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Volumn 15, Issue 6, 2012, Pages 1286-1299

Cross-linking and glucosamine conjugation of casein by transglutaminase and the emulsifying property and digestibility in vitro of the modified product

Author keywords

Casein; Cross linking; Emulsifying property; Glucosamine; Transglutaminase

Indexed keywords

ACYL ACCEPTOR; ACYL DONORS; ELECTROPHORETIC ANALYSIS; EMULSIFYING ACTIVITY INDICES; EMULSIFYING PROPERTY; EMULSIFYING STABILITIES; EVALUATION RESULTS; FOOD PROTEINS; FUNCTIONAL PROPERTIES; HPLC ANALYSIS; IN-VITRO; MICROBIAL TRANSGLUTAMINASE; MODIFICATION METHODS; MODIFIED PRODUCTS; MOLAR RATIO; PREPARATION CONDITIONS; REACTION TEMPERATURE; SURFACE HYDROPHOBICITY; TRANSGLUTAMINASES;

EID: 84866403945     PISSN: 10942912     EISSN: 15322386     Source Type: Journal    
DOI: 10.1080/10942912.2010.521274     Document Type: Article
Times cited : (33)

References (40)
  • 1
    • 0036980061 scopus 로고    scopus 로고
    • Protein-protein crosslinking in food: Methods, consequences, applications
    • Gerrard, J.A. Protein-protein crosslinking in food: Methods, consequences, applications. Trends in Food Science and Technology 2002, 13 (12), 391-399.
    • (2002) Trends in Food Science and Technology , vol.13 , Issue.12 , pp. 391-399
    • Gerrard, J.A.1
  • 2
    • 1542708368 scopus 로고    scopus 로고
    • Recent advances in enzymatic modifications of food proteins for improving their functional properties
    • Chobert, J.M.; Briand, L.; Guéguen, J.; Popineau, Y.; Larré, C.; Haertlé, T. Recent advances in enzymatic modifications of food proteins for improving their functional properties. Nahrung/Food 2006, 40 (4), 177-182.
    • (2006) Nahrung/Food , vol.40 , Issue.4 , pp. 177-182
    • Chobert, J.M.1    Briand, L.2    Guéguen, J.3    Popineau, Y.4    Larré, C.5    Haertlé, T.6
  • 3
    • 34248180100 scopus 로고    scopus 로고
    • Texturisation and modification of vegetable proteins for food applications using microbial transglutaminase
    • Dube, M.; Schäfer, C.; Neidhart, S.; Carle, R. Texturisation and modification of vegetable proteins for food applications using microbial transglutaminase. European Food Research and Technology 2007, 225 (2), 287-299.
    • (2007) European Food Research and Technology , vol.225 , Issue.2 , pp. 287-299
    • Dube, M.1    Schäfer, C.2    Neidhart, S.3    Carle, R.4
  • 4
    • 69749099831 scopus 로고    scopus 로고
    • Laccase aided protein modification: Effects on the structural properties of acidified sodium caseinate gels
    • Cura, D.E.; 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 (12), 737-745.
    • (2009) International Dairy Journal , vol.19 , Issue.12 , pp. 737-745
    • Cura, D.E.1    Lantto, R.2    Lille, M.3    Andberg, M.4    Kruus, K.5    Buchert, J.6
  • 5
    • 0001175368 scopus 로고
    • Modification of whey protein to improve functionality
    • Kester, J.J.; Richardson, T. Modification of whey protein to improve functionality. Journal of Dairy Science 1984, 67 (11), 2757-2774.
    • (1984) Journal of Dairy Science , vol.67 , Issue.11 , pp. 2757-2774
    • Kester, J.J.1    Richardson, T.2
  • 6
    • 0000361330 scopus 로고
    • Physicochemical aspect of whey protein functionality
    • Mangino, M.E. Physicochemical aspect of whey protein functionality. Journal of Dairy Science 1984, 67 (11), 2711-2722.
    • (1984) Journal of Dairy Science , vol.67 , Issue.11 , pp. 2711-2722
    • Mangino, M.E.1
  • 7
    • 0037125110 scopus 로고    scopus 로고
    • Solubility improvement of shellfish muscle proteins by reaction with glucose and its soluble state in low-ionic strength medium
    • Katayama, S.; Shima, J.; Saeki, H. Solubility improvement of shellfish muscle proteins by reaction with glucose and its soluble state in low-ionic strength medium. Journal of Agricultural and Food Chemistry 2002, 50 (15), 4327-4332.
    • (2002) Journal of Agricultural and Food Chemistry , vol.50 , Issue.15 , pp. 4327-4332
    • Katayama, S.1    Shima, J.2    Saeki, H.3
  • 8
    • 33947177578 scopus 로고    scopus 로고
    • Stability and release properties of doubleemulsions stabilised by caseinate-dextran conjugates
    • Fechner, A.; Knoth, A.; Scherze, I.; Muschiolik, G. Stability and release properties of doubleemulsions stabilised by caseinate-dextran conjugates. Food Hydrocolloids 2007, 21 (5-6), 943-952.
    • (2007) Food Hydrocolloids , vol.21 , Issue.5-6 , pp. 943-952
    • Fechner, A.1    Knoth, A.2    Scherze, I.3    Muschiolik, G.4
  • 9
    • 0035117850 scopus 로고    scopus 로고
    • Functional improvement of whey protein concentrate on interaction with pectin
    • Mishra, S.; Mann, B.; Joshi, V.K. Functional improvement of whey protein concentrate on interaction with pectin. Food Hydrocolloids 2001, 15 (1): 9-15.
    • (2001) Food Hydrocolloids , vol.15 , Issue.1 , pp. 9-15
    • Mishra, S.1    Mann, B.2    Joshi, V.K.3
  • 10
    • 29144447015 scopus 로고    scopus 로고
    • Improvement of functional properties of whey protein isolate through glycation and phosphorylation by dry heating
    • Li, C.P.; Enomoto, H.; Ohki, S.; Ohtomo, H.; Aoki, T. Improvement of functional properties of whey protein isolate through glycation and phosphorylation by dry heating. Journal of Dairy Science 2005, 88 (12), 4137-4145.
    • (2005) Journal of Dairy Science , vol.88 , Issue.12 , pp. 4137-4145
    • Li, C.P.1    Enomoto, H.2    Ohki, S.3    Ohtomo, H.4    Aoki, T.5
  • 11
    • 34547672904 scopus 로고    scopus 로고
    • Functional properties of melanoidins: In vitro antioxidant, antimicrobial and antihypertensive activities
    • Rufián-Henares, J.A.; Morales, F.J. Functional properties of melanoidins: In vitro antioxidant, antimicrobial and antihypertensive activities. Food Research International 2007, 40 (8), 995-1002.
    • (2007) Food Research International , vol.40 , Issue.8 , pp. 995-1002
    • Rufián-Henares, J.A.1    Morales, F.J.2
  • 12
    • 67651002133 scopus 로고    scopus 로고
    • Functional properties of milk proteins as affected by enzymatic oligomerisation
    • Hiller, B.; Lorenzen, P.C. Functional properties of milk proteins as affected by enzymatic oligomerisation. Food Research International 2009, 42 (8), 899-908.
    • (2009) Food Research International , vol.42 , Issue.8 , pp. 899-908
    • Hiller, B.1    Lorenzen, P.C.2
  • 18
    • 0032877391 scopus 로고    scopus 로고
    • Transglutaminase-mediated amine incorporation into substance P protects the peptide against proteolysis in vitro
    • Esposito, C.; Costa, C.; Amoresano, A.; Mariniello, L.; Sommella, M.G.; Caputo, I.; Porta, R. Transglutaminase-mediated amine incorporation into substance P protects the peptide against proteolysis in vitro. Regulatory Peptides 1999, 84 (1-3), 75-80.
    • (1999) Regulatory Peptides , vol.84 , Issue.1-3 , pp. 75-80
    • Esposito, C.1    Costa, C.2    Amoresano, A.3    Mariniello, L.4    Sommella, M.G.5    Caputo, I.6    Porta, R.7
  • 19
    • 0034883031 scopus 로고    scopus 로고
    • Substance p its transglutaminase-synthesized derivatives elicit yawning behaviour via nitric oxide in rats
    • Mancuso, F.; Porta, R.; Calignano, A.; Di Pierro, P.; Sommella, M.C.; Esposito, C. Substance P and its transglutaminase-synthesized derivatives elicit yawning behaviour via nitric oxide in rats. Peptides 2001, 22 (9), 1453-1457.
    • (2001) Peptides , vol.22 , Issue.9 , pp. 1453-1457
    • Mancuso, F.1    Porta, R.2    Calignano, A.3    Di Pierro, P.4    Sommella, M.C.5    Esposito, C.6
  • 23
    • 0038417840 scopus 로고    scopus 로고
    • Enzyme-catalyzed gel formation of gelatin and chitosan: Potential for in situ applications
    • Chen, T.H.; Embree, H.D.; Brown, E.M.; Taylor, M.M.; Payne, G.F. Enzyme-catalyzed gel formation of gelatin and chitosan: Potential for in situ applications. Biomaterials 2003, 24 (17), 2831-2841.
    • (2003) Biomaterials , vol.24 , Issue.17 , pp. 2831-2841
    • Chen, T.H.1    Embree, H.D.2    Brown, E.M.3    Taylor, M.M.4    Payne, G.F.5
  • 25
    • 57149112544 scopus 로고    scopus 로고
    • Effect of conjugation with glucosamine on the functional properties of lysozyme and casein
    • Ramezani, R.; Esmailpour, M.; Aminlari, M. Effect of conjugation with glucosamine on the functional properties of lysozyme and casein. Journal of the Science of Food and Agriculture 2008, 88 (15), 2730-2737.
    • (2008) Journal of the Science of Food and Agriculture , vol.88 , Issue.15 , pp. 2730-2737
    • Ramezani, R.1    Esmailpour, M.2    Aminlari, M.3
  • 26
    • 33847091761 scopus 로고    scopus 로고
    • Study of some functional properties of casein: Effect of pH and tryptic hydrolysis
    • Biasutti, E.A.R.; Vieira, C.R.; Capobiango, M. Study of some functional properties of casein: Effect of pH and tryptic hydrolysis. International Journal of Food Properties 2007, 10 (1), 173-183.
    • (2007) International Journal of Food Properties , vol.10 , Issue.1 , pp. 173-183
    • Biasutti, E.A.R.1    Vieira, C.R.2    Capobiango, M.3
  • 27
    • 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
  • 29
    • 20444499789 scopus 로고    scopus 로고
    • Application of capillary zone electrophoresis and reversedphase high-performance liquid chromatography in the biopharmaceutical industry for the quantitative analysis of the monosaccharides released from a highly glycosylated therapeutic protein
    • Ra?aityte, K.; Kiessig, S.; Kálmán, F. Application of capillary zone electrophoresis and reversedphase high-performance liquid chromatography in the biopharmaceutical industry for the quantitative analysis of the monosaccharides released from a highly glycosylated therapeutic protein. Journal of Chromatography A 2005, 1079 (1-2), 354-365.
    • (2005) Journal of Chromatography A , vol.1079 , Issue.1-2 , pp. 354-365
    • Racaityte, K.1    Kiessig, S.2    Kálmán, F.3
  • 30
    • 24144467835 scopus 로고    scopus 로고
    • Physicochemical and structural characteristics of sodium caseinate biopolymers induced by microbial transglutaminase
    • Tang, C.H.; Yang, X.Q.; Chen, Z.;Wu, H.; Peng, Z.Y. Physicochemical and structural characteristics of sodium caseinate biopolymers induced by microbial transglutaminase. Journal of Food Biochemistry 2005, 29 (4), 402-421.
    • (2005) Journal of Food Biochemistry , vol.29 , Issue.4 , pp. 402-421
    • Tang, C.H.1    Yang, X.Q.2    Chen, Z.3    Wu, H.4    Peng, Z.Y.5
  • 31
    • 33947092713 scopus 로고
    • Emulsifying properties of proteins: Evaluation of a turbidimetric technique
    • Pearce, K.N.; Kinsella, J.E. Emulsifying properties of proteins: Evaluation of a turbidimetric technique. Journal of Agricultural and Food Chemistry 1978, 26 (3), 716-723.
    • (1978) Journal of Agricultural and Food Chemistry , vol.26 , Issue.3 , pp. 716-723
    • Pearce, K.N.1    Kinsella, J.E.2
  • 32
    • 68849116240 scopus 로고    scopus 로고
    • Influence of nonenzymatic glycosylation (glycation) of pea protein (pisum sativum) on their susceptibility to enzymatic hydrolysis
    • Marciniak-Darmochwall, K.; Kostyra, H. Influence of nonenzymatic glycosylation (glycation) of pea protein (pisum sativum) on their susceptibility to enzymatic hydrolysis. Journal of Food Biochemistry 2009, 33 (4), 506-521.
    • (2009) Journal of Food Biochemistry , vol.33 , Issue.4 , pp. 506-521
    • Marciniak-Darmochwall, K.1    Kostyra, H.2
  • 33
    • 76349104429 scopus 로고    scopus 로고
    • The relationships between physicochemical properties and conformational features of succinylated and acetylated kidney bean (phaseolus vulgaris l.) protein isolates
    • Yin, S.W.; Tang, C.H.; Wen, Q.B.; Yang, X.Q.; Yuan, D.B. The relationships between physicochemical properties and conformational features of succinylated and acetylated kidney bean (Phaseolus vulgaris L.) protein isolates. Food Research International 2010, 43 (3), 730-738.
    • (2010) Food Research International , vol.43 , Issue.3 , pp. 730-738
    • Yin, S.W.1    Tang, C.H.2    Wen, Q.B.3    Yang, X.Q.4    Yuan, D.B.5
  • 34
    • 0031253029 scopus 로고    scopus 로고
    • Characterization by ionisation mass spectrometry of lactosyl β-lactoglobulin conjugates formed during heat treatment of milk and whey and identification of one lactose binding site
    • Leonil, J.; Molle, D.; Fauquant, J.; Maubois, J.L.; Pearce, R.J.; Bouhallab, S. Characterization by ionisation mass spectrometry of lactosyl β-lactoglobulin conjugates formed during heat treatment of milk and whey and identification of one lactose binding site. Journal of Dairy Science 1997, 80 (10), 2270-2281.
    • (1997) Journal of Dairy Science , vol.80 , Issue.10 , pp. 2270-2281
    • Leonil, J.1    Molle, D.2    Fauquant, J.3    Maubois, J.L.4    Pearce, R.J.5    Bouhallab, S.6
  • 35
    • 0037214940 scopus 로고    scopus 로고
    • Functional properties of bacillus proteinase hydrolysates of sodium caseinate incubated with transglutaminase pre- and post-hydrolysis
    • Flanagan, J.; FitzGerald, R.J. Functional properties of Bacillus proteinase hydrolysates of sodium caseinate incubated with transglutaminase pre- and post-hydrolysis. International Dairy Journal 2003, 13 (2-3), 135-143.
    • (2003) International Dairy Journal , vol.13 , Issue.2-3 , pp. 135-143
    • Flanagan, J.1    Fitzgerald, R.J.2
  • 36
    • 33749608762 scopus 로고    scopus 로고
    • β-Lactoglobulin-dextran-Maillard conjugates: Their effect on interfacial thickness and emulsion stability
    • Wooster, T.J.; Augustin, M.A. β-Lactoglobulin-dextran-Maillard conjugates: Their effect on interfacial thickness and emulsion stability. Journal of Colloid Interface Science 2006, 303 (2), 564-572.
    • (2006) Journal of Colloid Interface Science , vol.303 , Issue.2 , pp. 564-572
    • Wooster, T.J.1    Augustin, M.A.2
  • 37
    • 2442481757 scopus 로고    scopus 로고
    • Cross-linking by transglutaminase changes neither the in vitro proteolysis nor the in vivo digestibility of caseinate
    • Roos, N.; Lorenzen, P.C.; Sick, H.; Schrezenmeir, J.; Schlimme, E. Cross-linking by transglutaminase changes neither the in vitro proteolysis nor the in vivo digestibility of caseinate. Kieler Milchwirtschaftliche Forschungsberichte 2003, 55 (4), 261-276.
    • (2003) Kieler Milchwirtschaftliche Forschungsberichte , vol.55 , Issue.4 , pp. 261-276
    • Roos, N.1    Lorenzen, P.C.2    Sick, H.3    Schrezenmeir, J.4    Schlimme, E.5
  • 39
    • 23644445987 scopus 로고    scopus 로고
    • Glycosylation of β-lactoglobulin lowers the heat capacity change of unfolding: A unique way to affect protein thermodynamics
    • van Teeffelen, A.M.M.; Broersen, K.; de Jongh, H.H.J. Glycosylation of β-lactoglobulin lowers the heat capacity change of unfolding: A unique way to affect protein thermodynamics. Protein Science 2005, 14 (8), 2187-2194.
    • (2005) Protein Science , vol.14 , Issue.8 , pp. 2187-2194
    • Van Teeffelen, A.M.M.1    Broersen, K.2    De Jongh, H.H.J.3
  • 40
    • 67349288437 scopus 로고    scopus 로고
    • Optimization of Maillard reaction products from casein- glucose using response surface methodology
    • Gu, F.L.; Abbas, S.; Zhang, X.M. Optimization of Maillard reaction products from casein- glucose using response surface methodology. LWT-Food Science and Technology 2009, 42 (8), 1374-1379.
    • (2009) LWT-Food Science and Technology , vol.42 , Issue.8 , pp. 1374-1379
    • Gu, F.L.1    Abbas, S.2    Zhang, X.M.3


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