Y.1    Shiell, B.2    Wan, J.3    Coventry, M.J.4    Roginski, H.5    Lee, A.6
  • 23
    • 0026787169 scopus 로고
    • Interaction of d-amino acid incorporated analogs of pardaxin with membranes
    • Pouny Y., and Shai Y. Interaction of d-amino acid incorporated analogs of pardaxin with membranes. Biochemistry 31 (1992) 9482-9490
    • (1992) Biochemistry , vol.31 , pp. 9482-9490
    • Pouny, Y.1    Shai, Y.2
  • 24
    • 0344404404 scopus 로고    scopus 로고
    • Protein isolates from chickpea (Cicer arietinum L.): Chemical composition, functional properties and protein characterization
    • Sánchez-Vioque R., Clemente A., Vioque J., Bautista J., and Millán F. Protein isolates from chickpea (Cicer arietinum L.): Chemical composition, functional properties and protein characterization. Food Chemistry 64 (1999) 237-243
    • (1999) Food Chemistry , vol.64 , pp. 237-243
    • Sánchez-Vioque, R.1    Clemente, A.2    Vioque, J.3    Bautista, J.4    Millán, F.5
  • 25
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • Shai Y. Mode of action of membrane active antimicrobial peptides. Biopolymers 66 (2002) 236-248
    • (2002) Biopolymers , vol.66 , pp. 236-248
    • Shai, Y.1
  • 26
    • 0034342594 scopus 로고    scopus 로고
    • Factors influencing protein esterification reaction using β-lacto globulin as a model protein
    • Sitohy M.Z., Chobert J.-M., and Haertlé T. Factors influencing protein esterification reaction using β-lacto globulin as a model protein. Journal of Food Biochemistry 24 (2000) 381-398
    • (2000) Journal of Food Biochemistry , vol.24 , pp. 381-398
    • Sitohy, M.Z.1    Chobert, J.-M.2    Haertlé, T.3
  • 27
    • 0034342594 scopus 로고    scopus 로고
    • Study of factors influencing protein esterification reaction using β-lactoglobulin as a model
    • Sitohy M.Z., Chobert J.-M., and Haertlé T. Study of factors influencing protein esterification reaction using β-lactoglobulin as a model. Journal of Food Biochemistry 24 (2000) 381-398
    • (2000) Journal of Food Biochemistry , vol.24 , pp. 381-398
    • Sitohy, M.Z.1    Chobert, J.-M.2    Haertlé, T.3
  • 28
    • 0035586024 scopus 로고    scopus 로고
    • Simplified short-time method for the esterification of milk proteins
    • Sitohy M.Z., Chobert J.-M., and Haertlé T. Simplified short-time method for the esterification of milk proteins. Milchwissenschaft 56 (2001) 127-131
    • (2001) Milchwissenschaft , vol.56 , pp. 127-131
    • Sitohy, M.Z.1    Chobert, J.-M.2    Haertlé, T.3
  • 29
    • 0041591616 scopus 로고    scopus 로고
    • Improvement of solubility and of emulsifying properties of milk proteins at acid pHs by esterification
    • Sitohy M.Z., Chobert J.-M., and Haertlé T. Improvement of solubility and of emulsifying properties of milk proteins at acid pHs by esterification. Die Nahrung 45 (2001) 87-93
    • (2001) Die Nahrung , vol.45 , pp. 87-93
    • Sitohy, M.Z.1    Chobert, J.-M.2    Haertlé, T.3
  • 30
    • 0001984295 scopus 로고
    • Isolation and characterization of the multiple 7S globulins of soybean proteins
    • Thanh V.H., Okubo K., and Shibasaki K. Isolation and characterization of the multiple 7S globulins of soybean proteins. Plant Physiology 56 (1975) 19-22
    • (1975) Plant Physiology , vol.56 , pp. 19-22
    • Thanh, V.H.1    Okubo, K.2    Shibasaki, K.3
  • 31
    • 0030935921 scopus 로고    scopus 로고
    • Fabatins: New antimicrobial plant peptides
    • Zhang Y., and Lewis K. Fabatins: New antimicrobial plant peptides. FEMS Microbiology Letters 149 (1997) 59-64
    • (1997) FEMS Microbiology Letters , vol.149 , pp. 59-64
    • Zhang, Y.1    Lewis, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.