[1] 赵新淮, 食品化学[M]. 北京:化学工业出版社, 2006: 62~65[2] KOBAYSSHI K, KATO A. Developments in new functional food materials by hybridization of soy protein to polysaccharides[J]. Nutritional Science of Soy Protein, 1992, 13(1):15-21.[3] DICKINSON E, MCCLEMENTS D J. Advances in food colloids[M]. Blackie Academic and Professional, 1996.[4] MU L X, ZHAO H F, ZHAO M M, et al. Physicochemical properties of soy protein isolates-acacia gum conjugates[J]. Czech Journal of Food Sciences, 2011, 29(2):129-136. [5] KATO Y, MATSUDA T, KATO N, et al. Browning and insolubilization of ovalbumin by the Maillard reaction with some aldohexoses[J]. Journal of Agricultural and Food Chemistry, 1986, 34(2): 351-355.[6] SATO R, SAWABE T, KISHIMURA H, et.al. Preparation of neoglycoprotein from carp myofibrillar protein and alginate oligosaccharide: improved solubility in low ionic strength medium[J]. Journal of Agricultural and Food Chemistry, 2000,48(1):17-21.[7] SAEKI H, AND INOUE K. Improved solubility of carp myofibrillar proteins in low ionic strength medium by glycosylation[J]. Journal of Agricultural and Food Chemistry, 1997, 45(9):3419-3422.[8] MATSUDOMI N, INOUE Y. Emulsion stabilization by Maillard-type covalent complex of plsama protein with galactomannan[J]. Journal of Food Science, 1995, 60(2): 265-268.[9] SHU Y W, SAHARA S. Effect of the length of polysaccharide chains on the functional properties of the maillard-type lysozyme-polysaccharide conjugates[J]. Journal of Agricultural and Food Chemistry, 1996, 44(9): 2544-2548.[10] BABIKER E E. Effect of chitosan conjugation on the functional properties and bactericidal activity of gluten peptides[J]. Food chemistry, 2002, 79(3):367-372. [11] 齐军茹,杨晓泉,彭志英. 大豆蛋白-多糖复合物的制备及乳化性能的研究[J]. 食品科学, 2003, 24(11): 34–37.[12] DIFTIS N, KIOSSEOGLOU V. Physicochemical properties of dry-heated soy protein isolate-dextran mixtures[J]. Food Chemistry, 2006, 96(2): 228-233.[13] CHEVALIER F, HOBERT M, POPINEAU Y, et al. Improvement of functional properties of β-lactoglobulin glycated through the Maillard reaction is related to the nature of the sugar[J]. International Dairy Journal, 2001, 11(3):145-152.[14] HANDA A, KURODA N. Functional improvements in dried egg white through the Maillard reaction[J]. Journal of Agricultural and Food Chemistry, 1999, 47(5): 1845-1850.[15] ARMSTRONG H J, HILL S E, SCHROOYEN P, et al. A comparison of the viscoelastic properties of conventional and Maillard protein gels[J]. Journal of Texture Studies, 1994, 25(3):285-298.[16] RICH L M, FOEGEDING E A. Effects of sugars on whey protein isolate gelation[J]. Journal of Agricultural and Food Chemistry, 2000, 48(10):5046-5052.[17] Armstrong H J, Hill S E, Schrooyen P, et al. A comparison of the viscoelastic properties of conventional and Maillard protein gels[J]. Journal of Texture Studies,1994, 25, 285–298.[18] CORZO-MARTíNEZ M, JAVIER MORENO F, VILLAMIEL M, et al. Characterization and improvement of rheological properties of sodium caseinate glycated with galactose, lactose and dextran[J]. Food Hydrocolloids, 2010, 24(1):88-97.[19] OLIVER C M, MELTON L D, STANLEY R A. Functional properties of caseinate glycoconjugates prepared by controlled heating in the ‘dry’ state[J]. Journal of the Science of Food and Agriculture, 2006, 86(5):732-740.[20] DIFTIS N G, BILIADERIS C G, KIOSSEOGLOU V D. Rheological properties and stability of model salad dressing emulsions prepared with a dry-heated soybean protein isolate–dextran mixture[J]. Food Hydrocolloids, 2005, 19(6):1025-1031.[21] JIMéNEZ-CASTA?O L, LóPEZ-FANDI?O R, OLANO A. Study on β-lactoglobulin glycosylation with dextran: Effect on solubility and heat stability[J]. Food Chemistry, 2005, 93(4):689-695.[22] FUJIWARA K, OOSAWA T, SAEKI H. Improved thermal stability and emulsifying properties of carp myofibrillar proteins by conjugation with dextran[J]. Journal of Agricultural and Food Chemistry, 1998, 46(4): 1257-1261.[23] NAKAMURA S, KATO A, KOBAYASHI K. Enhanced antioxidative effect of ovalbumin due to covalent binding of polysaccharides [J]. Journal of Agricultural and Food Chemistry, 1992, 40(11): 2033-2037[24] DONG S Y, WEI B B, CHEN B C. Chemical and antioxidant properties of casein peptide and its glucose Maillard reaction products in fish oil-in-water Emulsions[J]. Journal of Agricultural and Food Chemistry, 2011, 59(24): 13311-13317.[25] CHEVALIER F, CHOBERT J-M, GENOT C, et al. Scavenging of free radicals, antimicrobial, and cytotoxic activities of the Maillard reaction products of ?-lactoglobulin glycated with several sugars[J]. Journal of Agricultural and Food Chemistry, 2001, 49(10): 5031-5038.[26] MAKOTO H, KOICHI H, KOKI O, et al. Reduced immunogenicity of β-lactoglobulin by conjugation with carboxymethy dextran[J]. Bioconjugate Chemistry, 2000, 11(1): 84-93.[27] CHUNG S-Y, CHAMPAGNE E T. Allergenicity of Maillard reaction products from peanut proteins[J]. Journal of Agricultural and Food Chemistry, 1999, 47(12): 5227-5231.[28] ZHU D, DAMODARAN S, LUCEY J A. Physicochemical and emulsifying properties of whey protein isolate (WPI)–dextran conjugates produced in aqueous solution[J]. Journal of Agricultural and Food Chemistry, 2010, 58(5):2988-2994.[29] NIU L Y, JIANG S T, PAN L J, et al. Characteristics and functional properties of wheat germ protein glycated with saccharides through Maillard reaction[J]. International Journal of Food Science and Technology, 2011, 46(10): 2197-2203.[30] MU M F, PAN X Y, YAO P, et al. Acidic solution properties of β-casein-graft-dextran copolymer prepared through Maillard reaction [J]. Journal of Colloid and Interface Science, 2006, 301(1): 98-106.[31] ZHANG J B, WU N N, YANG X Q, et al. Improvement of emulsifying properties of Maillard reaction products from β-conglycinin and dextran using controlled enzymatic hydrolysis[J]. Food Hydrocolloids, 2012, 28(2):301-312.[32] OLIVER C M. Insight into the glycation of milk proteins, an ESI-and MALDI-MS perspective (review)[J]. Critical Reviews in Food Science and Nutrition, 2011, 51(5):410-431.[33] FENAILLE F, MORGAN F, PARISOD V, et al. Solid-state glycation of β-lactoglobulin by lactose and galactose: Localization of the modified amino acids using mass spectrometric techniques[J]. Journal of Mass Spectrometry, 2004, 39(1): 16-28.[34] SANZ M L, CORZO-MARTíNEZ M, RASTALL R A, et al. Characterization and in vitro digestibility of bovine β-lactoglobulin glycated with galactooligosaccharides[J]. Journal of Agricultural and Food Chemistry, 2007, 55(19): 7916-7925.[35] FRENCH S J, HARPER W J, KLEINHOLZ N M, et al. Maillard reaction induced lactose attachment to bovine β-lactoglobulin: Electrospray ionization and matrix-assisted laser desorption/ionization examination[J]. Journal of Agricultural and Food Chemistry, 2002, 50(4): 820-823.[36] GU F L, KIM J M, ABBAS S, et al. Structure and antioxidant activity of high molecular weight Maillard reaction products from casein-glucose [J]. Food Chemistry, 2010, 120(2):505-511.[37] DAREWICZ M, DZIUBA J. The effect of glycosylation on emulsifying and structural properties of bovine β-casein[J]. Nahrung/Food, 2001, 45(1): 15-20.[38] STANIC-VUCINIC D, PRODIC I, APOSTOLOVIC D, et al. Structure and antioxidant activity of β-lactoglobulin-glycoconjugates obtained by high-intensity-ultrasound-induced Maillard reaction in aqueous model systems under neutral conditions[J]. Food Chemistry, 2013, 138(1):590-599.[39] VAN TEEFFELEN A M M, BOERSEN K, DE JONGH H H J. Glucosylation of β-lactoglobulin lowers the heat capacity change of unfolding: A unique way to affect protein thermodynamics[J]. Protein Science, 2005, 14(8): 2187-2194.[40] SU J F, HUANG Z, YUAN X Y, et al. Structure and properties of carboxymethyl cellulose/soy protein isolate blend edible films crosslinked by Maillard reactions[J]. Carbohydrate Polymers, 2010, 79(1):145-153.[41] MARTINS S I F S, JONGEN W M F, VAN-BOEKEL M A J S. A review of Maillard reaction in food and implications to kinetic modeling[J]. Trends in Food Science and Technology, 2001, 11(9):364-373. [42] BRANDS C M J, ALINK G M, VAN-BOEKEL M A J S, et al. Mutagenicity of heated sugar-casein systems: effect of the Maillard reaction[J]. Journal of Agricultural and Food Chemistry, 2000, 48(6): 2271-2275.[43] GLATT H R, SOMMER Y. Health risks by 5-hydroxymethylfurfural( HMF) and related compounds[M]. In: Skog K, Alexander J, editors. Acrylamide and other health hazardous compounds in heat-treated foods. Cambridge: Woodhead Publishing; 2007: 328-357.[44] MRUTHINTI S, SOOD A, HUMPHREY C L, et al. The induction of surface beta-amyloid binding proteins and enhanced cytotoxicity in cultured PC- 12 and IMR- 32 cells by advanced glycation end products[J]. Neuro Science, 2006, 142(2): 463-473.[45] WEI Y, CHEN L, CHEN J. Rapid glycation with D-ribose induces globular amyloid-like aggregations of BSA with high cytotoxicity to SH-SY5Y cells[J]. BMC Cell Biology, 2009, 10(1): 10.[46] MUNCH G, APELT J, ROSEMARIE KIENTSCH E, et al. Advanced glycation endproducts and pro- inflammatory cytokines in transgenic Tg2576 mice with amyloid plaque pathology[J]. Neurochemistry, 2003, 86(2): 283-289.[47] BAYNES J W, MONNIER V M, AMES J M, et al.The Maillard reaction.Chemistry at the interface of nutrition, aging and disease[M]. Annals of the New York Academy of Sciences, 2005: 1043.[48] DE-JONG G A H, KOPPELMAN S J. Transglutaminase catalyzed reactions: impact on food applications[J]. Concise Reviews and Hypotheses in Food Science, 2002, 67(8): 2798-2806.[49] VILLALONGA R, FERNáNDEZ M, FRAGOSO A, et al. Thermal stabilization of trypsin by enzymatic modification with β-cyclodextrin derivatives[J]. Biotechnology and Applied Biochemistry, 2003, 38(1): 53-59. [50] YAN S C B, WOLD F. Neoglucoproteins: In vitro introduction of glycosyl units at glutamine in α-casein using transglutaminase[J]. Biochemistry, 1984, 23(16): 3759-3769.[51] COLAS B, CAER D, FOURNIER, E. Transglutaminase-catalyzed glycosylation of vegetable proteins. Effect on solubility of pea legumin and wheat gliadins[J], Journal of Agricultural and Food Chemistry, 1993, 41, 1811-1815.[52] 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[J]. European Food Research and Technology, 2010, 231(5): 679-689.[53] JIANG S J, & ZHAO X H. Transglutaminase-induced cross-linking and glucosamine conjugation of casein and some functional properties of the modified product[J]. International Dairy Journal, 2011, 21(4):198-205.[54] JIANG S J, & ZHAO X H. Cross-linking and glucosamine conjugation of casein by transglutaminase and the emulsifying property and digestibility in vitro of the modified product[J]. International Journal of Food Properties, 2012, 15(6): 1286-1299.[55] FLANAGAN J, SINGH H. Conjugation of sodium caseinate and gum arabic catalyzed by transglutaminase[J]. Journal of Agricultural and Food Chemistry, 2006, 54(19):7305-7310. |