Controlling Food Protein Folding and Aggregation: Challenges and Perspectives in Industry, Experiments and Simulation.
- Erik Santiso (North Carolina State University, USA)
- Fernando Luís Barroso da Silva (University of São Paulo, Brazil)
- Donal MacKernan (University College Dublin, Ireland)
The proposed workshop comes at an ideal time in order to compare and creatively confront different modern approaches to food protein systems. Its primary purpose will be to cross-pollinate the different theoretical, experimental and simulation approaches in order to progress towards a unified description of the molecular mechanism to generate new functionalities and rheological properties, including mouth feel, and to enhance processing methods. Coarse-grained models , as well as more detailed ones should pave the way in this endeavour. The workshop will first present the state-of-the-art as well as induce constructive interactions between these different theoretical approaches, as well as with the available experimental data . Besides the scientific aspects, we aim the establishment of new academic contacts between the participants. This will also contribute to push the present state-of-the-art of the field.
Three key issues or questions to be specifically discussed in the workshop are as follows.
(A) the accuracy of mesoscale models and phenomenological will be compared with molecular and where necessary quantum approaches with appropriate modelling of pH and salt concentration both under equilibrium and shear conditions, for the eventual parametrization of the former, validated also by experiments.
(B) One of the challenges will include an adequate treatment of dynamical properties – including in particular rheological aspects important for food taste and processing alike.
(C) One open experimental and industrial question is whether environmental changes;
happen on a similar or slightly faster time scale than the protein unfolding, which would possibly explain the large variations in the end product that occur depending on minute variations in composition, temperature, flow rates etc. But this is only an educated guess, Another possible explanation would be simply a vast number of accessible metastable states. A central objective of the workshop would be to thrash out these ideas. Such an objective calls for the use of the most advanced methods of simulation, both from a rigorous perspective, and more pragmatically motivated phenomenological models, i.e. points (A) and (B) above, and with experiment.
1. J. Petit, A.-L. Herbig, A. Moreau, and G. Delaplace, Influence of calcium on beta-lactoglobulin denaturation kinetics: Implications in unfolding and aggregation mechanisms, J. Dairy Sci. 94:57945810 (2011).
2. Taco Nicolai, Michel Britten, Christophe Schmitt. Beta-Lactoglobulin and WPI aggregates: Formation, structure and applications Food Hydrocolloids 25 (2011).
3. Food protein functionality: A comprehensive approach, E. A. Foegeding , Jack P. Davis,Food Hydrocolloids Volume 25, 1853 (2011).
4. Peter Fischer and E. J. Windhab, Rheology of food materials , Current Opinion in Colloid & Interface Science 16 , 3640 (2011).
5. F.A. Escobedo, J.J. de Pablo, Molecular simulation of polymeric networks and gels: Phase behavior and swelling, Physics Reports 318 (1999).
6. C. Akkermans, P. Venema, S. S. Rogers, A. J. van der Goot, R. M. Boom, E. van der Linden, Shear pulses nucleate fibril aggregation. Food Biophysics 1, 144 (2006).
7. M. Khaldi P. Blanpain-Avet , R. Guérin G. Ronse, L. Bouvier, C. André, S. Bornaz, T. Croguennec , R. Jeantet , G. Delaplace, Effect of calcium content and flow regime on whey protein fouling and cleaning in a plate heat exchanger Journal of Food Engineering 147, 6878, (2015).
8. 13 C. H.J. Evers, T. Andersson, M. Lund, and M. Skepo Adsorption of Unstructured Protein Casein to Hydrophobic and Charged Surfaces; Langmuir 28, 11843 (2012).
9. How surface composition of high milk proteins powders is influenced by spray drying temperature. C. Gaiani , M. Morand , C. Sanchez , E. Arab Tehrany , M. Jacquot , P. Schuck , R. Jeantet , J. Scher , Colloids and Surfaces B: Biointerfaces 75, 377384 (2010).
10. N. Bhattacharjee, P. Rani, and P. Biswas, Capturing molten globule state of lactalbumin through constant pH molecular dynamics simulations , Journal of Chemical Physics 138, 095101 (2013).
11. Teixeira, A. A. R., Lund, M., and da Silva, F. L. B. Fast proton titration scheme for multiscale modeling of protein solutions. Journal of Chemical Theory and Computation, 6(10), 3259-3266. (2010).
12. Donnini, S., Tegeler, F., Groenhof, G., & Grubmuller, H. Constant pH molecular dynamics in explicit solvent with dynamics. Journal of chemical theory and computation, 7(6), 1962-1978. (2011).
13. Ryan, K. N., Vardhanabhuti, B., Jaramillo, D. P., van Zanten, J. H., Coupland, J. N., Foegeding, E. A. Stability and mechanism of whey protein soluble aggregates thermally treated with salts, Food Hydrocolloids 27, 411420 (2012).
14. Batt, C. A., Brady, J., Sawyer, L.. Design improvements of lactoglobulin. Trends in Food Science & Technology 5 (8), 261265 (1994).
15. Clare, D. A., Daubert, C. R. Expanded Functionality of Modified Whey Protein Dispersions after Transglutaminase Catalysis. Journal of Food Science 76, 576 (2011).
16. Dickinson, E. Interfacial structure and stability of food emulsions as affected by proteinpolysaccharide interactions. Soft Matter 4, 932 (2008).
17. Dickinson, E. Stabilising emulsion-based colloidal structures with mixed food ingredients. J. Sci. Food Agric. 93, 710 (2013).
18. de Wit, J.. Thermal behaviour of bovine lactoglobulin at temperatures up to 150 C. A review. Trends in Food Science & Technology 20, 2734 (2009).
19. Wijayanti, H. B., Bansal, N., Deeth, H. C. Stability of whey proteins during thermal processing: A review. Comprehensive Reviews in Food Science and Food Safety 13, 12351251 (2014).
20. Zeiler, R. N. W., Bolhuis, P. G.. Exposure of thiol groups in the heat induced denaturation of lactoglobulin. MS 41 (10-12), 10061014 (2015).
21. Ryan, K. N., Foegeding, E. A. Formation of soluble whey protein aggregates and their stability in beverages. Food Hydrocolloids 43, 265274 (2015).
22. da Silva, F. L. B., and Jönsson, B. Polyelectrolyteprotein complexation driven by charge regulation. Soft Matter, 5(15), 2862-2868 (2009).
23. Santiso, E. E. Understanding the effect of adsorption on activated processes using molecular theory and simulation. Molecular Simulation, 40(7-9), 664-677. (2014).
24. Lyubartsev, A. P., Karttunen, M., Vattulainen, I., and Laaksonen, A. On coarse-graining by the inverse monte carlo method: Dissipative particle dynamics simulations made to a precise tool in soft matter modeling. Soft Materials, 1(1), 121-137 (2002).
25. ONeill, G. J., T. Egan, J. C. Jacquier, M. OSullivan, and E. D. ORiordan. Kinetics of immobilisation and release of tryptophan, riboflavin and peptides from whey protein microbeads. Food chemistry 180 (2015): 150-155.
26. Mac Kernan, D., Ciccotti, G., and Kapral, R. Trotter-based simulation of quantum-classical dynamics. The Journal of Physical Chemistry B, 112(2), 424-432 (2008).
27. Cottone, G. R. A. Z. I. A., Giuffrida, S., Ciccotti, G., & Cordone, L. Molecular dynamics simulation of sucrose and trehalose;coated carboxy yoglobin. Proteins: Structure, Function, and Bioinformatics, 59(2), 291-302 (2005).
28. Deiana, A., and Giansanti, A. Tuning the precision of predictors to reduce overestimation of protein disorder over large datasets. Journal of bioinformatics and computational biology, 11(02), 1250023 (2013).