메뉴 건너뛰기




Volumn 25, Issue 1, 2011, Pages 71-81

Effect of enzymatic cross-linking of β-casein on proteolysis by pepsin

Author keywords

Cross linking; Digestion; Pepsin; Transglutaminase; Tyrosinase; Casein

Indexed keywords

CROSSLINKING; ELECTROPHORESIS; MASS SPECTROMETRY; PH EFFECTS; PROTEOLYSIS; SIZE EXCLUSION CHROMATOGRAPHY; SODIUM COMPOUNDS; SULFUR COMPOUNDS;

EID: 77957795367     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2010.05.007     Document Type: Article
Times cited : (94)

References (53)
  • 1
    • 0012997691 scopus 로고
    • Methods in food protein hydrolysis
    • Elsevier Applied Science Publishers, London, England
    • Adler-Nissen J. Methods in food protein hydrolysis. Anonymous enzymic hydrolysis in food proteins 1986, Elsevier Applied Science Publishers, London, England, (p. 110).
    • (1986) Anonymous enzymic hydrolysis in food proteins , pp. 110
    • Adler-Nissen, J.1
  • 2
    • 33750129519 scopus 로고    scopus 로고
    • In vitro studies of the digestion of caprine whey proteins by human gastric and duodenal juice and the effects on selected microorganisms
    • Almaas H., Holm H., Langsrud T., Flengsrud R., Vegarud G.E. In vitro studies of the digestion of caprine whey proteins by human gastric and duodenal juice and the effects on selected microorganisms. British Journal of Nutrition 2006, 96(3):562-569.
    • (2006) British Journal of Nutrition , vol.96 , Issue.3 , pp. 562-569
    • Almaas, H.1    Holm, H.2    Langsrud, T.3    Flengsrud, R.4    Vegarud, G.E.5
  • 3
    • 0028877688 scopus 로고
    • The amount of ultraviolet absorbance in a synthetic peptide is directly proportional to its number of peptide bonds
    • Becklin R.R., Desiderio D.M. The amount of ultraviolet absorbance in a synthetic peptide is directly proportional to its number of peptide bonds. Analytical Letters 1995, 28(12):2175-2190.
    • (1995) Analytical Letters , vol.28 , Issue.12 , pp. 2175-2190
    • Becklin, R.R.1    Desiderio, D.M.2
  • 5
    • 33646564345 scopus 로고    scopus 로고
    • When quinones meet amino acids: chemical, physical and biological consequences
    • Bittner S. When quinones meet amino acids: chemical, physical and biological consequences. Amino Acids 2006, 30(3):205-224.
    • (2006) Amino Acids , vol.30 , Issue.3 , pp. 205-224
    • Bittner, S.1
  • 8
    • 0034641671 scopus 로고    scopus 로고
    • Cross-linking in adhesive quinoproteins: studies with model decapeptides
    • Burzio L.A., Waite J.H. Cross-linking in adhesive quinoproteins: studies with model decapeptides. Biochemistry 2000, 39(36):11147-11153.
    • (2000) Biochemistry , vol.39 , Issue.36 , pp. 11147-11153
    • Burzio, L.A.1    Waite, J.H.2
  • 10
    • 8844240048 scopus 로고    scopus 로고
    • Peptic hydrolysis of ovine β-lactoglobulin and α-lactalbumin exceptional susceptibility of native ovine β-lactoglobulin to pepsinolysis
    • El-Zahar K., Sitohy M., Choiset Y., Métro F., Haertlé T., Chobert J. Peptic hydrolysis of ovine β-lactoglobulin and α-lactalbumin exceptional susceptibility of native ovine β-lactoglobulin to pepsinolysis. International Dairy Journal 2005, 15(1):17-27.
    • (2005) International Dairy Journal , vol.15 , Issue.1 , pp. 17-27
    • El-Zahar, K.1    Sitohy, M.2    Choiset, Y.3    Métro, F.4    Haertlé, T.5    Chobert, J.6
  • 11
    • 0039844984 scopus 로고    scopus 로고
    • 2+ independent transglutaminase for cross-linking of β-lactoglobulin
    • 2+ independent transglutaminase for cross-linking of β-lactoglobulin. Food Hydrocolloids 1999, 13(3):199-201.
    • (1999) Food Hydrocolloids , vol.13 , Issue.3 , pp. 199-201
    • Færgemand, M.1    Qvist, K.B.2
  • 12
    • 77953134492 scopus 로고    scopus 로고
    • Kinetic analysis of melanogenesis by means of Agaricus bisporus tyrosinase
    • Falguera V., Gatius F., Pagán J., Ibarz A. Kinetic analysis of melanogenesis by means of Agaricus bisporus tyrosinase. Food Research International 2010, 43(4):1174-1179.
    • (2010) Food Research International , vol.43 , Issue.4 , pp. 1174-1179
    • Falguera, V.1    Gatius, F.2    Pagán, J.3    Ibarz, A.4
  • 13
    • 0000326990 scopus 로고
    • Transglutaminase (guinea pig liver)
    • Academic Press, Part 1, H. Tabor, C.W. Tabor (Eds.)
    • Folk J.E. Transglutaminase (guinea pig liver). Methods in enzymology 1970, Vol. 17:889-894. Academic Press, Part 1. H. Tabor, C.W. Tabor (Eds.).
    • (1970) Methods in enzymology , vol.17 , pp. 889-894
    • Folk, J.E.1
  • 14
    • 0031784879 scopus 로고    scopus 로고
    • Hydrolysis and amino acid composition analysis of proteins
    • Fountoulakis M., Lahm H. Hydrolysis and amino acid composition analysis of proteins. Journal of Chromatography A 1998, 826(2):109-134.
    • (1998) Journal of Chromatography A , vol.826 , Issue.2 , pp. 109-134
    • Fountoulakis, M.1    Lahm, H.2
  • 15
    • 0345115202 scopus 로고
    • Structural studies of ribonuclease. XVIII. An investigation of the peptic digestion products of ribonuclease
    • Fujioka H., Scheraga H.A. Structural studies of ribonuclease. XVIII. An investigation of the peptic digestion products of ribonuclease. Biochemistry 1965, 4(10):2197-2205.
    • (1965) Biochemistry , vol.4 , Issue.10 , pp. 2197-2205
    • Fujioka, H.1    Scheraga, H.A.2
  • 16
    • 0021213448 scopus 로고
    • Oxidation of tyrosine residues in proteins by tyrosinase. Formation of protein-bonded 3,4-dihydroxyphenylalanine and 5-S-cysteinyl-3,4-dihydroxyphenylalanine
    • Ito S., Kato T., Shinpo K., Fujita K. Oxidation of tyrosine residues in proteins by tyrosinase. Formation of protein-bonded 3,4-dihydroxyphenylalanine and 5-S-cysteinyl-3,4-dihydroxyphenylalanine. Biochemical Journal 1984, 222(2):407-411.
    • (1984) Biochemical Journal , vol.222 , Issue.2 , pp. 407-411
    • Ito, S.1    Kato, T.2    Shinpo, K.3    Fujita, K.4
  • 17
    • 34447314205 scopus 로고    scopus 로고
    • Enzymatic digestion of the milk protein β-casein releases potent chemotactic peptide(s) for monocytes and macrophages
    • Kitazawa H., Yonezawa K., Tohno M., Shimosato T., Kawai Y., Saito T., et al. Enzymatic digestion of the milk protein β-casein releases potent chemotactic peptide(s) for monocytes and macrophages. International Immunopharmacology 2007, 7(9):1150-1159.
    • (2007) International Immunopharmacology , vol.7 , Issue.9 , pp. 1150-1159
    • Kitazawa, H.1    Yonezawa, K.2    Tohno, M.3    Shimosato, T.4    Kawai, Y.5    Saito, T.6
  • 18
    • 44949255007 scopus 로고    scopus 로고
    • Disintegration of solid foods in human stomach
    • Kong F., Singh R.P. Disintegration of solid foods in human stomach. Journal of Food Science 2008, 73(5):R67-R80.
    • (2008) Journal of Food Science , vol.73 , Issue.5
    • Kong, F.1    Singh, R.P.2
  • 19
    • 85167856346 scopus 로고    scopus 로고
    • Aggregation of peptides in soy protein isolate hydrolysates: the individual contributions of glycinin- and β-conglycinin-derived peptides
    • Kuipers, B. J. H. (2007). Aggregation of peptides in soy protein isolate hydrolysates: the individual contributions of glycinin- and β-conglycinin-derived peptides.
    • (2007)
    • Kuipers, B.J.H.1
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227(5259):680-685.
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 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., 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 2007, 55(4):1248-1255.
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , Issue.4 , pp. 1248-1255
    • Lantto, R.1    Puolanne, E.2    Kruus, K.3    Buchert, J.4    Autio, K.5
  • 23
    • 33748416072 scopus 로고    scopus 로고
    • Antibacterial activity of peptides and folding variants from milk proteins
    • López Expósito I., Recio I. Antibacterial activity of peptides and folding variants from milk proteins. International Dairy Journal 2006, 16(11):1294-1305.
    • (2006) International Dairy Journal , vol.16 , Issue.11 , pp. 1294-1305
    • López Expósito, I.1    Recio, I.2
  • 24
    • 33748297647 scopus 로고    scopus 로고
    • Physiological, chemical and technological aspects of milk-protein-derived peptides with antihypertensive and ACE-inhibitory activity
    • López-Fandiño R., Otte J., van Camp J. Physiological, chemical and technological aspects of milk-protein-derived peptides with antihypertensive and ACE-inhibitory activity. International Dairy Journal 2006, 16(11):1277-1293.
    • (2006) International Dairy Journal , vol.16 , Issue.11 , pp. 1277-1293
    • López-Fandiño, R.1    Otte, J.2    van Camp, J.3
  • 25
    • 1542576838 scopus 로고    scopus 로고
    • Crosslinking of sodium caseinate by a microbial transglutaminase
    • Lorenzen P.C., Schlimme E., Roos N. Crosslinking of sodium caseinate by a microbial transglutaminase. Nahrung/Food 1998, 42(3-4):151-154.
    • (1998) Nahrung/Food , vol.42 , Issue.3-4 , pp. 151-154
    • Lorenzen, P.C.1    Schlimme, E.2    Roos, N.3
  • 26
    • 0027305178 scopus 로고
    • The complete amino acid sequence of a thrombin-like enzyme/gyroxin analogue from venom of the bushmaster snake (Lachesis muta muta)
    • Magalhaes A., Da Fonseca B.C.B., Ribeiro Diniz C., Gilroy J., Richardson M. The complete amino acid sequence of a thrombin-like enzyme/gyroxin analogue from venom of the bushmaster snake (Lachesis muta muta). FEBS Letters 1993, 329(1-2):116-120.
    • (1993) FEBS Letters , vol.329 , Issue.1-2 , pp. 116-120
    • Magalhaes, A.1    Da Fonseca, B.C.B.2    Ribeiro Diniz, C.3    Gilroy, J.4    Richardson, M.5
  • 27
    • 34250742375 scopus 로고    scopus 로고
    • Synthesis and resistance to in vitro proteolysis of transglutaminase cross-linked phaseolin, the major storage protein from Phaseolus vulgaris
    • Mariniello L., Giosafatto C.V.L., Di Pierro P., Sorrentino A., Porta R. Synthesis and resistance to in vitro proteolysis of transglutaminase cross-linked phaseolin, the major storage protein from Phaseolus vulgaris. Journal of Agricultural and Food Chemistry 2007, 55(12):4717-4721.
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , Issue.12 , pp. 4717-4721
    • Mariniello, L.1    Giosafatto, C.V.L.2    Di Pierro, P.3    Sorrentino, A.4    Porta, R.5
  • 28
    • 37349070966 scopus 로고    scopus 로고
    • Oxidation of peptides and proteins by Trichoderma reesei and Agaricus bisporus tyrosinases
    • Mattinen M., Lantto R., Selinheimo E., Kruus K., Buchert J. Oxidation of peptides and proteins by Trichoderma reesei and Agaricus bisporus tyrosinases. Journal of Biotechnology 2008, 133(3):395-402.
    • (2008) Journal of Biotechnology , vol.133 , Issue.3 , pp. 395-402
    • Mattinen, M.1    Lantto, R.2    Selinheimo, E.3    Kruus, K.4    Buchert, J.5
  • 29
    • 67349124399 scopus 로고    scopus 로고
    • Cross-linking of β-casein by Trichoderma reesei tyrosinase and Streptoverticillium mobaraense transglutaminase followed by SEC-MALLS
    • Monogioudi E., Creusot N., Kruus K., Gruppen H., Buchert J., Mattinen M. Cross-linking of β-casein by Trichoderma reesei tyrosinase and Streptoverticillium mobaraense transglutaminase followed by SEC-MALLS. Food Hydrocolloids 2009, 23(7):2008-2015.
    • (2009) Food Hydrocolloids , vol.23 , Issue.7 , pp. 2008-2015
    • Monogioudi, E.1    Creusot, N.2    Kruus, K.3    Gruppen, H.4    Buchert, J.5    Mattinen, M.6
  • 31
    • 34548484135 scopus 로고    scopus 로고
    • Fractionation and identification of ACE-inhibitory peptides from α-lactalbumin and β-casein produced by thermolysin-catalysed hydrolysis
    • Otte J., Shalaby S.M.A., Zakora M., Nielsen M.S. Fractionation and identification of ACE-inhibitory peptides from α-lactalbumin and β-casein produced by thermolysin-catalysed hydrolysis. International Dairy Journal 2007, 17(12):1460-1472.
    • (2007) International Dairy Journal , vol.17 , Issue.12 , pp. 1460-1472
    • Otte, J.1    Shalaby, S.M.A.2    Zakora, M.3    Nielsen, M.S.4
  • 32
    • 33748319573 scopus 로고    scopus 로고
    • Antioxidative peptides derived from milk proteins
    • Pihlanto A. Antioxidative peptides derived from milk proteins. International Dairy Journal 2006, 16(11):1306-1314.
    • (2006) International Dairy Journal , vol.16 , Issue.11 , pp. 1306-1314
    • Pihlanto, A.1
  • 33
    • 41449109241 scopus 로고    scopus 로고
    • Pepsin-induced changes in the size and molecular weight distribution of bovine casein during enzymatic hydrolysis
    • Qi W., Su R.X., He Z.M., Zhang Y.B., Jin F.M. Pepsin-induced changes in the size and molecular weight distribution of bovine casein during enzymatic hydrolysis. Journal of Dairy Science 2007, 90(11):5004-5011.
    • (2007) Journal of Dairy Science , vol.90 , Issue.11 , pp. 5004-5011
    • Qi, W.1    Su, R.X.2    He, Z.M.3    Zhang, Y.B.4    Jin, F.M.5
  • 34
  • 36
    • 85053591293 scopus 로고
    • Tyrosinase
    • CRC Press, Florida, R. Lontie (Ed.)
    • Robb D.A. Tyrosinase. Copper proteins and copper enzymes 1984, Vol. II:207-240. CRC Press, Florida. R. Lontie (Ed.).
    • (1984) Copper proteins and copper enzymes , vol.2 , pp. 207-240
    • Robb, D.A.1
  • 37
    • 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., Korhonen H. Release of bioactive peptides by enzymatic proteolysis of Lactobacillus GG fermented UHT milk. Milchwissenschaft 1997, 52:675-678.
    • (1997) Milchwissenschaft , vol.52 , pp. 675-678
    • Rokka, T.1    Syväoja, E.L.2    Tuominen, J.3    Korhonen, H.4
  • 41
    • 21544481753 scopus 로고    scopus 로고
    • Mass spectrometric characterization of human skin elastin peptides produced by proteolytic digestion with pepsin and thermitase
    • Schmelzer C.E.H., Getie M., Neubert R.H.H. Mass spectrometric characterization of human skin elastin peptides produced by proteolytic digestion with pepsin and thermitase. Journal of Chromatography A 2005, 1083(1-2):120-126.
    • (2005) Journal of Chromatography A , vol.1083 , Issue.1-2 , pp. 120-126
    • Schmelzer, C.E.H.1    Getie, M.2    Neubert, R.H.H.3
  • 43
    • 0000900124 scopus 로고
    • e{open}-(γ-Glutamyl) lysine: hydrolysis by γ-glutamyltransferase of different origins, when free or protein bound
    • Seguro K., Kumazawa Y., Ohtsuka T., Ide H., Nio N., Motoki M., et al. e{open}-(γ-Glutamyl) lysine: hydrolysis by γ-glutamyltransferase of different origins, when free or protein bound. Journal of Agricultural and Food Chemistry 1995, 1977-1981.
    • (1995) Journal of Agricultural and Food Chemistry , pp. 1977-1981
    • Seguro, K.1    Kumazawa, Y.2    Ohtsuka, T.3    Ide, H.4    Nio, N.5    Motoki, M.6
  • 45
    • 33748327047 scopus 로고    scopus 로고
    • Production and characterization of a secreted, C-terminally processed tyrosinase from the filamentous fungus Trichoderma reesei
    • Selinheimo E., Saloheimo M., Ahola E., Westerholm-Parvinen A., Kalkkinen N., Buchert J., et al. Production and characterization of a secreted, C-terminally processed tyrosinase from the filamentous fungus Trichoderma reesei. FEBS Journal 2006, 273(18):4322-4335.
    • (2006) FEBS Journal , vol.273 , Issue.18 , pp. 4322-4335
    • Selinheimo, E.1    Saloheimo, M.2    Ahola, E.3    Westerholm-Parvinen, A.4    Kalkkinen, N.5    Buchert, J.6
  • 48
    • 35448990075 scopus 로고    scopus 로고
    • Pancreatic hydrolysis of bovine casein: changes in the aggregate size and molecular weight distribution
    • Su R., He Z., Qi W. Pancreatic hydrolysis of bovine casein: changes in the aggregate size and molecular weight distribution. Food Chemistry 2008, 107(1):151-157.
    • (2008) Food Chemistry , vol.107 , Issue.1 , pp. 151-157
    • Su, R.1    He, Z.2    Qi, W.3
  • 49
    • 33751100096 scopus 로고    scopus 로고
    • Influence of transglutaminase-induced cross-linking on in vitro digestibility of soy protein isolate
    • Tang C.H., Li L., Yang X.-Q. Influence of transglutaminase-induced cross-linking on in vitro digestibility of soy protein isolate. Journal of Food Biochemistry 2006, 30(6):718-731.
    • (2006) Journal of Food Biochemistry , vol.30 , Issue.6 , pp. 718-731
    • Tang, C.H.1    Li, L.2    Yang, X.-Q.3
  • 50
    • 0030784243 scopus 로고    scopus 로고
    • Cleavage of the X-Pro peptide bond by pepsin is specific for the trans isomer
    • Vance J.E., LeBlanc D.A., London R.E. Cleavage of the X-Pro peptide bond by pepsin is specific for the trans isomer. Biochemistry 1997, 36(43):13232-13240.
    • (1997) Biochemistry , vol.36 , Issue.43 , pp. 13232-13240
    • Vance, J.E.1    LeBlanc, D.A.2    London, R.E.3
  • 52
    • 23444431647 scopus 로고    scopus 로고
    • A high-protein diet induces sustained reductions in appetite, ad libitum caloric intake, and body weight despite compensatory changes in diurnal plasma leptin and ghrelin concentrations
    • Weigle D.S., Breen P.A., Matthys C.C., Callahan H.S., Meeuws K.E., Burden V.R., et al. A high-protein diet induces sustained reductions in appetite, ad libitum caloric intake, and body weight despite compensatory changes in diurnal plasma leptin and ghrelin concentrations. American Journal of Clinical Nutrition 2005, 82(1):41-48.
    • (2005) American Journal of Clinical Nutrition , vol.82 , Issue.1 , pp. 41-48
    • Weigle, D.S.1    Breen, P.A.2    Matthys, C.C.3    Callahan, H.S.4    Meeuws, K.E.5    Burden, V.R.6
  • 53
    • 0025049408 scopus 로고
    • Aspartyl- and glutamyl-lysine crosslinks formation and their nutritional availability
    • Yasumoto K., Suzuki F. Aspartyl- and glutamyl-lysine crosslinks formation and their nutritional availability. Journal of Nutritional Science and Vitaminology 1990, 36:S71-S77.
    • (1990) Journal of Nutritional Science and Vitaminology , vol.36
    • Yasumoto, K.1    Suzuki, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.