Changes in Physical and Chemical Properties of Whey Protein Isolate during Maillard Reaction

Abstract

Abstract: In this study, Maillard reaction products (MRPs) were prepared by heating 1:1 (m/m) mixtures of whey protein isolates (WPI) with D-glucose or D-galactose at 95 ℃ for 6 h and sampling at different time points during the heating period for the determination of pH, absorbance at 294 nm and 420 nm (A294 nm and A420 nm), fluorescence intensity, free amino group content and protein polymerization. The pH and free amino group content of each reaction system significantly (P＜0.05) decreased and the yields of non-fluorescent intermediate products (A294 nm) and browning products (A420 nm) and fluorescence intensity significantly (P＜0.05) increased with increasing heating time. SDS-PAGE analysis demonstrated that both α-lactalbumin and β-lactoglobulin could be polymerized to different extents into larger molecules. More intermediate products and higher degree of browning were generated from WPI-D-glucose system compared with WPI-D-glucose system.

Key words: Maillard reaction, whey protein isolate, reducing sugar, reaction characteristics

CLC Number:

TS201.3

References

[1] YE A, SINGH H. Influence of calcium chloride addition on the properties of emulsions stabilized by whey protein concentrate[J]. Food Hydrocolloids, 2000, 14(4): 337-346.
[2] DALAFUENTE M A, SINGH H, HEMAR Y. Recent advances in the characterisation of heat-induced aggregates and intermediates of whey proteins[J]. Trends in Food Science and Technology, 2002, 13(8): 262-274.
[3] GUNASEKARAN S, KO S, XIAO L. Use of whey proteins for encapsulation and controlled delivery applications[J]. Journal of Food Engineering, 2007, 83(1): 31-40.
[4] ALTING A.C, HAMER R.J, DE KRUIF C.G, et al. Number of thiol groups rather than the size of the aggregates determines the hardness of cold set whey protein gels[J]. Food Hydrocolloids, 2003, 17(4): 469-479.
[5] MARINOVA K G, BASHEVA E S, NENOVA B, et al. Physico-chemical factors controlling the foamability and foam stability of milk proteins: Sodium caseinate and whey protein concentrates[J]. Food Hydrocolloids, 2009, 23(7): 1864-1876.
[6] SERPEN A, ATA? B, G?KMEN V. Adsorption of Maillard reaction products from aqueous solutions and sugar syrups using adsorbent resin[J]. Journal of Food Engineering, 2007, 82(3): 342-350.
[7] GIUSTI A M, BIGNETTI E, CANNELLA C. Exploring new frontiers in total food quality definition and assessment: From chemical to neurochemical properties[J]. Food and Bioprocess Technology, 2008, 1(2): 130-142.
[8] KAROUI R, NICOLA? B, DE BAERDEMAEKER J. Monitoring the egg freshness during storage under modified atmosphere by fluorescence spectroscopy[J]. Food and Bioprocess Technology, 2008, 1(4): 346-356.
[9] LERTITTIKUL W, BENJAKUL S, TANAKA M. Characteristics and antioxidative activity of Maillard reaction products from a porcine plasma protein–glucose model system as influenced by pH[J]. Food Chemistry, 2007, 100(2): 669-677.
[10] MORALES F J, JIMéNEZ-PéREZ S. Free radical scavenging capacity of Maillard reaction products as related to colour and fluorescence[J]. Food Chemistry, 2000, 72 (1): 119-125.
[11] JING H, KITTS D D. Chemical and biochemical properties of casein–sugar Maillard reaction products[J]. Food and Chemical Toxicology, 2002, 40(7): 1007-1015.
[12] FARAG K, MARRA F, LYNG J, et al. Temperature changes and power consumption during radio frequency tempering of beef lean/fat formulations[J]. Food and Bioprocess Technology, 2010, 3(5): 732-740.
[13] SUN Y, HAYAKAWA S, PUANGMANEE S, et al. Chemical properties and antioxidative activity of glycated α-lactalbumin with a rare sugar, d-allose, by Maillard reaction[J]. Food Chemistry, 2006, 95(3): 509-517.
[14] 赵艳娜, 辛岩, 姜瞻梅. 乳清蛋白糖基化反应特性及抗氧化性的研究[J]. 中国乳品工业, 2010, 38(8):
[15] 郑喆, 芦晶, 罗永康. 乳清蛋白-D-葡萄糖的制备及溶解性和热稳定性研究[J]. 乳业科学与技术, 2009, 32(2): 4.
[16] AKHTAR M, DICKINSON E. Emulsifying properties of whey protein–dextran conjugates at low pH and different salt concentrations[J]. Colloids and Surfaces B: Biointerfaces, 2003, 31(1-4): 125-132.
[17] 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.
[18] SISKOS I, ZOTOS A, MELIDOU S, et al. The effect of liquid smoking of fillets of trout (Salmo gairdnerii) on sensory, microbiological and chemical changes during chilled storage[J]. Food Chemistry, 2007, 101(2): 458-464.
[19] BAISIER W M, LABUZA T P. Maillard browning kinetics in a liquid model system[J]. Journal of Agricultural and Food Chemistry, 1992, 40(5): 707-713.
[20] ZWEIG M, CUMMINGS D J. Cleavage of head and tail proteins during bacteriophage T5 assembly: Selective host involvement in the cleavage of a tail protein[J]. Journal of Molecular Biology, 1973, 80(3): 505-518.
[21] BENJAKUL S, MORRISSEY M T. Protein hydrolysates from Pacific whiting solid wastes[J]. Journal of Agricultural and Food Chemistry, 1997, 45(9): 3423-3430.
[22] BENJAKUL S, LERTITTIKUL W, BAUER F. Antioxidant activity of Maillard reaction products from a porcine plasma protein–sugar model system[J]. Food Chemistry, 2005, 93(2): 189-196.
[23] LI Y, LU F, LUO C, et al. Functional properties of the Maillard reaction products of rice protein with sugar[J]. Food Chemistry, 2009, 117(1): 69-74.
[24] DAVIDEK T, BLANK I, CLETY N, et al. The fate of N-(1-deoxy-d-fructose-1-yl)glycine in aqueous model systems[J]. International Congress Series, 2002, 1245(11): 375-376.
[25] VAN BOEKEL M A J S, MARTINS S I F S. Fate of glycine in the glucose–glycine reaction: a kinetic analysis[J]. International Congress Series, 2002, 1245(5): 289-293.
[26] SéROT T, BARON R, KNOCKAERT C, et al. Effect of smoking processes on the contents of 10 major phenolic compounds in smoked fillets of herring (Cuplea harengus)[J]. Food Chemistry, 2004, 85(1): 111-120.
[27] AJANDOUZ E H, TCHIAKPE L S, ORE F D, et al. Effects of pH on caramelization and Maillard reaction kinetics in fructose-lysine model systems[J]. Journal of Food Science, 2001, 66(7): 926-931.
[28] MORENO F J, MOLINA E, OLANO A, et al. High-pressure effects on Maillard reaction between glucose and lysine[J]. Journal of Agricultural and Food Chemistry, 2002, 51(2): 394-400.
[29] CHAWLA S P, CHANDER R, SHARMA A. Antioxidant formation by γ-irradiation of glucose–amino acid model systems[J]. Food Chemistry, 2007, 103(4): 1297-1304.
[30] OH S H, LEE Y S, LEE J W, et al. The effect of γ-irradiation on the non-enzymatic browning reaction in the aqueous model solutions[J]. Food Chemistry, 2005, 92(2): 357-363.
[31] JING H, KITTS D D. Comparison of the antioxidative and cytotoxic properties of glucose-lysine and fructose-lysine Maillard reaction products[J]. Food Research International, 2000, 33(6): 509-516.
[32] SUN Y, HAYAKAWA S, IZUMORI K. Modification of ovalbumin with a rare ketohexose through the Maillard reaction:?Effect on protein structure and gel properties[J]. Journal of Agricultural and Food Chemistry, 2004, 52(5): 1293-1299.
[33] OLIVER C M, MELTON L D, STANLEY R A. Creating proteins with novel functionality via the Maillard reaction: A review[J]. Critical Reviews in Food Science and Nutrition, 2006, 46(4): 337-350.
[34] MIRALLES B, MARTíNEZ-RODRíGUEZ A, SANTIAGO A, et al. The occurrence of a Maillard-type PROTEIN-polysaccharide reaction between β-lactoglobulin and chitosan[J]. Food Chemistry, 2007, 100(3): 1071-1075.