992
Views
9
CrossRef citations to date
0
Altmetric
Articles

In vitro immuno-modulatory ability of tryptic caseinate hydrolysate affected by prior caseinate glycation using the Maillard reaction or transglutaminase

& ORCID Icon
Pages 1029-1045 | Received 24 Mar 2017, Accepted 27 Apr 2017, Published online: 11 May 2017

References

  • Ahmad, W., Jantan, I., Kumolosasi, E., & Bukhari, S. N. A. (2015). Immunostimulatory effects of the standardized extract of Tinospora crispa on innate immune responses in Wistar Kyoto rats. Drug Design Development and Therapy, 9, 2961–2973.
  • Ajandouz, E. H., Desseaux, V., Tazi, S., & Puigserver, A. (2008). Effects of temperature and pH on the kinetics of caramelisation, protein cross-linking and Maillard reactions in aqueous model systems. Food Chemistry, 107, 1244–1252. doi: 10.1016/j.foodchem.2007.09.062
  • Anumula, K. R. (1994). Quantitative determination of monosaccharides in glycoproteins by high-performance liquid chromatography with highly sensitive fluorescence detection. Analytical Biochemistry, 220, 275–283. doi: 10.1006/abio.1994.1338
  • AOAC. (2005). Official methods of analysis (6th ed.). Washington, DC: Author.
  • Arena, S., Salzano, A. M., Renzone, G., D’Ambrosio, C., & Scaloni, A. (2014). Non-enzymatic glycation and glycoxidation protein products in foods and diseases: An interconnected, complex scenario fully open to innovative proteomic studies. Mass Spectrometry Reviews, 33, 49–77. doi: 10.1002/mas.21378
  • Balkwill, F. R. (1992). Tumour necrosis factor and cancer. Progress in Growth Factor Research, 4, 121–137. doi: 10.1016/0955-2235(92)90027-F
  • Brands, C. M., Alink, G. M., van Boekel, M. A., & Jongen, W. M. (2000). Mutagenicity of heated sugar-casein systems: Effect of the Maillard reaction. Journal of Agricultural and Food Chemistry, 48, 2271–2275. doi: 10.1021/jf9907586
  • Cabodevila, O., Hill, S. E., Armstrong, H. J., De Sousa, I., & Mitchell, J. R. (1994). Gelation enhancement of soy protein isolate using the Maillard reaction and high temperatures. Journal of Food Science, 59, 872–875. doi: 10.1111/j.1365-2621.1994.tb08147.x
  • Calder, P. C., Krauss-Etschmann, S., de Jong, E. C., Dupont, C., Frick, J. S., Frokiaer, H., … Lacker, G. (2006). Early nutrition and immunity – progress and perspectives. British Journal of Nutrition, 96, 774–790. doi: 10.1079/BJN20061881
  • Carini, M., Aldini, G., Orioli, G., Piccoli, A., Rossoni, G., & Facino, R. M. (2004). Nitric oxide release and distribution following oral and intraperitoneal administration of nitroaspirin (NCX 4016) in the rat. Life Sciences, 74, 3291–3305. doi: 10.1016/j.lfs.2003.11.018
  • Chun, S. H., Lee, H. A., Lee, K. B., Kim, S. H., Park, K. Y., & Lee, K. W. (2016). Effects of glycated whey protein concentrate on pro-inflammatory cytokine expression and phagocytic activity in RAW 264.7 macrophages. Biological & Pharmaceutical Bulletin, 39, 199–206. doi: 10.1248/bpb.b15-00596
  • Dell, A., Haslam, S. M., Morris, H. R., & Khoo, K. H. (1999). Immunogenic glycoconjugates implicated in parasitic nematode diseases. Biochimica et Biophysica Acta-Molecular Basis of Disease, 1455, 353–362. doi: 10.1016/S0925-4439(99)00064-2
  • Die, I. V., & Cummings, R. D. (2010). Glycomics in unraveling glycan-driven immune responses by parasitic helminthes. In R. D. Cummings, & J. M. Pierce (Eds.), Handbook of Glycomics (pp. 367–397). Burlington: Academic Press.
  • Diftis, N., & Kiosseoglou, V. (2006). Physicochemical properties of dry-heated soy protein isolate-dextran mixtures. Food Chemistry, 96, 228–233. doi: 10.1016/j.foodchem.2005.02.036
  • FitzGerald, R. J., & Murray, B. A. (2006). Bioactive peptides and lactic fermentations. International Journal of Dairy Technology, 59, 118–125. doi: 10.1111/j.1471-0307.2006.00250.x
  • Fu, Y., Young, J. F., Rasmussen, M. K., Dalsgaard, T. K., Lametsch, R., Aluko, R. E., & Therkildsen, M. (2016). Angiotensin I-converting enzyme-inhibitory peptides from bovine collagen: Insights into inhibitory mechanism and transepithelial transport. Food Research International, 89, 373–381. doi: 10.1016/j.foodres.2016.08.037
  • Fu, M., & Zhao, X. H. (2016). Structure and property changes of transglutaminase-induced modification of sodium caseinate in the presence of oligochitosan of 5 kDa. International Journal of Food Properties, 19, 2596–2607. doi: 10.1080/10942912.2015.1137937
  • Fu, M., & Zhao, X. H. (2017). Modified properties of a glycated and cross-linked soy protein isolate by transglutaminase and an oligochitosan of 5 kDa. Journal of the Science of Food and Agriculture, 97, 58–64. doi: 10.1002/jsfa.7682
  • Gauthier, S. F., Pouliot, Y., & Saint-Sauveur, D. (2006). Immunomodulatory peptides obtained by the enzymatic hydrolysis of whey proteins. International Dairy Journal, 16, 1315–1323. doi: 10.1016/j.idairyj.2006.06.014
  • Gill, H. S., Doull, F., Rutherfurd, K. J., & Cross, M. L. (2000). Immunoregulatory peptides in bovine milk. British Journal of Nutrition, 84, S111–S117.
  • Goossens, V., Grooten, J., De Vos, K., & Fiers, W. (1995). Direct evidence for tumor necrosis factor-induced mitochondrial reactive oxygen intermediates and their involvement in cytotoxicity. Proceedings of the National Academy of Sciences of the United States America, 92, 8115–8119. doi: 10.1073/pnas.92.18.8115
  • Ha, Y. M., Chun, S. H., Hong, S. T., Koo, Y. C., Choi, H. D., & Lee, K. W. (2013). Immune enhancing effect of a Maillard-type lysozyme-galactomannan conjugate via signaling pathways. International Journal of Biological Macromolecules, 60, 399–404. doi: 10.1016/j.ijbiomac.2013.06.007
  • Hao, L. X., & Zhao, X. H. (2016). Immunomodulatory potentials of the water-soluble yam (Dioscorea opposita Thunb) polysaccharides for the normal and cyclophosphamide-suppressed mice. Food and Agricultural Immunology, 27, 667–677. doi: 10.1080/09540105.2016.1148666
  • Hartmann, R., & Meisel, H. (2007). Food-derived peptides with biological activity: From research to food applications. Current Opinion in Biotechnology, 18, 163–169. doi: 10.1016/j.copbio.2007.01.013
  • Hong, P. K., Gottardi, D., Ndagijimana, M., & Betti, M. (2014). Glycation and transglutaminase mediated glycosylation of fish gelatin peptides with glucosamine enhance bioactivity. Food Chemistry, 142, 285–293. doi: 10.1016/j.foodchem.2013.07.045
  • Hong, P. K., Ndagijimana, M., & Betti, M. (2016). Glucosamine-induced glycation of hydrolysed meat proteins in the presence or absence of transglutaminase: Chemical modifications and taste-enhancing activity. Food Chemistry, 197, 1143–1152. doi: 10.1016/j.foodchem.2015.11.096
  • Hou, H., Fan, Y., Li, B. F., Xue, C. H., & Yu, G. L. (2012). Preparation of immunomodulatory hydrolysates from Alaska pollock frame. Journal of the Science of Food and Agriculture, 92, 3029–3038. doi: 10.1002/jsfa.5719
  • Jiang, S. J., & Zhao, X. H. (2010). 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, 231, 679–689. doi: 10.1007/s00217-010-1319-2
  • Jiang, S. J., & Zhao, X. H. (2011). Transglutaminase-induced cross-linking and glucosamine conjugation of casein and some functional properties of the modified product. International Dairy Journal, 21, 198–205. doi: 10.1016/j.idairyj.2010.12.004
  • Jollès, P., Fiat, A., Migliore-Samour, D., Drouet, L., & Caen, J. (1992). Peptides from milk proteins implicated in antithrombosis and immunomodulation. In B. Renner & G. Sawatzki (Eds.), New perspectives in infant nutrition (pp. 160–172). New York, NY: Thieme Medical Press.
  • Kim, S. Y., Je, J. Y., & Kim, S. K. (2007). Purification and characterization of antioxidant peptide from hoki (Johnius belengerii) frame protein by gastrointestinal digestion. Journal of Nutritional Biochemistry, 18, 31–38. doi: 10.1016/j.jnutbio.2006.02.006
  • Kim, T. H., Lee, S. J., Rim, H. K., Shin, J. S., Jung, J. Y., Heo, J. S., … Lee, K. T. (2013). In vitro and in vivo immunostimulatory effects of hot water extracts from the leaves of Artemisia princeps Pampanini cv. Sajabal. Journal of Ethnopharmacology, 149, 254–262. doi: 10.1016/j.jep.2013.06.030
  • Kleekayai, T., Harnedy, P. A., O’Keeffe, M. B., Poyarkov, A. A., CunhaNeves, A., Suntornsuk, W., & FitzGerald, R. J. (2015). Extraction of antioxidant and ACE inhibitory peptides from Thai traditional fermented shrimp pastes. Food Chemistry, 176, 441–447. doi: 10.1016/j.foodchem.2014.12.026
  • Lee, J., Lee, S. J., & Lim, K. T. (2014). ZPDC glycoprotein (24 kDa) induces apoptosis and enhances activity of NK cells in N-nitrosodiethylamine-injected BALB/c. Cellular Immunology, 289, 1–6. doi: 10.1016/j.cellimm.2014.03.002
  • Lin, S. Y., Liu, X. T., Liu, B. L., & Yu, Y. L. (2017). Optimization of pine nut (Pinus koraiensis) meal protein peptides on immunocompetence in innate and adaptive immunity response aspects. Food and Agricultural Immunology, 28, 109–120. doi: 10.1080/09540105.2016.1228835
  • Liu, X. D., Zhou, B., Cao, R. B., Feng, X. L., Li, X. F., & Chen, P. Y. (2013). Comparison of immunomodulatory functions of three peptides from the chicken bursa of Fabricius. Regulatory Peptides, 186, 57–61. doi: 10.1016/j.regpep.2013.07.007
  • Luft, F. C. (2008). Curbing the appetites of the big eaters. Journal of Molecular Medicine, 86, 351–352. doi: 10.1007/s00109-008-0321-7
  • Mallet, J. F., Duarte, J., Vinderola, G., Anguenot, R., Beaulieu, M., & Matar, C. (2014). The immunopotentiating effects of shark-derived protein hydrolysate. Nutrition, 30, 706–712. doi: 10.1016/j.nut.2013.10.025
  • Martins, S. I., Jongen, W. M., & van Boekel, M. A. (2000). A review of Maillard reaction in food and implications to kinetic modelling. Trends in Food Science and Technology, 11, 364–373. doi: 10.1016/S0924-2244(01)00022-X
  • Martins, S. I., & van Boekel, M. A. (2005). A kinetic model for the glucose/glycine Maillard reaction pathways. Food Chemistry, 90, 257–269. doi: 10.1016/j.foodchem.2004.04.006
  • Matsuda, T., Gu, J. X., Tsuruta, K., & Nakamura, R. (1985). Immunoreactive glycopeptides separated from peptic hydrolysate of chicken egg white ovomucoid. Journal of Food Science, 50, 592–594. doi: 10.1111/j.1365-2621.1985.tb13751.x
  • Mercier, A., Gauthier, S. F., & Fliss, I. (2004). Immunomodulating effects of whey proteins and their enzymatic digests. International Dairy Journal, 14, 175–183. doi: 10.1016/j.idairyj.2003.08.003
  • Mu, L. X., Zhao, H. F., Zhao, M. M., Cui, C., & Liu, L. Y. (2011). Physicochemical properties of soy protein isolates-acacia gum conjugates. Czech Journal of Food Science, 29, 129–136.
  • Oliver, C. M., Melton, L. D., & Stanley, R. A. (2006). Creating protein with novel functionality via the Maillard reaction: A review. Critical Reviews in Food Science and Nutrition, 46, 337–350. doi: 10.1080/10408690590957250
  • Parkin, J., & Cohen, B. (2001). An overview of the immune system. The Lancet, 357, 1777–1789. doi: 10.1016/S0140-6736(00)04904-7
  • Park, H. Y., Yu, A. R., Choi, I. W., Hong, H. D., Lee, K. W., & Choi, H. D. (2013). Immunostimulatory effects and characterization of a glycoprotein fraction from rice bran. International Immunopharmacology, 17, 191–197. doi: 10.1016/j.intimp.2013.06.013
  • Račaitytė, K., Kiessig, S., & Kálmán, F. (2005). Application of capillary zone electrophoresis and reversed-phase high-performance liquid chromatography in the biopharmaceutical industry for the quantitative analysis of the monosaccharides released from a highly glycosylated therapeutic protein. Journal of Chromatography A, 1079, 354–365. doi: 10.1016/j.chroma.2005.03.080
  • Ramezani, R., Esmailpour, M., & Aminlari, M. (2008). Effect of conjugation with glucosamine on the functional properties of lysozyme and casein. Journal of the Science of Food and Agriculture, 88, 2730–2737. doi: 10.1002/jsfa.3400
  • Renn, P. T., & Sathe, S. K. (1997). Effect of pH, temperature, and reactant molar ratio on L-leucine and D-glucose Maillard browning reaction in an aqueous system. Journal of Agricultural and Food Chemistry, 45, 3782–3787. doi: 10.1021/jf9608231
  • Santiago-López, L., Hernández-Mendoza, A., Vallejo-Cordoba, B., Mata-Haro, V., & González-Córdova, A. (2016). Food-derived immunomodulatory peptides. Journal of the Science of Food and Agriculture, 96, 3631–3641. doi: 10.1002/jsfa.7697
  • Schlimme, E., & Meisel, H. (1995). Bioactive peptides derived from milk proteins. Structural, physiological and analytical aspects. Molecular Nutrition and Food Research, 39, 1–20.
  • Shu, M., Shen, W., Wang, X. J., Wang, F., Ma, L. X., & Zhai, C. (2015). Expression, activation and characterization of porcine trypsin in Pichia pastoris GS115. Protein Expression and Purification, 114, 149–155. doi: 10.1016/j.pep.2015.06.014
  • Song, C. L., & Zhao, X. H. (2013). Rheological, gelling, and emulsifying properties of a glycosylated and cross-linked caseinate generated by transglutaminase. International Journal of Food Science and Technology, 48, 2595–2602. doi: 10.1111/ijfs.12255
  • Song, C. L., & Zhao, X. H. (2014). Structure and property modification of oligochitosan- glycosylated and crosslinked soybean protein generated by microbial transglutaminase. Food Chemistry, 163, 114–119. doi: 10.1016/j.foodchem.2014.04.089
  • Varela, B. Y. P., Arce, M. D. M., Marcos, A., & Castrillón, A. M. (1997). Immunocompetence in relation to a heat-processed diet (Maillard reaction) in weanling rats. British Journal of Nutrition, 77, 947–956. doi: 10.1079/BJN19970092
  • Vivier, E., Tomasello, E., Baratin, M., Walzer, T., & Ugolini, S. (2008). Functions of natural killer cells. Nature Immunology, 9, 503–510. doi: 10.1038/ni1582
  • Wang, M. C., Jiang, C. X., Ma, L. P., Zhang, Z. J., Cao, L., Liu, J., & Zeng, X. X. (2013). Preparation, preliminary characterization and immunostimulatory activity of polysaccharide fractions from the peduncles of Hovenia dulcis. Food Chemistry, 138, 41–47. doi: 10.1016/j.foodchem.2012.09.098
  • Wang, X. P., & Zhao, X. H. (2017). Using an enzymatic galactose assay to detect lactose glycation extents of caseinate and soybean protein isolate via the Maillard reaction. Journal of the Science of Food and Agriculture. doi: 10.1002/jsfa.8084
  • Yuan, C. F., Wang, C. D., Bu, Y. Q., Xiang, T. X., Huang, X. N., Wang, Z. W., … Song, F. Z. (2010). Antioxidative and immunoprotective effects of Pyracantha fortuneana (Maxim.) Li polysaccharides in mice. Immunology Letters, 133, 14–18. doi: 10.1016/j.imlet.2010.04.004
  • Zhou, J. H., Ma, L. L., Xu, H. H., Gao, Y., Jin, Y. K., Zhao, L., … Zhang, S. H. (2014). Immunomodulating effects of casein-derived peptides QEPVL and QEPV on lymphocytes in vitro and in vivo. Food and Function, 5, 2061–2069. doi: 10.1039/C4FO00384E

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.