메뉴 건너뛰기




Volumn 19, Issue 12, 2009, Pages 746-752

Removal of N-terminal peptides from β-lactoglobulin by proteolytic contaminants in a commercial phenol oxidase preparation

Author keywords

[No Author keywords available]

Indexed keywords

AGARICUS BISPORUS; ENZYME PREPARATION; FOOD BIOPROCESSING; FOOD INGREDIENTS; FUNCTIONAL PROPERTIES; GLOBULAR PROTEINS; LACCASES; LACTOGLOBULIN; N-TERMINALS; TRAMETES VERSICOLOR;

EID: 69949182410     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.idairyj.2009.05.008     Document Type: Article
Times cited : (8)

References (23)
  • 1
    • 0029764078 scopus 로고    scopus 로고
    • Stability of food allergens to digestion in vitro
    • Astwood J.D., Leach J.N., and Fuchs R.L. Stability of food allergens to digestion in vitro. Nature Biotechnology 14 (1996) 1269-1273
    • (1996) Nature Biotechnology , vol.14 , pp. 1269-1273
    • Astwood, J.D.1    Leach, J.N.2    Fuchs, R.L.3
  • 2
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • Berlett B.S., and Stadtman E.R. Protein oxidation in aging, disease, and oxidative stress. Journal of Biological Chemistry 272 (1997) 20313-20316
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 3
    • 40549106069 scopus 로고    scopus 로고
    • Oxidative transformation of natural and synthetic phenolic mixtures by Trametes versicolor laccase
    • Canfora L., Iamarino G., Rao M.A., and Gianfreda L. Oxidative transformation of natural and synthetic phenolic mixtures by Trametes versicolor laccase. Journal of Agricultural and Food Chemistry 56 (2008) 1398-1407
    • (2008) Journal of Agricultural and Food Chemistry , vol.56 , pp. 1398-1407
    • Canfora, L.1    Iamarino, G.2    Rao, M.A.3    Gianfreda, L.4
  • 4
    • 33748449287 scopus 로고    scopus 로고
    • Bioactivity of beta-lactoglobulin and alpha-lactalbumin - technological implications for processing
    • Chatterton D.E.W., Smithers G., Roupas P., and Brodkorb A. Bioactivity of beta-lactoglobulin and alpha-lactalbumin - technological implications for processing. International Dairy Journal 16 (2006) 1229-1240
    • (2006) International Dairy Journal , vol.16 , pp. 1229-1240
    • Chatterton, D.E.W.1    Smithers, G.2    Roupas, P.3    Brodkorb, A.4
  • 8
    • 33947316219 scopus 로고    scopus 로고
    • Promiscuous binding of ligands by beta-lactoglobulin involves hydrophobic interactions and plasticity
    • Konuma T., Sakurai K., and Goto Y. Promiscuous binding of ligands by beta-lactoglobulin involves hydrophobic interactions and plasticity. Journal of Molecular Biology 368 (2007) 209-218
    • (2007) Journal of Molecular Biology , vol.368 , pp. 209-218
    • Konuma, T.1    Sakurai, K.2    Goto, Y.3
  • 9
    • 0032701274 scopus 로고    scopus 로고
    • Involvement of the binuclear copper site in the proteolytic activity of polyphenol oxidase
    • Kuwabara T., and Katoh Y. Involvement of the binuclear copper site in the proteolytic activity of polyphenol oxidase. Plant and Cell Physiology 40 (1999) 1029-1035
    • (1999) Plant and Cell Physiology , vol.40 , pp. 1029-1035
    • Kuwabara, T.1    Katoh, Y.2
  • 10
    • 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. Journal of Agricultural and Food Chemistry 53 (2005) 9231-9237
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , pp. 9231-9237
    • Lantto, R.1    Puolanne, E.2    Kalkkinen, N.3    Buchert, J.4    Autio, K.5
  • 11
    • 34249853658 scopus 로고    scopus 로고
    • Tyrosinase-aided protein cross-linking: effects on gel formation of chicken breast myofibrils and texture and water-holding of chicken breast meat homogenate gels
    • Lantto R., Puolanne E., Kruus K., Buchert J., and Autio K. Tyrosinase-aided protein cross-linking: effects on gel formation of chicken breast myofibrils and texture and water-holding of chicken breast meat homogenate gels. Journal of Agricultural and Food Chemistry 55 (2007) 1248-1255
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , pp. 1248-1255
    • Lantto, R.1    Puolanne, E.2    Kruus, K.3    Buchert, J.4    Autio, K.5
  • 12
    • 0020688520 scopus 로고
    • Neurospora tyrosinase: structural, spectroscopic and catalytic properties
    • Lerch K. Neurospora tyrosinase: structural, spectroscopic and catalytic properties. Molecular and Cellular Biochemistry 52 (1983) 125-138
    • (1983) Molecular and Cellular Biochemistry , vol.52 , pp. 125-138
    • Lerch, K.1
  • 14
    • 0031055268 scopus 로고    scopus 로고
    • Identification of a novel angiotensin-I-converting enzyme inhibitory peptide corresponding to a tryptic fragment of bovine beta-lactoglobulin
    • Mullally M.M., Meisel H., and FitzGerald R.J. Identification of a novel angiotensin-I-converting enzyme inhibitory peptide corresponding to a tryptic fragment of bovine beta-lactoglobulin. FEBS Letters 402 (1997) 99-101
    • (1997) FEBS Letters , vol.402 , pp. 99-101
    • Mullally, M.M.1    Meisel, H.2    FitzGerald, R.J.3
  • 16
    • 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 T.R., 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 Expression and Purification 29 (2003) 202-208
    • (2003) Protein Expression and Purification , vol.29 , pp. 202-208
    • Neyestani, T.R.1    Djalali, M.2    Pezeshki, M.3
  • 17
    • 0035799705 scopus 로고    scopus 로고
    • Isolation and characterization of four bactericidal domains in the bovine beta-lactoglobulin
    • Pellegrini A., Dettling C., Thomas U., and Hunziker P. Isolation and characterization of four bactericidal domains in the bovine beta-lactoglobulin. Biochimica and Biophysica Acta 1526 (2001) 131-140
    • (2001) Biochimica and Biophysica Acta , vol.1526 , pp. 131-140
    • Pellegrini, A.1    Dettling, C.2    Thomas, U.3    Hunziker, P.4
  • 18
    • 0032717550 scopus 로고    scopus 로고
    • The effect of alpha-lactalbumin and beta-lactoglobulin hydrolysates on the metabolic activity of Escherichia coli JM103
    • Pihlanto-Leppala A., Marnila P., Hubert L., Rokka T., Korhonen H.J., and Karp M. The effect of alpha-lactalbumin and beta-lactoglobulin hydrolysates on the metabolic activity of Escherichia coli JM103. Journal of Applied Microbiology 87 (1999) 540-545
    • (1999) Journal of Applied Microbiology , vol.87 , pp. 540-545
    • Pihlanto-Leppala, A.1    Marnila, P.2    Hubert, L.3    Rokka, T.4    Korhonen, H.J.5    Karp, M.6
  • 19
    • 33646154205 scopus 로고    scopus 로고
    • Laccases: blue enzymes for green chemistry
    • Riva S. Laccases: blue enzymes for green chemistry. Trends in Biotechnology 24 (2006) 219-226
    • (2006) Trends in Biotechnology , vol.24 , pp. 219-226
    • Riva, S.1
  • 20
    • 61349161803 scopus 로고    scopus 로고
    • Should digestion assays be used to estimate persistence of potential allergens in tests for safety of novel food proteins?
    • Schnell S., and Herman R.A. Should digestion assays be used to estimate persistence of potential allergens in tests for safety of novel food proteins?. Clinical and Molecular Allergy 7 (2009) 1
    • (2009) Clinical and Molecular Allergy , vol.7 , pp. 1
    • Schnell, S.1    Herman, R.A.2
  • 22
    • 20444486236 scopus 로고    scopus 로고
    • Humoral and cellular responses to cow milk proteins in patients with milk-induced IgE-mediated and non-IgE-mediated disorders
    • Shek L.P., Bardina L., Castro R., Sampson H.A., and Beyer K. Humoral and cellular responses to cow milk proteins in patients with milk-induced IgE-mediated and non-IgE-mediated disorders. Allergy 60 (2005) 912-919
    • (2005) Allergy , vol.60 , pp. 912-919
    • Shek, L.P.1    Bardina, L.2    Castro, R.3    Sampson, H.A.4    Beyer, K.5
  • 23
    • 69949139090 scopus 로고
    • Action of tyrosinase on alpha-lactalbumin, beta-lactoglobulin, and ribonuclease
    • Yasunobu K.T., and Dandliker W.B. Action of tyrosinase on alpha-lactalbumin, beta-lactoglobulin, and ribonuclease. Journal of Biological Chemistry 224 (1957) 1065-1072
    • (1957) Journal of Biological Chemistry , vol.224 , pp. 1065-1072
    • Yasunobu, K.T.1    Dandliker, W.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.