메뉴 건너뛰기




Volumn 20, Issue 12, 2010, Pages 830-837

Effect of Trichoderma reesei tyrosinase on rheology and microstructure of acidified milk gels

Author keywords

[No Author keywords available]

Indexed keywords

AGARICUS BISPORUS; LINK PROTEIN; MILK GELS; MILK PROTEIN; PROTEIN CROSSLINKING; RAW MILK; SODIUM CASEINATE; STRUCTURAL ENGINEERING; TRANSGLUTAMINASES; TRICHODERMA REESEI;

EID: 77956618691     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.idairyj.2010.06.008     Document Type: Article
Times cited : (52)

References (42)
  • 1
    • 1242269225 scopus 로고    scopus 로고
    • Enzymatic grafting of peptides from casein hydrolysate to chitosan. Potential for value-added byproducts from food-processing wastes
    • Aberg C.M., Chen T., Olumide A., Raghavan S.R., Payne G.F. Enzymatic grafting of peptides from casein hydrolysate to chitosan. Potential for value-added byproducts from food-processing wastes. Journal of Agricultural and Food Chemistry 2004, 52:788-793.
    • (2004) Journal of Agricultural and Food Chemistry , vol.52 , pp. 788-793
    • Aberg, C.M.1    Chen, T.2    Olumide, A.3    Raghavan, S.R.4    Payne, G.F.5
  • 2
    • 58149512320 scopus 로고    scopus 로고
    • Role of colloidal calcium phosphate in the acid gelation properties of heated skim milk
    • Anema S.G. Role of colloidal calcium phosphate in the acid gelation properties of heated skim milk. Food Chemistry 2009, 114:161-167.
    • (2009) Food Chemistry , vol.114 , pp. 161-167
    • Anema, S.G.1
  • 3
    • 17444362230 scopus 로고    scopus 로고
    • Rheological properties of acid gels prepared from pressure- and transglutaminase-treated skim milk
    • Anema S.G., Lauber S., Lee S.K., Henle T., Klostermeyer H. Rheological properties of acid gels prepared from pressure- and transglutaminase-treated skim milk. Food Hydrocolloids 2005, 19:879-887.
    • (2005) Food Hydrocolloids , vol.19 , pp. 879-887
    • Anema, S.G.1    Lauber, S.2    Lee, S.K.3    Henle, T.4    Klostermeyer, H.5
  • 4
    • 33846096748 scopus 로고    scopus 로고
    • Improvement of enzymatic cross-linking of casein micelles with transglutaminase by glutathione addition
    • Bönisch M.P., Lauber S., Kulozik U. Improvement of enzymatic cross-linking of casein micelles with transglutaminase by glutathione addition. International Dairy Journal 2007, 17:3-11.
    • (2007) International Dairy Journal , vol.17 , pp. 3-11
    • Bönisch, M.P.1    Lauber, S.2    Kulozik, U.3
  • 9
    • 69749099831 scopus 로고    scopus 로고
    • Laccase-aided protein modification: effects on the structural properties of acidified sodium caseinate gels
    • Ercili Cura D., Lantto R., Lille M., Andberg M., Kruus K., Buchert J. Laccase-aided protein modification: effects on the structural properties of acidified sodium caseinate gels. International Dairy Journal 2009, 19:737-745.
    • (2009) International Dairy Journal , vol.19 , pp. 737-745
    • Ercili Cura, D.1    Lantto, R.2    Lille, M.3    Andberg, M.4    Kruus, K.5    Buchert, J.6
  • 10
    • 0000326990 scopus 로고
    • Transglutaminase (guinea pig liver)
    • Academic Press, New York, USA, Metabolism of amino acids and amines
    • Folk J.E. Transglutaminase (guinea pig liver). Methods in enzymology 1970, Vol. 17. Part 1, Academic Press, New York, USA, (pp. 889-894).
    • (1970) Methods in enzymology , vol.17 , Issue.PART 1 , pp. 889-894
    • Folk, J.E.1
  • 12
    • 57849121085 scopus 로고    scopus 로고
    • Heat-induced aggregation of whey proteins in the presence of κ-casein or sodium caseinate
    • Guyomarc'h F., Nono M., Nicolai T., Durand D. Heat-induced aggregation of whey proteins in the presence of κ-casein or sodium caseinate. Food Hydrocolloids 2009, 23:1103-1110.
    • (2009) Food Hydrocolloids , vol.23 , pp. 1103-1110
    • Guyomarc'h, F.1    Nono, M.2    Nicolai, T.3    Durand, D.4
  • 13
    • 13244258458 scopus 로고    scopus 로고
    • Characterization of a new tyrosinase from Pycnoporus species with high potential for food technological applications
    • Halaouli S. Characterization of a new tyrosinase from Pycnoporus species with high potential for food technological applications. Journal of Applied Microbiology 2005, 98:332-343.
    • (2005) Journal of Applied Microbiology , vol.98 , pp. 332-343
    • Halaouli, S.1
  • 14
    • 40649122040 scopus 로고    scopus 로고
    • Structure and stability of nanogel particles prepared by internal cross-linking of casein micelles
    • Huppertz T., De Kruif C.G. Structure and stability of nanogel particles prepared by internal cross-linking of casein micelles. International Dairy Journal 2008, 18:556-565.
    • (2008) International Dairy Journal , vol.18 , pp. 556-565
    • Huppertz, T.1    De Kruif, C.G.2
  • 15
    • 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, 222:407-411.
    • (1984) Biochemical Journal , vol.222 , pp. 407-411
    • Ito, S.1    Kato, T.2    Shinpo, K.3    Fujita, K.4
  • 16
    • 33645726443 scopus 로고    scopus 로고
    • Transglutaminase in dairy products: chemistry, physics, applications
    • Jaros D., Partschefeld C., Henle T., Rohm H. Transglutaminase in dairy products: chemistry, physics, applications. Journal of Texture Studies 2006, 37:113-155.
    • (2006) Journal of Texture Studies , vol.37 , pp. 113-155
    • Jaros, D.1    Partschefeld, C.2    Henle, T.3    Rohm, H.4
  • 17
    • 0022472726 scopus 로고
    • Tyrosinase-catalyzed binding of 3,4-dihydroxyphenylalanine with proteins through the sulfhydryl group
    • Kato T., Ito S., Fujita K. Tyrosinase-catalyzed binding of 3,4-dihydroxyphenylalanine with proteins through the sulfhydryl group. Biochimica et Biophysica Acta 1986, 881:415-421.
    • (1986) Biochimica et Biophysica Acta , vol.881 , pp. 415-421
    • Kato, T.1    Ito, S.2    Fujita, K.3
  • 18
    • 40549146770 scopus 로고    scopus 로고
    • Acid skim milk gels: the gelation process as affected by preheating pH
    • Lakemond C.M.M., van Vliet T. Acid skim milk gels: the gelation process as affected by preheating pH. International Dairy Journal 2008, 18:574-584.
    • (2008) International Dairy Journal , vol.18 , pp. 574-584
    • Lakemond, C.M.M.1    van Vliet, T.2
  • 19
    • 40649105711 scopus 로고    scopus 로고
    • Rheological properties of acid skim milk gels as affected by the spatial distribution of the structural elements and the interaction forces between them
    • Lakemond C.M.M., van Vliet T. Rheological properties of acid skim milk gels as affected by the spatial distribution of the structural elements and the interaction forces between them. International Dairy Journal 2008, 18:585-593.
    • (2008) International Dairy Journal , vol.18 , pp. 585-593
    • Lakemond, C.M.M.1    van Vliet, T.2
  • 20
    • 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., 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 2005, 53:9231-9237.
    • (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
  • 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, 55:1248-1255.
    • (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
  • 22
    • 0031752754 scopus 로고    scopus 로고
    • Effects of interactions between denaturated whey proteins and casein micelles on the formation and rheological properties of acid skim milk gels
    • Lucey J.A., Tamehana M., Singh H., Munro P.A. Effects of interactions between denaturated whey proteins and casein micelles on the formation and rheological properties of acid skim milk gels. Journal of Dairy Research 1998, 65:555-567.
    • (1998) Journal of Dairy Research , vol.65 , pp. 555-567
    • Lucey, J.A.1    Tamehana, M.2    Singh, H.3    Munro, P.A.4
  • 23
    • 0033826687 scopus 로고    scopus 로고
    • Rheological properties of milk gels formed by a combination of rennet and glucono-delta-lactone
    • Lucey J.A., Tamehana M., Singh H., Munro P.A. Rheological properties of milk gels formed by a combination of rennet and glucono-delta-lactone. Journal of Dairy Research 2000, 67:415-427.
    • (2000) Journal of Dairy Research , vol.67 , pp. 415-427
    • Lucey, J.A.1    Tamehana, M.2    Singh, H.3    Munro, P.A.4
  • 24
    • 0034871048 scopus 로고    scopus 로고
    • Effect of heat treatment on the physical properties of milk gels made with both rennet and acid
    • Lucey J.A., Tamehana M., Singh H., Munro P.A. Effect of heat treatment on the physical properties of milk gels made with both rennet and acid. International Dairy Journal 2001, 11:559-565.
    • (2001) International Dairy Journal , vol.11 , pp. 559-565
    • Lucey, J.A.1    Tamehana, M.2    Singh, H.3    Munro, P.A.4
  • 25
    • 84986520447 scopus 로고
    • Modification of proteins by polyphenol oxidase and peroxidase and their products
    • Matheis G., Whitaker J.R. Modification of proteins by polyphenol oxidase and peroxidase and their products. Journal of Food Biochemistry 1984, 8:137-162.
    • (1984) Journal of Food Biochemistry , vol.8 , pp. 137-162
    • Matheis, G.1    Whitaker, J.R.2
  • 26
    • 37349070966 scopus 로고    scopus 로고
    • Oxidation of peptides and proteins by Trichoderma reesei and Agaricus bisporus tyrosinases
    • Mattinen M.L., Lantto R., Selinheimo E., Kruus K., Buchert J. Oxidation of peptides and proteins by Trichoderma reesei and Agaricus bisporus tyrosinases. Journal of Biotechnology 2008, 133:395-402.
    • (2008) Journal of Biotechnology , vol.133 , pp. 395-402
    • Mattinen, M.L.1    Lantto, R.2    Selinheimo, E.3    Kruus, K.4    Buchert, J.5
  • 27
    • 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.L. Cross-linking of β-casein by Trichoderma reesei tyrosinase and Streptoverticillium mobaraense transglutaminase followed by SEC-MALLS. Food Hydrocolloids 2009, 23:2008-2015.
    • (2009) Food Hydrocolloids , vol.23 , pp. 2008-2015
    • Monogioudi, E.1    Creusot, N.2    Kruus, K.3    Gruppen, H.4    Buchert, J.5    Mattinen, M.L.6
  • 28
    • 33947699947 scopus 로고    scopus 로고
    • Effect of transglutaminase on rheological properties and microstructure of chemically acidified sodium caseinate gels
    • Myllärinen P., Buchert J., Autio K. Effect of transglutaminase on rheological properties and microstructure of chemically acidified sodium caseinate gels. International Dairy Journal 2007, 17:800-807.
    • (2007) International Dairy Journal , vol.17 , pp. 800-807
    • Myllärinen, P.1    Buchert, J.2    Autio, K.3
  • 29
    • 77953912568 scopus 로고    scopus 로고
    • Gelling properties of tyrosinase-treated dairy proteins
    • Onwulata C.I., Tomasula P.M. Gelling properties of tyrosinase-treated dairy proteins. Food Bioprocess Technology 2008, 3:554-560.
    • (2008) Food Bioprocess Technology , vol.3 , pp. 554-560
    • Onwulata, C.I.1    Tomasula, P.M.2
  • 31
    • 85053591293 scopus 로고
    • Tyrosinase
    • CRC Press Inc, Boca Raton, FL., USA
    • Robb D.A. Tyrosinase. Copper proteins and copper enzymes 1984, Vol. 2. CRC Press Inc, Boca Raton, FL., USA, (pp. 207-240).
    • (1984) Copper proteins and copper enzymes , vol.2 , pp. 207-240
    • Robb, D.A.1
  • 32
    • 33846195491 scopus 로고    scopus 로고
    • Relation between pH-induced stickiness and gelation behaviour of sodium caseinate aggregates as determined by light scattering and rheology
    • Ruis H.G.M., Venema P., van der Linden E. Relation between pH-induced stickiness and gelation behaviour of sodium caseinate aggregates as determined by light scattering and rheology. Food Hydrocolloids 2007, 21:545-554.
    • (2007) Food Hydrocolloids , vol.21 , pp. 545-554
    • Ruis, H.G.M.1    Venema, P.2    van der Linden, E.3
  • 33
    • 0033673716 scopus 로고    scopus 로고
    • Cross-linking casein micelles by a microbial transglutaminase: influence of cross-links in acid-induced gelation
    • Schorsch C., Carrie H., Norton I.T. Cross-linking casein micelles by a microbial transglutaminase: influence of cross-links in acid-induced gelation. International Dairy Journal 2000, 10:529-539.
    • (2000) International Dairy Journal , vol.10 , pp. 529-539
    • Schorsch, C.1    Carrie, H.2    Norton, I.T.3
  • 37
    • 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, 273:4322-4335.
    • (2006) FEBS Journal , vol.273 , pp. 4322-4335
    • Selinheimo, E.1    Saloheimo, M.2    Ahola, E.3    Westerholm-Parvinen, A.4    Kalkkinen, N.5    Buchert, J.6
  • 42
    • 0043241649 scopus 로고    scopus 로고
    • Casein-whey protein interactions in heated milk: the influence of pH
    • Vasbinder A.J., de Kruif C.G. Casein-whey protein interactions in heated milk: the influence of pH. International Dairy Journal 2003, 13:669-677.
    • (2003) International Dairy Journal , vol.13 , pp. 669-677
    • Vasbinder, A.J.1    de Kruif, C.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.