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Volumn 17, Issue 8, 2014, Pages 1750-1762

Emulsifying properties of cross-linking between proteins extracted from cold/hot pressed peanut meal and hydrolysed fish (decapterus maruadsi) proteins

Author keywords

Cold pressed peanut protein; Emulsifying properties; Fish protein hydrolysate; Hot pressed peanut protein; Transglutaminase

Indexed keywords

AMINO ACIDS; ELECTROPHORESIS; EMULSIFICATION; FISH; HYDROLYSIS; PROTEINS;

EID: 84899823421     PISSN: 10942912     EISSN: 15322386     Source Type: Journal    
DOI: 10.1080/10942912.2012.724755     Document Type: Article
Times cited : (9)

References (32)
  • 2
    • 0026147278 scopus 로고
    • Peanut as a source of protein for human foods
    • Singh, B.; Singh, U. Peanut as a source of protein for human foods. Plant Foods for Human Nutrition 1991, 41, 165-177.
    • (1991) Plant Foods for Human Nutrition , vol.41 , pp. 165-177
    • Singh, B.1    Singh, U.2
  • 3
    • 35348870642 scopus 로고    scopus 로고
    • Properties and microstructure of protein-based film from round scad (Decapterus maruadsi) muscle as affected by palm oil and chitosan incorporation
    • Prodpran, T.; Benjakul, S.; Artharn, A. Properties and microstructure of protein-based film from round scad (Decapterus maruadsi) muscle as affected by palm oil and chitosan incorporation. International Journal of Biological Macromolecules 2007, 41, 605-614.
    • (2007) International Journal of Biological Macromolecules , vol.41 , pp. 605-614
    • Prodpran, T.1    Benjakul, S.2    Artharn, A.3
  • 4
    • 33947527548 scopus 로고    scopus 로고
    • Compositions, functional properties, and antioxidative activity of protein hydrolysates prepared from round scad (Decapterus maruadsi)
    • Thiansilakul, Y.; Benjakul, S.; Shahidi, F. Compositions, functional properties, and antioxidative activity of protein hydrolysates prepared from round scad (Decapterus maruadsi). Food Chemistry 2007, 103, 1385-1394.
    • (2007) Food Chemistry , vol.103 , pp. 1385-1394
    • Thiansilakul, Y.1    Benjakul, S.2    Shahidi, F.3
  • 8
  • 9
    • 77955762508 scopus 로고    scopus 로고
    • Transglutaminase-induced cross-linking and glucosamine conjugation in soybean protein isolates and its impacts on some functional properties of the products
    • Jiang, S.J.; Zhao, X.H. Transglutaminase-induced cross-linking and glucosamine conjugation in soybean protein isolates and its impacts on some functional properties of the products. European Food Research and Technology 2010, 231, 679-689.
    • (2010) European Food Research and Technology , vol.231 , pp. 679-689
    • Jiang, S.J.1    Zhao, X.H.2
  • 10
    • 76749160630 scopus 로고    scopus 로고
    • Enhanced water absorption of wheat gluten by hydrothermal treatment followed by microbial transglutaminase reaction
    • Liu, S.; Zhang, D.X.; Liu, L.;Wang, M.; Du, G.C.; Chen, J. Enhanced water absorption of wheat gluten by hydrothermal treatment followed by microbial transglutaminase reaction. Journal of the Science of Food and Agriculture 2010, 90, 658-663.
    • (2010) Journal of the Science of Food and Agriculture , vol.90 , pp. 658-663
    • Liu, S.1    Zhang, D.X.2    Liu, L.3    Wang, M.4    Du, G.C.5    Chen, J.6
  • 11
    • 80051713269 scopus 로고    scopus 로고
    • Effects of microfluidization treatment and transglutaminase cross-Linking on physicochemical, functional, and conformational properties of peanut protein isolate
    • Hu, X.; Zhao, M.M.; Sun,W.Z.; Zhao, G.L.; Ren, J.Y. Effects of microfluidization treatment and transglutaminase cross-Linking on physicochemical, functional, and conformational properties of peanut protein isolate. Journal of Agricultural and Food Chemistry 2011, 59, 8886-8894.
    • (2011) Journal of Agricultural and Food Chemistry , vol.59 , pp. 8886-8894
    • Hu, X.1    Zhao, M.M.2    Sun, W.Z.3    Zhao, G.L.4    Ren, J.Y.5
  • 12
    • 79957529334 scopus 로고    scopus 로고
    • Application and sensory evaluation of enzymatically texturized vegetable proteins in food models
    • Schäfer, C.; Neidhart, S.; Carle, R. Application and sensory evaluation of enzymatically texturized vegetable proteins in food models. European Food Research and Technology 2011, 232, 1043-1056.
    • (2011) European Food Research and Technology , vol.232 , pp. 1043-1056
    • Schäfer, C.1    Neidhart, S.2    Carle, R.3
  • 13
    • 0034255689 scopus 로고    scopus 로고
    • Effect of transglutaminase treatment on the functional properties of native and chymotrypsin-digested soy protein
    • Babiker, E.E. Effect of transglutaminase treatment on the functional properties of native and chymotrypsin-digested soy protein. Food Chemistry 2000, 70, 139-145.
    • (2000) Food Chemistry , vol.70 , pp. 139-145
    • Babiker, E.E.1
  • 14
    • 0037063376 scopus 로고    scopus 로고
    • Physicochemical and nitrogen solubility properties of bacillus proteinase hydrolysates of sodium caseinate incubated with transglutaminase pre-and posthydrolysis
    • Flanagan, J.; FitzGerald, R.J. Physicochemical and nitrogen solubility properties of bacillus proteinase hydrolysates of sodium caseinate incubated with transglutaminase pre-and posthydrolysis. Journal of Agricultural and Food Chemistry 2002, 50, 5429-5436.
    • (2002) Journal of Agricultural and Food Chemistry , vol.50 , pp. 5429-5436
    • Flanagan, J.1    Fitzgerald, R.J.2
  • 15
    • 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, 135-143.
    • (2003) International Dairy Journal , vol.13 , pp. 135-143
    • Flanagan, J.1    Fitzgerald, R.J.2
  • 16
    • 36348995909 scopus 로고    scopus 로고
    • Influence of salt and pH on the solubility and structural characteristics of transglutaminase-treated wheat gluten hydrolysate
    • Agyare, K.K.; Xiong, Y.L.; Addo, K. Influence of salt and pH on the solubility and structural characteristics of transglutaminase-treated wheat gluten hydrolysate. Food Chemistry 2008, 107, 1131-1137.
    • (2008) Food Chemistry , vol.107 , pp. 1131-1137
    • Agyare, K.K.1    Xiong, Y.L.2    Addo, K.3
  • 17
    • 38049034404 scopus 로고    scopus 로고
    • Purification and identification of antioxidant peptides from grass carp muscle hydrolysates by consecutive chromatography and electrospray ionization-mass spectrometry
    • Ren, J.Y.; Zhao, M.M.; Shi, J.;Wang, J.S.; Jiang, Y.M.; Cui, C.; Kakuda, Y.; Xue, S.J. Purification and identification of antioxidant peptides from grass carp muscle hydrolysates by consecutive chromatography and electrospray ionization-mass spectrometry. Food Chemistry 2008, 108, 727-736.
    • (2008) Food Chemistry , vol.108 , pp. 727-736
    • Ren, J.Y.1    Zhao, M.M.2    Shi, J.3    Wang, J.S.4    Jiang, Y.M.5    Cui, C.6    Kakuda, Y.7    Xue, S.J.8
  • 18
    • 0018536145 scopus 로고
    • Determination of degree of hydrolysis of food protein hydrolysates by trinitrobenzenosulfonic acid
    • Adler-Nissen, J. Determination of degree of hydrolysis of food protein hydrolysates by trinitrobenzenosulfonic acid. Journal of Agricultural and Food Chemistry 1979, 27, 1256-1262.
    • (1979) Journal of Agricultural and Food Chemistry , vol.27 , pp. 1256-1262
    • Adler-Nissen, J.1
  • 19
    • 33645903211 scopus 로고    scopus 로고
    • Effects of transglutaminase treatment on the thermal properties of soy protein isolates
    • Tang, C.H.; Chen, Z.; Li, L.; Yang, X.Q. Effects of transglutaminase treatment on the thermal properties of soy protein isolates. Food Research International 2006, 39, 704-711.
    • (2006) Food Research International , vol.39 , pp. 704-711
    • Tang, C.H.1    Chen, Z.2    Li, L.3    Yang, X.Q.4
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 60149090291 scopus 로고    scopus 로고
    • Effect of degree of hydrolysis on the antioxidant activity of loach (Misgurnus anguillicaudatus) protein hydrolysates
    • You, L.J.; Zhao, M.M.; Cui, C.; Zhao, H.F.; Yang, B. Effect of degree of hydrolysis on the antioxidant activity of loach (Misgurnus anguillicaudatus) protein hydrolysates. Innovative Food Science and Emerging Technologies 2008, 10 (2), 235-240.
    • (2008) Innovative Food Science and Emerging Technologies , vol.10 , Issue.2 , pp. 235-240
    • You, L.J.1    Zhao, M.M.2    Cui, C.3    Zhao, H.F.4    Yang, B.5
  • 22
    • 77950595205 scopus 로고    scopus 로고
    • Effects of limited proteolysis and high-pressure homogenisation on structural and functional characteristics of glycinin
    • Luo, D.H.; Zhao, Q.Z.; Zhao, M.M.; Yang, B.; Long, X.T.; Ren, J.Y.; Zhao, H.F. Effects of limited proteolysis and high-pressure homogenisation on structural and functional characteristics of glycinin. Food Chemistry 2010, 122, 25-30.
    • (2010) Food Chemistry , vol.122 , pp. 25-30
    • Luo, D.H.1    Zhao, Q.Z.2    Zhao, M.M.3    Yang, B.4    Long, X.T.5    Ren, J.Y.6    Zhao, H.F.7
  • 23
    • 79952533269 scopus 로고    scopus 로고
    • Modifications of soy protein isolates using combined extrusion pre-treatment and controlled enzymatic hydrolysis for improved emulsifying properties
    • Chen, L.; Chen, J.S.; Ren, J.Y.; Zhao, M.M. Modifications of soy protein isolates using combined extrusion pre-treatment and controlled enzymatic hydrolysis for improved emulsifying properties. Food Hydrocolloids 2011, 25, 887-897.
    • (2011) Food Hydrocolloids , vol.25 , pp. 887-897
    • Chen, L.1    Chen, J.S.2    Ren, J.Y.3    Zhao, M.M.4
  • 24
    • 84986467045 scopus 로고
    • Effects of heat treatments on peanut arachin and conarachin
    • Chiou, R.Y.Y. Effects of heat treatments on peanut arachin and conarachin. Journal of Food Biochemistry 1990, 14, 219-232.
    • (1990) Journal of Food Biochemistry , vol.14 , pp. 219-232
    • Chiou, R.Y.Y.1
  • 25
    • 0041723403 scopus 로고    scopus 로고
    • Changes in interfacial behaviour, emulsifying, and foaming properties of faba bean legumin after modification with dimethylsuberimidate
    • Krause, J.P.; Dudek, S.; Schwenke, K.D. Changes in interfacial behaviour, emulsifying, and foaming properties of faba bean legumin after modification with dimethylsuberimidate. Nahrung 2000, 44, 403-406.
    • (2000) Nahrung , vol.44 , pp. 403-406
    • Krause, J.P.1    Dudek, S.2    Schwenke, K.D.3
  • 27
    • 77955085756 scopus 로고    scopus 로고
    • Effects of extrusion on the emulsifying properties of rumen and soy protein
    • Silva, A.C.C.; Areas, E.P.G.; Silva, M.A.; Areas, J.A.G. Effects of extrusion on the emulsifying properties of rumen and soy protein. Food Biophysics 2010, 5, 94-102.
    • (2010) Food Biophysics , vol.5 , pp. 94-102
    • Silva, A.C.C.1    Areas, E.P.G.2    Silva, M.A.3    Areas, J.A.G.4
  • 28
    • 79953203868 scopus 로고    scopus 로고
    • Enzymatic hydrolysis and their effects on conformational and functional properties of peanut protein isolate
    • Zhao, G.L.; Liu, Y.; Zhao, M.M.; Ren, J.Y.; Yang, B. Enzymatic hydrolysis and their effects on conformational and functional properties of peanut protein isolate. Food Chemistry 2011, 127, 1438-1443.
    • (2011) Food Chemistry , vol.127 , pp. 1438-1443
    • Zhao, G.L.1    Liu, Y.2    Zhao, M.M.3    Ren, J.Y.4    Yang, B.5
  • 29
    • 0033022220 scopus 로고    scopus 로고
    • Effect of a microbial calcium-independent transglutaminase on functional properties of a partially purified cowpea (Vigna unguiculata) globulin
    • Aluko, R.E.; Yada, R.Y. Effect of a microbial calcium-independent transglutaminase on functional properties of a partially purified cowpea (Vigna unguiculata) globulin. Journal of the Science of Food and Agriculture 1999, 79, 286-290.
    • (1999) Journal of the Science of Food and Agriculture , vol.79 , pp. 286-290
    • Aluko, R.E.1    Yada, R.Y.2
  • 30
    • 23744480550 scopus 로고    scopus 로고
    • Functional and thermal properties of wheat, barley, and soy flours and their blends treated with a microbial transglutaminase
    • Ahn, H.J.; Kim, J.H.; Ng, P.K.W. Functional and thermal properties of wheat, barley, and soy flours and their blends treated with a microbial transglutaminase. Journal of Food Science 2005, 70, 380-386.
    • (2005) Journal of Food Science , vol.70 , pp. 380-386
    • Ahn, H.J.1    Kim, J.H.2    Ng, P.K.W.3
  • 31
    • 80053968755 scopus 로고    scopus 로고
    • Influence of maltodextrin addition on the freeze-dry stability of ?-lactoglobulin-based emulsions with controlled electrostatic and/or steric interactions
    • Mun, S.; McClements, D.J.; Surh, J. Influence of maltodextrin addition on the freeze-dry stability of ?-lactoglobulin-based emulsions with controlled electrostatic and/or steric interactions. Food Science and Biotechnology 2011, 20 (4), 1143-1150.
    • (2011) Food Science and Biotechnology , vol.20 , Issue.4 , pp. 1143-1150
    • Mun, S.1    McClements, D.J.2    Surh, J.3
  • 32
    • 85025323198 scopus 로고
    • Changes caused by microbial transglutaminase on physical properties of thermally induced soy protein gels
    • Nonaka, M.; Toiguchi, S.; Sakamoto, H.; Kawajiri, H.; Soeda, T.; Motoki, M. Changes caused by microbial transglutaminase on physical properties of thermally induced soy protein gels. Food Hydrocolloids 1994, 8, 1-8.
    • (1994) Food Hydrocolloids , vol.8 , pp. 1-8
    • Nonaka, M.1    Toiguchi, S.2    Sakamoto, H.3    Kawajiri, H.4    Soeda, T.5    Motoki, M.6


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