Effect of Glycosylation Treatment Coupled with Dynamic High Pressure Microfluidization on Emulsifying Properties and Structure of β-Lactoglobulin

doi:10.7506/spkx1002-6630-201401002

Abstract

Abstract:

The effect of glycosylation treatment coupled with dynamic high-pressure microfluidization (DHPM) on
emulsifying properties and structure change of β-lactoglobulin (β-Lg) was investigated. The results showed that glycosylation
treatment coupled with DHPM obviously improved the emulsifying capacity and emulsion stability of β-Lg. The emulsifying
activity index (EAI) of β-Lg subjected to glycosylation treatment in the presence of high pressure at 0, 40 and 120 MPa were
136.3, 168.1 m2/g and 177.9 m2/g, respectively. The emulsifying stability index (ESI) of β-Lg subjected to glycosylation
treatment was 52.3 min. With increasing the pressure up to 40 MPa and 120 MPa, the ESI of β-Lg treated by glycosylation
were increased to 56.4 min and 59.0 min, respectively, indicating the structural change of β-Lg due to the combinatorial
treatment of DHPM and glycosylation. This structural change was characterized as increased molecular weight, sulphydryl
(—SH) content, reduced surface hydrophobicity (Ho), changed secondary structure, and unmasked amino acids in the tertiary
structure after the combinatorial treatment of DHPM and glycosylation. These results revealed that the conjugation with
galacto-oligosaccharides (GOS) changed the structure of β-Lg, which contributed to the increase of surface hydrophilic
groups of β-Lg and resulted in the improvement of emulsifying properties.

Key words: β-lactoglobulin, dynamic high pressure microfluidization, glycosylation, emulsifying properties, structure

CLC Number:

TS252

ZHONG Jun-zhen, TU Yue, LIU Wei, LIU Cheng-mei*. Effect of Glycosylation Treatment Coupled with Dynamic High Pressure Microfluidization on Emulsifying Properties and Structure of β-Lactoglobulin[J]. FOOD SCIENCE, 2014, 35(1): 7-11.

References

[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.