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Volumn 49, Issue 1, 2012, Pages 73-79

New peptides obtained by hydrolysis of caseins from bovine milk by protease extracted from the latex Jacaratia corumbensis

Author keywords

Antimicrobial peptides; Casein; Hydrolyzed protein; Jacaratia corumbensis

Indexed keywords

BACTERIOLOGY; CASEIN; DAIRIES; ELECTROPHORESIS; ESCHERICHIA COLI; HYDROLYSIS; LIQUID CHROMATOGRAPHY; MAMMALS; MASS SPECTROMETRY; PROTEOLYSIS;

EID: 84862679992     PISSN: 00236438     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.lwt.2012.04.001     Document Type: Article
Times cited : (22)

References (28)
  • 2
    • 40949131305 scopus 로고    scopus 로고
    • Thermodynamics of the interactions of tryptophan-rich cathelicidin antimicrobial peptides with model and natural membranes
    • Andrushchenko V.V., Aarabi M.H., Nguyen L.T., Prenner E.J., Vogel H.J. Thermodynamics of the interactions of tryptophan-rich cathelicidin antimicrobial peptides with model and natural membranes. Biochimica et Biophysica Acta 2008, 1778:1004-1014.
    • (2008) Biochimica et Biophysica Acta , vol.1778 , pp. 1004-1014
    • Andrushchenko, V.V.1    Aarabi, M.H.2    Nguyen, L.T.3    Prenner, E.J.4    Vogel, H.J.5
  • 5
    • 0011372270 scopus 로고
    • An improved method of observing the clotting of milk containing rennin
    • Berridge N.J. An improved method of observing the clotting of milk containing rennin. Journal of Dairy Research 1952, 9:328-329.
    • (1952) Journal of Dairy Research , vol.9 , pp. 328-329
    • Berridge, N.J.1
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 1976, 72:248-254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 33748935159 scopus 로고    scopus 로고
    • LL-37, the only human member of the cathelicidin family of antimicrobial peptides
    • Dürr U.H.N., Sudheendra U.S., Ramamoorthy A. LL-37, the only human member of the cathelicidin family of antimicrobial peptides. Biochimica et Biophysica Acta 2006, 1758:1408-1425.
    • (2006) Biochimica et Biophysica Acta , vol.1758 , pp. 1408-1425
    • Dürr, U.H.N.1    Sudheendra, U.S.2    Ramamoorthy, A.3
  • 10
    • 34047107397 scopus 로고    scopus 로고
    • Milk - clotting activity of enzyme extracts from sunflower and albizia seeds and specific hydrolysis of bovine k-casein
    • Egito A.S., Girardet J.M., Laguna L.E., Poirson C., Mollé D., Miclo L., et al. Milk - clotting activity of enzyme extracts from sunflower and albizia seeds and specific hydrolysis of bovine k-casein. International Dairy Journal 2007, 17:816-825.
    • (2007) International Dairy Journal , vol.17 , pp. 816-825
    • Egito, A.S.1    Girardet, J.M.2    Laguna, L.E.3    Poirson, C.4    Mollé, D.5    Miclo, L.6
  • 12
    • 0038058813 scopus 로고    scopus 로고
    • Antibacterial and antiviral effects of milk proteins and derivatives thereof
    • Floris R., Recio I., Berkhout B., Visser S. Antibacterial and antiviral effects of milk proteins and derivatives thereof. Current Pharmaceutical Design 2003, 16:1257-1275.
    • (2003) Current Pharmaceutical Design , vol.16 , pp. 1257-1275
    • Floris, R.1    Recio, I.2    Berkhout, B.3    Visser, S.4
  • 13
    • 2942560423 scopus 로고    scopus 로고
    • Jelleines: a family of antimicrobial peptides from the royal jelly of honeybees (Apis mellifera)
    • Fontana R., Mendes M.A., Souza B.M., Konno K., Cesar L.M.M., Malaspina O., et al. Jelleines: a family of antimicrobial peptides from the royal jelly of honeybees (Apis mellifera). Peptides 2004, 25:919-928.
    • (2004) Peptides , vol.25 , pp. 919-928
    • Fontana, R.1    Mendes, M.A.2    Souza, B.M.3    Konno, K.4    Cesar, L.M.M.5    Malaspina, O.6
  • 14
    • 0018394517 scopus 로고
    • Sporulation and the production of serine protease and cephamycin c by Streptomyces lactamdurans
    • Ginther C.L. Sporulation and the production of serine protease and cephamycin c by Streptomyces lactamdurans. Antimicrobial Agents and Chemotherapy 1979, 1:522-526.
    • (1979) Antimicrobial Agents and Chemotherapy , vol.1 , pp. 522-526
    • Ginther, C.L.1
  • 16
    • 58149113170 scopus 로고    scopus 로고
    • Antimicrobial properties of lactoferrin
    • Jenssen H., Hancock R.E.W. Antimicrobial properties of lactoferrin. Biochimie 2009, 91:19-29.
    • (2009) Biochimie , vol.91 , pp. 19-29
    • Jenssen, H.1    Hancock, R.E.W.2
  • 17
    • 77956263461 scopus 로고    scopus 로고
    • Antibiotic and synergistic effect of Leu-Lys rich peptide against antibiotic resistant microorganisms isolated from patients with cholelithiasis
    • Jeong N., Kima J., Park S., Lee J., Gopal R., Yoo S., et al. Antibiotic and synergistic effect of Leu-Lys rich peptide against antibiotic resistant microorganisms isolated from patients with cholelithiasis. Biochemical and Biophysical Research Communications 2010, 399:581-586.
    • (2010) Biochemical and Biophysical Research Communications , vol.399 , pp. 581-586
    • Jeong, N.1    Kima, J.2    Park, S.3    Lee, J.4    Gopal, R.5    Yoo, S.6
  • 18
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10,000 Daltons
    • Karas M., Hillenkamp F. Laser desorption ionization of proteins with molecular masses exceeding 10,000 Daltons. Analytical Chemistry 1988, 60:2299-2301.
    • (1988) Analytical Chemistry , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 19
    • 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 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 60749118913 scopus 로고    scopus 로고
    • Antimicrobial peptides: linking partition, activity and high membrane-bound concentration
    • Melo M.N., Ferre R., Castanho M.A.R.B. Antimicrobial peptides: linking partition, activity and high membrane-bound concentration. Nature Opinion 2009, 7.
    • (2009) Nature Opinion , vol.7
    • Melo, M.N.1    Ferre, R.2    Castanho, M.A.R.B.3
  • 22
    • 49449115536 scopus 로고    scopus 로고
    • Purification, biochemical and functional characterization of Miliin, a new thiol-dependent serine protease isolated from the latex of Euphorbia milii
    • Moro L.P., Murakami M.T., Cabral H., Vidotto A., Tajara E.H., Arni R.K. Purification, biochemical and functional characterization of Miliin, a new thiol-dependent serine protease isolated from the latex of Euphorbia milii. Protein and Peptides Letter 2008, 15:724-730.
    • (2008) Protein and Peptides Letter , vol.15 , pp. 724-730
    • Moro, L.P.1    Murakami, M.T.2    Cabral, H.3    Vidotto, A.4    Tajara, E.H.5    Arni, R.K.6
  • 23
    • 78751650063 scopus 로고    scopus 로고
    • Applications of antimicrobial peptides from fish and perspectives for the future
    • Rajanbabu V., Chen J. Applications of antimicrobial peptides from fish and perspectives for the future. Peptides 2011, 32:415-420.
    • (2011) Peptides , vol.32 , pp. 415-420
    • Rajanbabu, V.1    Chen, J.2
  • 25
    • 77952892222 scopus 로고    scopus 로고
    • Enzymatic fragmentation of the antimicrobial peptides casocidin and isracidin by Streptococcus thermophilus and Lactobacillus delbrueckii ssp. Bulgaricus
    • Somkuti G.A., Paul M. Enzymatic fragmentation of the antimicrobial peptides casocidin and isracidin by Streptococcus thermophilus and Lactobacillus delbrueckii ssp. Bulgaricus. Applied Microbiology and Biotechnology 2010, 87:235-242.
    • (2010) Applied Microbiology and Biotechnology , vol.87 , pp. 235-242
    • Somkuti, G.A.1    Paul, M.2
  • 27
    • 78149407716 scopus 로고    scopus 로고
    • Purification and biochemical characterisation of a novel protease streblin
    • Tripathi P., Tomar R., Jagannadham M.V. Purification and biochemical characterisation of a novel protease streblin. Food Chemistry 2011, 125:1005-1012.
    • (2011) Food Chemistry , vol.125 , pp. 1005-1012
    • Tripathi, P.1    Tomar, R.2    Jagannadham, M.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.