[1]. MORO A, BAEZ G D, BUSTI P A, et al. Effects of heat-treated beta-lactoglobulin and its aggregates on foaming properties[J]. Food Hydrocolloids, 2011, 25(5): 1009-1015.[2]. LI C P, ENOMOTO H, OHKI S, et al. Improvement of functional properties of whey protein isolate through glycation and phosphorylation by dry heating[J]. Journal of Dairy Science, 2005, 88(12): 4137-4145.[3]. KUMAR V, SHARMA V K, KALONIA D S. Effect of polyols on polyethylene glycol (PEG)-induced precipitation of proteins: Impact on solubility, stability and conformation[J]. International Journal of Pharmaceutics, 2009, 366(1-2): 38-43.[4]. CORZO-MARTINEZ M C, CARRERA SANCHEZ F, JAVIER MORENO J M, et al. Interfacial and foaming properties of bovine beta-lactoglobulin: Galactose Maillard conjugates[J]. Food Hydrocolloid, 2012, 27(2): 438-447.[5]. LIU Chengmei, ZHONG Junzhen, LIU Wei, et al. The relationship between functional properties and aggregation changes of whey protein induced by high pressure microfluidization[J]. Journal of Food Science, 2011, 76 (4): E341-E347.[6]. 涂越,刘伟,钟俊桢等,低聚木糖修饰对牛乳β-乳球蛋白功能性质的影响[J]. 中国乳品工业,2012,40(12):12-15.[7]. JIANG Z M, BRODKORB A. Structure and antioxidant activity of Maillard reaction products from alpha-lactalbumin and beta-lactoglobulin with ribose in an aqueous model system[J]. Food Chemistry, 2012, 133 (3): 960-968.[8]. ZHONG Junzhen, XU Yujia, LIU Wei, et al. Antigenicity and functional properties of β-lactoglobulin conjugated with fructo-oligosaccharides in relation with conformational Changes[J]. Journal of Dairy Science, 2013, DOI: 10.3168/jds.2012-6259.[9]. HATTORI M, MIYAKAWA S, OHAMA Y, et al. Reduced immunogenicity of beta-lactoglobulin by conjugation with acidic oligosaccharides[J]. Journal of Agricultural and Food Chemistry, 2004, 52(14): 4546-4553.[10]. LI Zheng, LUO Yongkang., FENG Ligeng. Effects of Maillard reaction conditions on the antigenicity of alpha-lactalbumin and beta-lactoglobulin in whey protein conjugated with maltose[J]. European Food Research Technology, 2011, 233(3): 387-394.[11]. PEARCE K N, KINSELLA J E. Emulsifying properties of proteins evaluation of a turbidimetric technique[J]. Journal of Agricultural and Food Chemistry, 1978, 26(3): 716-723.[12]. WANG Xiansheng, TANG Chuanhe, LI Biansheng, et al. Effects of high-pressure treatment on some physicochemical and functional properties of soy protein isolates[J]. Food Hydrocolloids, 2008, 22(4): 560-567.[13]. ELLMAN G L. Tissue sulfhydryl groups[J]. Archives of Biochemistry and Biophysics 1959, 82(1): 70-77.[14]. SAVA N, VAN DER PLANCKEN I, CLAEYS W, et al. The kinetics of heat-induced structural changes of beta-lactoglobulin[J]. Journal of Dairy Science, 2005, 88(5): 1646-1653.[15]. HASKARD C A, LI-CHAN E C Y. Hydophobicity of bovine serum albumin and ovalbumin determined using uncharged (PRODAN) and anionic (ANS-) fluorescent probes[J]. Journal of Agricultural and Food Chemistry, 1998, 46(7): 2671-2677.[16]. CHEN W L, HWANG M T, LIAU C. Y, et al. Beta-Lactoglobulin is a thermal marker in processed milk as studied by electrophoresis and circular dichroic spectra[J]. Journal of Dairy Science 2005, 88(5): 1618-1630.[17]. DE LA HOZ L, NETTO F M. Structural modifications of beta-lactoglobulin subjected to gamma radiation[J]. International Dairy Journal, 2008, 18(12): 1126-1132.[18]. FACHIN L, VIOTTO W H. Effect of pH and heat treatment of cheese whey on solubility and emulsifying properties of whey protein concentrate produced by ultrafiltration[J]. International Dairy Journal, 2005, 15(4): 325-332.[19]. ZHONG Junzhen, LIU Wei, LIU Chengmei, et al. Aggregation and conformational changes of bovine β-lactoglobulin subjected to dynamic high pressure microfluidization in relation with antigenicity[J]. Journal of Dairy Science, 2012, 95(8): 4237-4245.[20]. MONAHAN F J, GERMAN J B, KINSELLA J E. Effect of pH and temperature on protein unfolding and thiol-disulfide interchange reactions during heat-induced gelation of whey proteins[J]. Journal of Agricultural and Food Chemistry, 1995, 43(1): 46-52.[21]. KEHOE J J, REMONDETTO G E, SUBIRADE M, et al. Tryptophan-mediated denaturation of beta-lactoglobulin A by UV irradiation[J]. Journal of Agricultural and Food Chemistry, 2008, 56(12): 4720-4725.[22]. MATSUMOTO T. Mitigation of the allergenic activity of beta-lactoglobulin by electrolysis[J]. Pediatric Allergy and Immunology 2011, 22(2): 235-242.[23]. GULZAR M, CROGUENNEC T, JARDIN J, et al. Copper modulates the heat-induced sulfhydryl/disulfide interchange reactions of beta-Lactoglobulin[J]. Food Chemistry, 2009, 116(4): 884-891.[24]. CHAPLEAU N, DE LAMBALLERIE-ANTON M. Improvement of emulsifying properties of lupin proteins by high pressure induced aggregation[J]. Food Hydrocolloid, 2003, 17(3): 273–280.[25]. HILLER B, LORENZEN P C. Functional properties of milk proteins as affected by Maillard reaction induced oligomerisation[J]. Food Research International, 2010, 43(4): 1155-1166.[26]. SHIBAYAMA N. Circular dichroism study on the early folding events of beta-lactoglobulin entrapped in wet silica gels[J]. FEBS Letters, 2008, 582(17): 2668-2672. |