Emulsifying Properties of Cross-Linking Between Proteins Extracted from Cold/Hot Pressed Peanut Meal and Hydrolysed Fish (Decapterus Maruadsi) Proteins

REFERENCES

• FAO, Food and Agriculture Organization Statistics (FAOSTAT). http://faostat.fao.org/site/567/DesktopDefault.aspx?PageID=567#ancor ( accessed August 5, 2012.)
   Google Scholar
• Singh, B.; Singh, U. Peanut as a source of protein for human foods. Plant Foods for Human Nutrition 1991, 41, 165–177.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• 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.
   Web of Science ®Google Scholar
• Kristinsson, H.G.; Rasco, B.A. Fish protein hydrolysates: Production, biochemical, and functional properties. Critical Reviews in Food Science and Nutrition 2000, 40, 43–81.
   PubMed Web of Science ®Google Scholar
• Ando, H.; Adachi, M.; Umeda, K.; Matsuura, A.; Nonaka, M.; Uchio, R.; Tanaka, H.; Motoki, M. Purification and characteristics of a novel transglutaminase derived from microorganism. Agricultural and Biological Chemistry 1989, 53, 2613–2617.
   Web of Science ®Google Scholar
• Oner, Z.; Karahan, A.G.; Aydemir, S.; Sanlidere Aloglu, H. Effect of transglutaminase on physicochemical properties of set-style yogurt. International Journal of Food Properties 2008, 11 (1), 196–205.
   Web of Science ®Google Scholar
• Lin, C.F.; Wang, Y.T.; Wu, J.S.B. Modification in physical properties of rice gel by microbial transglutaminase. Journal of the Science of Food and Agriculture 2009, 89, 477–481.
   Web of Science ®Google Scholar
• 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.
   Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• 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.
   Web of Science ®Google Scholar
• Babiker, E.E. Effect of transglutaminase treatment on the functional properties of native and chymotrypsin-digested soy protein. Food Chemistry 2000, 70, 139–145.
   Web of Science ®Google Scholar
• Flanagan, J.; FitzGerald, R.J. Physicochemical and nitrogen solubility properties of bacillus proteinase hydrolysates of sodium caseinate incubated with transglutaminase pre- and post-hydrolysis. Journal of Agricultural and Food Chemistry 2002, 50, 5429–5436.
   PubMed Web of Science ®Google Scholar
• 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.
   Web of Science ®Google Scholar
• 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.
   Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• 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.
   Web of Science ®Google Scholar
• Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 1970, 227, 680–685.
   PubMed Web of Science ®Google Scholar
• 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.
   Web of Science ®Google Scholar
• 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.
   Web of Science ®Google Scholar
• 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.
   Web of Science ®Google Scholar
• Chiou, R.Y.Y. Effects of heat treatments on peanut arachin and conarachin. Journal of Food Biochemistry 1990, 14, 219–232.
   Web of Science ®Google Scholar
• 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.
   PubMedGoogle Scholar
• Poon, S.; Clarke, A.E.; Schultz, C.J. Effect of denaturants on the emulsifying activity of proteins. Journal of Agricultural and Food Chemistry 2001, 49, 281–286.
   PubMed Web of Science ®Google Scholar
• Silva, A.C.C.; Arêas, E.P.G.; Silva, M.A.; Arêas, J.A.G. Effects of extrusion on the emulsifying properties of rumen and soy protein. Food Biophysics 2010, 5, 94–102.
   Web of Science ®Google Scholar
• 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.
   Web of Science ®Google Scholar
• 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.
   Google Scholar
• 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.
   Web of Science ®Google Scholar
• Mun, S.; McClements, D.J.; Surh, J. Influence of maltodextrin addition on the freeze-dry stability of β-lactoglobulin-based emulsions with controlled electrostatic and/or steric interactions. Food Science and Biotechnology 2011, 20 (4), 1143–1150.
   Web of Science ®Google Scholar
• 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.
   Web of Science ®Google Scholar