Kinetics of wheat gluten polymerization at extrusion-like conditions relevant for the production of meat analog products

Food Hydrocolloids

Volumn 85, Issue , 2018, Pages 102-109

  Pietsch, Valerie L ^a   Karbstein, Heike P ^a   Emin, M Azad ^a  

^a KARLSRUHE INSTITUTE OF TECHNOLOGY   (Germany)

Author keywords

Concentrated proteins; Extrusion; Meat analogs; Reaction behavior; Thermomechanical treatment; Wheat gluten

Indexed keywords

COVALENT BONDS; EXTRUSION; MEATS; POLYMERIZATION; REACTION KINETICS; SULFUR COMPOUNDS; THERMAL PROCESSING (FOODS); VISCOSITY;

COMPLEX VISCOSITY; CONCENTRATED PROTEIN; CONDITION; GLUTEN POLYMERIZATIONS; MEAT ANALOG; MECHANICAL STRESS; REACTION BEHAVIOR; SHEAR-RATE; THERMAL; WHEAT GLUTEN;

PROTEINS;

EID: 85053059070     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2018.07.008     Document Type: Article

References (48)

1. Attenburrow, G., Barnes, D.J., Davies, A.P., Ingman, S.J., Rheological properties of wheat gluten. Journal of Cereal Science 12:1 (1990), 1–14 https://doi.org/10.1016/S0733-5210(09)80152-5.
2. Corradini, M.G., Peleg, M., Prediction of vitamins loss during non-isothermal heat processes and storage with non-linear kinetic models. Trends in Food Science & Technology 17:1 (2006), 24–34 https://doi.org/10.1016/j.tifs.2005.09.004.
3. Cuq, B., Boutrot, F., Redl, A., Lullien-Pellerin, V., Study of the temperature effect on the formation of wheat gluten Network: influence on mechanical properties and protein solubility. Journal of Agricultural and Food Chemistry 48:7 (2000), 2954–2959 https://doi.org/10.1021/jf991339b.
4. Day, L., Wheat gluten: Production, properties and application. Phillips, G.O., Williams, P.A., (eds.) Woodhead publishing series in food science, technology and nutrition. Handbook of food proteins, 2011, Woodhead Publishing, 267–288 https://doi.org/10.1533/9780857093639.267.
5. Delcour, J.A., Joye, I.J., Pareyt, B., Wilderjans, E., Brijs, K., Lagrain, B., Wheat gluten functionality as a quality determinant in cereal-based food products. Annual Review of Food Science and Technology 3:1 (2012), 469–492 https://doi.org/10.1146/annurev-food-022811-101303.
6. Domenek, S., Morel, M.-H., Redl, A., Guilbert, S., Rheological investigation of swollen gluten polymer networks: Effects of process parameters on cross-link density. Macromolecular Symposia 200:1 (2003), 137–146 https://doi.org/10.1002/masy.200351014.
7. Emin, M.A., Quevedo, M., Wilhelm, M., Karbstein, H.P., Analysis of the reaction behavior of highly concentrated plant proteins in extrusion-like conditions. Innovative Food Science & Emerging Technologies 44 (2017), 15–20 https://doi.org/10.1016/j.ifset.2017.09.013.
8. Emin, M.A., Schuchmann, H.P., Analysis of the dispersive mixing efficiency in a twin-screw extrusion processing of starch based matrix. Journal of Food Engineering 115:1 (2013), 132–143 https://doi.org/10.1016/j.jfoodeng.2012.10.008.
9. Emin, M.A., Schuchmann, H.P., A mechanistic approach to analyze extrusion processing of biopolymers by numerical, rheological, and optical methods. Trends in Food Science & Technology, 2016, 1–8 https://doi.org/10.1016/j.tifs.2016.10.003.
10. Emin, M.A., Teumer, T., Schmitt, W., Rädle, M., Schuchmann, H.P., Measurement of the true melt temperature in a twin-screw extrusion processing of starch based matrices via infrared sensor. Journal of Food Engineering 170:Supplement C (2016), 119–124 https://doi.org/10.1016/j.jfoodeng.2015.09.018.
11. Faubion, J.M., Hoseney, R.C., High-temperature short-time extrusion cooking of wheat starch and flour. I. Effect of moisture content and flour type on extrudate properties. Cereal Chemistry 59:6 (1982), 529–533.
12. Fischer, T., Effect of extrusion cooking on protein modification in wheat flour. European Food Research and Technology 218:2 (2004), 128–132 https://doi.org/10.1007/s00217-003-0810-4.
13. Guerrieri, N., Alberti, E., Lavelli, V., Cerletti, P., Use of spectroscopic and flueorescence techniques to assess heat-induced molecular modifications of gluten. Cereal Chemistry 73:3 (1996), 368–374.
14. Habeych, E., Dekkers, B., van der Goot, A.J., Boom, R., Starch–zein blends formed by shear flow. Chemical Engineering Science 63:21 (2008), 5229–5238 https://doi.org/10.1016/j.ces.2008.07.008.
15. Haraguchi, T., Abe, K., Arai, S., Homma, S., Fujimaki, M., Lysinoalanine formation in gluten: A conformational effect. Agricultural & Biological Chemistry 44:8 (1980), 1951–1952 https://doi.org/10.1271/bbb1961.44.1951.
16. Jansens, K.J.A., Lagrain, B., Rombouts, I., Brijs, K., Smet, M., Delcour, J.A., Effect of temperature, time and wheat gluten moisture content on wheat gluten network formation during thermomolding. Journal of Cereal Science 54:3 (2011), 434–441 https://doi.org/10.1016/j.jcs.2011.08.008.
17. Koch, L., Emin, M.A., Schuchmann, H.P., Reaction behaviour of highly concentrated whey protein isolate under defined heat treatments. International Dairy Journal 71:Supplement C (2017), 114–121 https://doi.org/10.1016/j.idairyj.2017.03.013.
18. Koch, L., Emin, M.A., Schuchmann, H.P., Influence of processing conditions on the formation of whey protein-citrus pectin conjugates in extrusion. Journal of Food Engineering 193:Supplement C (2017), 1–9 https://doi.org/10.1016/j.jfoodeng.2016.08.012.
19. Koch, L., Hummel, L., Schuchmann, H.P., Emin, M.A., Influence of defined shear rates on structural changes and functional properties of highly concentrated whey protein isolate-citrus pectin blends at elevated temperatures. Food Biophysics 12:3 (2017), 309–322 https://doi.org/10.1007/s11483-017-9487-2.
20. Koch, L., Hummel, L., Schuchmann, H.P., Emin, M.A., Improving the emulsifying properties of whey protein isolate-citrus pectin blends by a novel reactive extrusion approach. Journal of Food Engineering 223 (2018), 175–188 https://doi.org/10.1016/j.jfoodeng.2017.10.027.
21. Kokini, J.L., Cocero, A.M., Madeka, H., de Graaf, E., The development of state diagrams for cereal proteins. Trends in Food Science & Technology 5:9 (1994), 281–288 https://doi.org/10.1016/0924-2244(94)90136-8.
22. Lagrain, B., Brijs, K., Delcour, J.A., Reaction kinetics of Gliadin−Glutenin cross-linking in model systems and in bread making. Journal of Agricultural and Food Chemistry 56:22 (2008), 10660–10666 https://doi.org/10.1021/jf801894r.
23. Lagrain, B., de Vleechouwer, K., Rombouts, I., Brijs, K., Hendrickx, M.E., Delcour, J.A., The kinetics of β-elimination of cystine and the formation of lanthionine in gliadin. Journal of Agricultural and Food Chemistry 58:19 (2010), 10761–10767 https://doi.org/10.1021/jf102575r.
24. Lagrain, B., Rombouts, I., Brijs, K., Delcour, J.A., Kinetics of heat-induced polymerization of gliadin. Journal of Agricultural and Food Chemistry 59:5 (2011), 2034–2039 https://doi.org/10.1021/jf104201u.
25. Lagrain, B., Thewissen, B.G., Brijs, K., Delcour, J.A., Mechanism of gliadin–glutenin cross-linking during hydrothermal treatment. Food Chemistry 107:2 (2008), 753–760 https://doi.org/10.1016/j.foodchem.2007.08.082.
26. Langstraat, T.D., Jansens, K.J.A., Delcour, J.A., van Puyvelde, P., Goderis, B., Controlling wheat gluten cross-linking for high temperature processing. Industrial Crops and Products 72 (2015), 119–124 https://doi.org/10.1016/j.indcrop.2014.11.058.
27. Leeb, C.V., Maiser, B., Schuchmann, H.P., Identification of allocation of retention time in the cooking extrusion of samp in the high-speed extruder. Chemie Ingenieur Technik 80:8 (2008), 1175–1179 https://doi.org/10.1002/cite.200800072.
28. Lefebvre, J., An outline of the non-linear viscoelastic behaviour of wheat flour dough in shear. Rheologica Acta 45:4 (2006), 525–538 https://doi.org/10.1007/s00397-006-0093-3.
29. Li, T., Guo, X.-N., Zhu, K.-X., Zhou, H.-M., Effects of alkali on protein polymerization and textural characteristics of textured wheat protein. Food Chemistry 239:Supplement C (2018), 579–587 https://doi.org/10.1016/j.foodchem.2017.06.155.
30. Li, M., Lee, T.-C., Effect of extrusion temperature on solubility and molecular weight distribution of wheat flour proteins. Journal of Agricultural and Food Chemistry 44:3 (1996), 763–768 https://doi.org/10.1021/jf950582h.
31. Morgan, R.G., Steffe, J.F., Ofoli, R.Y., A generalized viscosity model for extrusion of protein doughs. Journal of Food Process Engineering 11:1 (1989), 55–78 https://doi.org/10.1111/j.1745-4530.1989.tb00022.x.
32. Ng, T.S.K., McKinley, G.H., Ewoldt, R.H., Large amplitude oscillatory shear flow of gluten dough: A model power-law gel. Journal of Rheology 55:3 (2011), 627–654 https://doi.org/10.1122/1.3570340.
33. Peleg, M., Corradini, M.G., Normand, M.D., Kinetic models of complex biochemical reactions and biological processes. Chemie Ingenieur Technik 76:4 (2004), 413–423 https://doi.org/10.1002/cite.200406157.
34. Peleg, M., Normand, M.D., Calculating microbial survival parameters and predicting survival curves from non-isothermal inactivation data. Critical Reviews in Food Science and Nutrition 44:6 (2004), 409–418 https://doi.org/10.1080/10408690490489297.
35. Pietsch, V.L., Emin, M.A., Schuchmann, H.P., Process conditions influencing wheat gluten polymerization during high moisture extrusion of meat analog products. Journal of Food Engineering 198:Supplement C (2017), 28–35 https://doi.org/10.1016/j.jfoodeng.2016.10.027.
36. Pommet, M., Morel, M.-H., Redl, A., Guilbert, S., Aggregation and degradation of plasticized wheat gluten during thermo-mechanical treatments, as monitored by rheological and biochemical changes. Polymer 45:20 (2004), 6853–6860 https://doi.org/10.1016/j.polymer.2004.07.076.
37. Rahaman, T., Vasiljevic, T., Ramchandran, L., Shear, heat and pH induced conformational changes of wheat gluten - impact on antigenicity. Food Chemistry 196 (2016), 180–188 https://doi.org/10.1016/j.foodchem.2015.09.041.
38. Redl, A., Guilbert, S., Morel, M.-H., Heat and shear mediated polymerisation of plasticized wheat gluten protein upon mixing. Journal of Cereal Science 38:1 (2003), 105–114 https://doi.org/10.1016/S0733-5210(03)00003-1.
39. Rombouts, I., Lagrain, B., Brijs, K., Delcour, J.A., β-Elimination reactions and formation of covalent cross-links in gliadin during heating at alkaline pH. Journal of Cereal Science 52:3 (2010), 362–367 https://doi.org/10.1016/j.jcs.2010.06.006.
40. Rombouts, I., Lagrain, B., Brunnbauer, M., Koehler, P., Brijs, K., Delcour, J.A., Identification of isopeptide bonds in heat-treated wheat gluten peptides. Journal of Agricultural and Food Chemistry 59:4 (2011), 1236–1243 https://doi.org/10.1021/jf103579u.
41. Schofield, J.D., Bottomley, R.C., Timms, M.F., Booth, M.R., The effect of heat on wheat gluten and the involvement of sulphydryl-disulphide interchange reactions. Journal of Cereal Science 1:4 (1983), 241–253 https://doi.org/10.1016/S0733-5210(83)80012-5.
42. Singh, H., Macritchie, F., Changes in proteins induced by heating gluten dispersions at high temperature. Journal of Cereal Science 39:2 (2004), 297–301 https://doi.org/10.1016/j.jcs.2003.11.004.
43. Strecker, T.D., Cavalieri, R.P., Zollars, R.L., Pomeranz, Y., Polymerization and mechanical degradation kinetics of gluten and glutenin at extruder melt-section temperatures and shear rates. Journal of Food Science 60:3 (1995), 532–537 https://doi.org/10.1111/j.1365-2621.1995.tb09820.x.
44. Van Boekel, M.A.J.S., On the use of the Weibull model to describe thermal inactivation of microbial vegetative cells. International Journal of Food Microbiology 74:1 (2002), 139–159 https://doi.org/10.1016/S0168-1605(01)00742-5.
45. Wang, K., Li, C., Wang, B., Yang, W., Luo, S., Zhao, Y., Zheng, Z., formation of macromolecules in wheat gluten/starch mixtures during twin-screw extrusion: Effect of different additives. Journal of the Science of Food and Agriculture 97:15 (2017), 5131–5138 https://doi.org/10.1002/jsfa.8392.
46. Wolz, M., Kulozik, U., Thermal denaturation kinetics of whey proteins at high protein concentrations. International Dairy Journal 49 (2015), 95–101 https://doi.org/10.1016/j.idairyj.2015.05.008.
47. Wolz, M., Mersch, E., Kulozik, U., Thermal aggregation of whey proteins under shear stress. Food Hydrocolloids 56 (2016), 396–404 https://doi.org/10.1016/j.foodhyd.2015.12.036.
48. Wrigley, C.W., Giant proteins with flour power. Nature 381 (1996), 738–739.