메뉴 건너뛰기




Volumn 119, Issue 2, 2010, Pages 560-566

Occurrence of β-casomorphins 5 and 7 in commercial dairy products and in their digests following in vitro simulated gastro-intestinal digestion

Author keywords

Casomorphins; Dairy products; HPLC MS MS; In vitro gastro intestinal digestion

Indexed keywords

BETA CASOMORPHINE 5; BETA CASOMORPHINE 7; BETA CASOMORPHINE DERIVATIVE; MILK PROTEIN; PEPTIDE; PROBIOTIC AGENT; UNCLASSIFIED DRUG; YOGHURT;

EID: 70350573378     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2009.06.058     Document Type: Article
Times cited : (90)

References (44)
  • 2
    • 0018687626 scopus 로고
    • Novel opioid peptides derived from casein (β-casomorphins). I. Isolation from bovine casein peptone
    • Brantl V., Teschemacher H., Henschen A., and Lottspeich F. Novel opioid peptides derived from casein (β-casomorphins). I. Isolation from bovine casein peptone. Hoppe-Seyler's Z Physiological Chemistry 360 (1979) 1211-1216
    • (1979) Hoppe-Seyler's Z Physiological Chemistry , vol.360 , pp. 1211-1216
    • Brantl, V.1    Teschemacher, H.2    Henschen, A.3    Lottspeich, F.4
  • 3
    • 34247119095 scopus 로고    scopus 로고
    • Beta-casomorphin 7 in raw and hydrolyzed milk derived from cows of alternative beta-casein genotypes
    • Cieslinska A., Kaminski S., Kostyra E., and Sienkiewicz-Szlapka E. Beta-casomorphin 7 in raw and hydrolyzed milk derived from cows of alternative beta-casein genotypes. Milchwissenschaft 62 (2007) 125-127
    • (2007) Milchwissenschaft , vol.62 , pp. 125-127
    • Cieslinska, A.1    Kaminski, S.2    Kostyra, E.3    Sienkiewicz-Szlapka, E.4
  • 4
    • 0742305574 scopus 로고    scopus 로고
    • Hydrolysis of bovine caseins by cathepsin B, a cysteine proteinase indigenous to milk
    • Considine T., Healy A., Kelly A.L., and McSweeney P.L.H. Hydrolysis of bovine caseins by cathepsin B, a cysteine proteinase indigenous to milk. International Dairy Journal 14 (2004) 117-124
    • (2004) International Dairy Journal , vol.14 , pp. 117-124
    • Considine, T.1    Healy, A.2    Kelly, A.L.3    McSweeney, P.L.H.4
  • 5
    • 43449103915 scopus 로고    scopus 로고
    • Release of beta-casomorphins 5 and 7 during simulated gastro-intestinal digestion of bovine beta-casein variants and milk-based infant formulas
    • De Noni I. Release of beta-casomorphins 5 and 7 during simulated gastro-intestinal digestion of bovine beta-casein variants and milk-based infant formulas. Food Chemistry 110 (2008) 897-903
    • (2008) Food Chemistry , vol.110 , pp. 897-903
    • De Noni, I.1
  • 8
    • 0033054968 scopus 로고    scopus 로고
    • Type I (insulin-dependent) diabetes mellitus and cow milk: Casein variant consumption
    • Elliott R.B., Harris D.P., Hill J.P., Bibby N.J., and Wasmuth H.E. Type I (insulin-dependent) diabetes mellitus and cow milk: Casein variant consumption. Diabetologia 42 (1999) 292-296
    • (1999) Diabetologia , vol.42 , pp. 292-296
    • Elliott, R.B.1    Harris, D.P.2    Hill, J.P.3    Bibby, N.J.4    Wasmuth, H.E.5
  • 9
    • 34347233365 scopus 로고    scopus 로고
    • Effects of storage temperature on physico-chemical characteristics of semi-skimmed UHT milk
    • Gaucher I., Mollé D., Gagnaire V., and Gaucheron F. Effects of storage temperature on physico-chemical characteristics of semi-skimmed UHT milk. Food Hydrocolloids 22 (2008) 130-143
    • (2008) Food Hydrocolloids , vol.22 , pp. 130-143
    • Gaucher, I.1    Mollé, D.2    Gagnaire, V.3    Gaucheron, F.4
  • 10
    • 34147123803 scopus 로고    scopus 로고
    • Food-derived peptides with biological activity: From research to food applications
    • Hartmann R., and Meisel H. Food-derived peptides with biological activity: From research to food applications. Current Opinion in Biotechnology 18 (2007) 163-169
    • (2007) Current Opinion in Biotechnology , vol.18 , pp. 163-169
    • Hartmann, R.1    Meisel, H.2
  • 11
    • 0000696245 scopus 로고    scopus 로고
    • Influence of genetic polymorphisms in bovine milk on the occurrence of bioactive peptides. Seminar on milk protein polymorphism, IDF Special Issue no. 9702
    • Hartwig A., Teschemacher H., Lehmann W., Gauly M., and Erhardt G. Influence of genetic polymorphisms in bovine milk on the occurrence of bioactive peptides. Seminar on milk protein polymorphism, IDF Special Issue no. 9702. International Dairy Federation, Brussels (1997) 459-460
    • (1997) International Dairy Federation, Brussels , pp. 459-460
    • Hartwig, A.1    Teschemacher, H.2    Lehmann, W.3    Gauly, M.4    Erhardt, G.5
  • 12
    • 4143138930 scopus 로고    scopus 로고
    • Release of angiotensin converting enzyme-inhibitory peptides by simulated gastrointestinal digestion of infant formulas
    • Hernandez-Ledesma B., Amigo L., Ramos M., and Recio I. Release of angiotensin converting enzyme-inhibitory peptides by simulated gastrointestinal digestion of infant formulas. International Dairy Journal 14 (2004) 889-898
    • (2004) International Dairy Journal , vol.14 , pp. 889-898
    • Hernandez-Ledesma, B.1    Amigo, L.2    Ramos, M.3    Recio, I.4
  • 13
    • 0011226893 scopus 로고
    • Milk. Determination of nitrogen content
    • IDF-International Dairy Federation
    • IDF-International Dairy Federation (1993). Milk. Determination of nitrogen content. Standard 20B.
    • (1993) Standard , vol.20 B
  • 16
    • 0032843790 scopus 로고    scopus 로고
    • Enzymatic release of neocasomorphin and β-casomorphin from bovine β-casein
    • Jinsmaa Y., and Yoshikawa M. Enzymatic release of neocasomorphin and β-casomorphin from bovine β-casein. Peptides 20 (1999) 957-962
    • (1999) Peptides , vol.20 , pp. 957-962
    • Jinsmaa, Y.1    Yoshikawa, M.2
  • 17
    • 0028989608 scopus 로고
    • The extracellular PI-type proteinase of Lactococcus lactis hydrolyzes beta-casein into more than one hundred different oligopeptides
    • Juillard V., Laan H., Kunji E.R., Jeronimus-Stratingh C.M., Bruins A.P., and Konings W.N. The extracellular PI-type proteinase of Lactococcus lactis hydrolyzes beta-casein into more than one hundred different oligopeptides. Journal of Bacteriology 177 (1995) 3472-3478
    • (1995) Journal of Bacteriology , vol.177 , pp. 3472-3478
    • Juillard, V.1    Laan, H.2    Kunji, E.R.3    Jeronimus-Stratingh, C.M.4    Bruins, A.P.5    Konings, W.N.6
  • 19
    • 33747503962 scopus 로고    scopus 로고
    • Bioactive peptides: Production and functionality
    • Korhonen H., and Pihlanto A. Bioactive peptides: Production and functionality. International Dairy Journal 16 (2006) 945-960
    • (2006) International Dairy Journal , vol.16 , pp. 945-960
    • Korhonen, H.1    Pihlanto, A.2
  • 23
    • 0033035252 scopus 로고    scopus 로고
    • Rapid new casomorphin-like peptide from a peptic casein hydrolysate second order derivative spectroscopy during HPLC
    • Macaud C., Zhao Q., Ricart G., and Piot J.M. Rapid new casomorphin-like peptide from a peptic casein hydrolysate second order derivative spectroscopy during HPLC. Chromatography and Related Technologies 22 (1999) 401-418
    • (1999) Chromatography and Related Technologies , vol.22 , pp. 401-418
    • Macaud, C.1    Zhao, Q.2    Ricart, G.3    Piot, J.M.4
  • 24
    • 0034745315 scopus 로고    scopus 로고
    • 1, ischaemic heart disease mortality, and other illnesses
    • 1, ischaemic heart disease mortality, and other illnesses. Medical Hypotheses 56 (2001) 262-272
    • (2001) Medical Hypotheses , vol.56 , pp. 262-272
    • McLachlan, C.N.S.1
  • 26
    • 58749115296 scopus 로고    scopus 로고
    • Whey proteins and peptides in human health
    • Onwulata, C, Ed, UK: Woodhead Publishing
    • Morris, P.E., & FitzGerald, R.J. (2008). Whey proteins and peptides in human health. In: Onwulata, C. (Ed.), Whey Processing, Functionality and Health Benefits (pp. 287-345). UK: Woodhead Publishing.
    • (2008) Whey Processing, Functionality and Health Benefits , pp. 287-345
    • Morris, P.E.1    FitzGerald, R.J.2
  • 27
    • 0029689077 scopus 로고    scopus 로고
    • Beta-casomorphins: Analysis in cheese and susceptibility to proteolytic enzymes from Lactococcus lactis ssp. cremoris
    • Muehlenkamp M.R., and Warthesen J.J. Beta-casomorphins: Analysis in cheese and susceptibility to proteolytic enzymes from Lactococcus lactis ssp. cremoris. Journal of Dairy Science 79 (1996) 20-26
    • (1996) Journal of Dairy Science , vol.79 , pp. 20-26
    • Muehlenkamp, M.R.1    Warthesen, J.J.2
  • 28
    • 34247148223 scopus 로고    scopus 로고
    • Angiotensin converting enzyme inhibitory peptides derived from food proteins: Biochemistry, bioactivity and production
    • Murray B.A., and FitzGerald R.J. Angiotensin converting enzyme inhibitory peptides derived from food proteins: Biochemistry, bioactivity and production. Current Pharmaceutical Design 13 (2007) 773-791
    • (2007) Current Pharmaceutical Design , vol.13 , pp. 773-791
    • Murray, B.A.1    FitzGerald, R.J.2
  • 29
    • 34547779366 scopus 로고    scopus 로고
    • Exploitation of endogenous protease activity in raw mastitic milk by MALDI-TOF/TOF
    • Napoli A., Aiello D., Di Donna L., Prendushi H., and Sindona G. Exploitation of endogenous protease activity in raw mastitic milk by MALDI-TOF/TOF. Analytical Chemistry 79 (2007) 5941-5948
    • (2007) Analytical Chemistry , vol.79 , pp. 5941-5948
    • Napoli, A.1    Aiello, D.2    Di Donna, L.3    Prendushi, H.4    Sindona, G.5
  • 30
    • 0242509041 scopus 로고    scopus 로고
    • In vitro study on digestion of peptides in Emmental cheese: Analytical evaluation and influence on angiotensin I converting enzyme inhibitory peptides
    • Parrot, S., Degraeve, P., Curia, C., & Martial-Gros, A. (2003). In vitro study on digestion of peptides in Emmental cheese: Analytical evaluation and influence on angiotensin I converting enzyme inhibitory peptides. Nahrung/Food, 47, 87-94.
    • (2003) Nahrung/Food , vol.47 , pp. 87-94
    • Parrot, S.1    Degraeve, P.2    Curia, C.3    Martial-Gros, A.4
  • 31
    • 0040790989 scopus 로고
    • La caratterizzazione analitica del formaggio Fontina sulla base della sua composizione in amminoacidi liberi
    • Pellegrino L., Hogenboom J.A., Pazzaglia C., and Todesco R. La caratterizzazione analitica del formaggio Fontina sulla base della sua composizione in amminoacidi liberi. Il Latte 10 (1995) 1086-1093
    • (1995) Il Latte , vol.10 , pp. 1086-1093
    • Pellegrino, L.1    Hogenboom, J.A.2    Pazzaglia, C.3    Todesco, R.4
  • 32
    • 0002862761 scopus 로고
    • Free amino acids for the quality control of Parmigiano-Reggiano cheese and particularly for the grated product
    • Resmini P., Pellegrino L., Pazzaglia C., and Hogenboom J.A. Free amino acids for the quality control of Parmigiano-Reggiano cheese and particularly for the grated product. Scienza e Tecnica Lattiero-Casearia 36 (1985) 557-592
    • (1985) Scienza e Tecnica Lattiero-Casearia , vol.36 , pp. 557-592
    • Resmini, P.1    Pellegrino, L.2    Pazzaglia, C.3    Hogenboom, J.A.4
  • 34
    • 0040511030 scopus 로고    scopus 로고
    • Release of bioactive peptides by enzymatic proteolysis of Lactobacillus GG fermented UHT-milk
    • Rokka T., Syväoja E.L., Tuominen J., and Korhonen H. Release of bioactive peptides by enzymatic proteolysis of Lactobacillus GG fermented UHT-milk. Milchwissenschaft 52 (1997) 675-678
    • (1997) Milchwissenschaft , vol.52 , pp. 675-678
    • Rokka, T.1    Syväoja, E.L.2    Tuominen, J.3    Korhonen, H.4
  • 35
    • 0034221181 scopus 로고    scopus 로고
    • Isolation and structural analysis of antihypertensive peptides that exist naturally in Gouda cheese
    • Saito T., Nakamura T., Kitazawa H., Kawai Y., and Itoh T. Isolation and structural analysis of antihypertensive peptides that exist naturally in Gouda cheese. Journal of Dairy Science 83 (2000) 1434-1440
    • (2000) Journal of Dairy Science , vol.83 , pp. 1434-1440
    • Saito, T.1    Nakamura, T.2    Kitazawa, H.3    Kawai, Y.4    Itoh, T.5
  • 36
    • 0242616156 scopus 로고    scopus 로고
    • Characterization of oligo-and polypeptides isolated from yoghurt
    • Schieber A., and Brückner H. Characterization of oligo-and polypeptides isolated from yoghurt. European Food Research and Technology 210 (2000) 310-313
    • (2000) European Food Research and Technology , vol.210 , pp. 310-313
    • Schieber, A.1    Brückner, H.2
  • 37
    • 0029399197 scopus 로고
    • Water-soluble peptides in Cheddar cheese: Isolation and identification of peptides in the diafiltration retentate of the water-soluble fraction
    • Singh T.K., Fox P.F., and Healy A. Water-soluble peptides in Cheddar cheese: Isolation and identification of peptides in the diafiltration retentate of the water-soluble fraction. Journal of Dairy Research 62 (1995) 629-640
    • (1995) Journal of Dairy Research , vol.62 , pp. 629-640
    • Singh, T.K.1    Fox, P.F.2    Healy, A.3
  • 38
    • 0031204504 scopus 로고    scopus 로고
    • Isolation and identification of further peptides in the diafiltration retentate of the water-soluble fraction of Cheddar cheese
    • Singh T.K., Fox P.F., and Healy A. Isolation and identification of further peptides in the diafiltration retentate of the water-soluble fraction of Cheddar cheese. Journal of Dairy Research 64 (1997) 433-443
    • (1997) Journal of Dairy Research , vol.64 , pp. 433-443
    • Singh, T.K.1    Fox, P.F.2    Healy, A.3
  • 39
    • 0000420163 scopus 로고
    • Effect of peptides from the sequence 58-72 of β-casein on the activity of endopeptidase, aminopeptidase, and X-prolyl-dipeptidyl aminopeptidase from Lactococcus lactis ssp. lactis MG1363
    • Stepaniak L., Fox P.F., Sorhaug T., and Grabska J. Effect of peptides from the sequence 58-72 of β-casein on the activity of endopeptidase, aminopeptidase, and X-prolyl-dipeptidyl aminopeptidase from Lactococcus lactis ssp. lactis MG1363. Journal of Agricultural and Food Chemistry 43 (1995) 849-853
    • (1995) Journal of Agricultural and Food Chemistry , vol.43 , pp. 849-853
    • Stepaniak, L.1    Fox, P.F.2    Sorhaug, T.3    Grabska, J.4
  • 41
    • 43649086418 scopus 로고    scopus 로고
    • Sensomics mapping and identification of the key bitter metabolites in Gouda cheese
    • Toelstede S., and Hofmann T. Sensomics mapping and identification of the key bitter metabolites in Gouda cheese. Journal of Agricultural and Food Chemistry 56 (2008) 2795-2804
    • (2008) Journal of Agricultural and Food Chemistry , vol.56 , pp. 2795-2804
    • Toelstede, S.1    Hofmann, T.2
  • 43
    • 43049135189 scopus 로고    scopus 로고
    • Identification of peptides in milk as a result of proteolysis at different levels of somatic cell counts using LC MALDI MS/MS detection
    • Wedholm A., Moller H.S., Lindmark-Mansson H., Rasmussen M.D., Andren A., and Larsen L.B. Identification of peptides in milk as a result of proteolysis at different levels of somatic cell counts using LC MALDI MS/MS detection. Journal of Dairy Research 75 (2008) 76-83
    • (2008) Journal of Dairy Research , vol.75 , pp. 76-83
    • Wedholm, A.1    Moller, H.S.2    Lindmark-Mansson, H.3    Rasmussen, M.D.4    Andren, A.5    Larsen, L.B.6
  • 44
    • 0024722980 scopus 로고
    • Solubility of peptides in trichloroacetic acid (TCA) solutions. Hypothesis on the precipitation mechanism
    • Yvon M., Chabanet C., and Pélissier J.P. Solubility of peptides in trichloroacetic acid (TCA) solutions. Hypothesis on the precipitation mechanism. International Journal of Peptide and Protein Research 34 (1989) 166-176
    • (1989) International Journal of Peptide and Protein Research , vol.34 , pp. 166-176
    • Yvon, M.1    Chabanet, C.2    Pélissier, J.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.