Modeling, Simulation, and Experimental Validation of Drying and Denaturation Behavior of Whey Protein Isolate–Based Coatings

REFERENCES

• Schmid, M.; Dallmann, K.; Bugnicourt, E.; Cordoni, D.; Wild, F.; Lazzeri, A.; Noller, K. Properties of whey-protein-coated films and laminates as novel recyclable food packaging materials with excellent barrier properties. International Journal of Polymer Science 2012, Article ID 562381.
   Google Scholar
• Schmid, M.; Krimmel, B.; Grupa, U.; Noller, K. Effects of thermally induced denaturation on technological–functional properties of whey protein isolate based films. Journal of Dairy Science 2014, 97(9), 5315–5327.
   PubMed Web of Science ®Google Scholar
• Mc Hugh, T.H.; Aujard, J.F.; Krochta, J.M. Plasticized whey protein edible films: Water vapor permeability properties. Journal of Food Science 1994, 59(2), 416–419.
   Web of Science ®Google Scholar
• Mc Hugh, T.H.; Krochta, J.M. Sorbitol-plasticized vs. glycerol-plasticized whey-protein edible films—Integrated oxygen permeability and tensile property evaluation. Journal of Agricultural and Food Chemistry 1994, 42(4), 841–845.
   Web of Science ®Google Scholar
• Hammann, F.; Schmid, M. Determination and quantification of molecular interactions in protein films: A review. Materials 2014, 7(12), 7975–7996.
   PubMed Web of Science ®Google Scholar
• Onwulata, C.; Huth, P. Whey Processing, Functionality and Health Benefits; Wiley-Blackwell: Oxford, UK, 2008.
   Google Scholar
• de Wit, J.N. Lecturer's Handbook on Whey and Whey Products; European Whey Products Association: Brussels, 2001.
   Google Scholar
• Chen, X.D.; Chen, Z.D.; Nguang, S.K.; Anema, S. Exploring the reaction kinetics of whey protein denaturation/aggregation by assuming the denaturation step is reversible. Biochemical Engineering Journal 1998, 2(1), 63–69.
   Web of Science ®Google Scholar
• Anema, S.G.; McKenna, A.B. Reaction kinetics of thermal denaturation of whey proteins in heated reconstituted whole milk. Journal of Agricultural and Food Chemistry 1996, 44(2), 422–428.
   Web of Science ®Google Scholar
• Schmid, M.; Hinz, L.-V.; Wild, F.; Noller, K. Effects of hydrolysed whey proteins on the techno-functional characteristics of whey protein–based films. Materials 2013, 6(3), 927–940.
   Web of Science ®Google Scholar
• Haque, A.M.; Putranto, A.; Aldred, P.; Chen, J.; Adhikari, B. Drying and denaturation kinetics of whey protein isolate (WPI) during convective air drying process. Drying Technology 2013, 31(13–14), 1532–1544.
   Web of Science ®Google Scholar
• Haque, A.; Aldred, P.; Chen, J.; Barrow, C.; Adhikari, B. Comparative study of denaturation of whey protein isolate (WPI) in convective air drying and isothermal heat treatment processes. Food Chemistry 2013, 141(2), 702–711.
   PubMed Web of Science ®Google Scholar
• Töpel, A. Chemie und Physik der Milch: Naturstoff- Rohstoff- Lebensmittel; Behr's Verlag: Hamburg, Germany, 2004.
   Google Scholar
• Jovanovic, S.; Barac, M.; Macej, O. Whey proteins—Properties and possibility of application. Mljekarstvo 2005, 55(3), 215–233.
   Google Scholar
• Anema, S.G.; Lloyd, R.J. Analysis of whey protein denaturation: A comparative study of alternative methods. Milchwissenschaft-Milk Science International 1999, 54(4), 206–210.
   Web of Science ®Google Scholar
• Dickow, J.A.; Kaufmann, N.; Wiking, L.; Hammershøj, M. Protein denaturation and functional properties of lenient steam injection heat treated whey protein concentrate. Innovative Food Science and Emerging Technologies 2012, 13, 178–183.
   Web of Science ®Google Scholar
• Haque, A.; Aldred, P.; Chen, J.; Barrow, C.; Adhikari, B. Drying and denaturation characteristics of α-lactalbumin, β-lactoglobulin, and bovine serum albumin in a convective drying process. Journal of Agricultural and Food Chemistry 2014, 62(20), 4695–4706.
   PubMed Web of Science ®Google Scholar
• Regalado, C.; Pérez-Pérez, C.; Lara-Cortés, E.; García-Almendarez, B. Whey protein based edible food packaging films and coatings. In Advances in Agricultural and Food Biotechnology; Guevara-González, R.G.; Torres-Pacheco, I. Eds.; Research Signpost: Trivandrum, India, 2006; 237–261.
   Google Scholar
• Chen, X.D.; Pirini, W.; Ozilgen, M. The reaction engineering approach to modelling drying of thin layer of pulped Kiwifruit flesh under conditions of small Biot numbers. Chemical Engineering and Processing: Process Intensification 2001, 40(4), 311–320.
   Web of Science ®Google Scholar
• Chen, X.D.; Lin, S.X.Q. Air drying of milk droplet under constant and time dependent conditions. AIChE Journal 2005, 51(6), 1790–1799.
   Web of Science ®Google Scholar
• Lin, S.X.Q.; Chen, X.D. Prediction of air drying of milk droplet under relatively high humidity using the reaction engineering approach. Drying Technology 2005, 23(7), 1396–1406.
   Google Scholar
• Lin, S.X.Q.; Chen, X.D. A model for drying of an aqueous lactose droplet using the reaction engineering approach. Drying Technology 2006, 24(11), 1329–1334.
   Web of Science ®Google Scholar
• Lin, S.X.Q.; Chena, X.D. The reaction engineering approach to modelling the cream and whey protein concentrate droplet drying. Chemical Engineering and Processing 2007, 46(5), 437–443.
   Web of Science ®Google Scholar
• Pelegrine, D.H.G.; Gasparetto, C.A. Whey proteins solubility as function of temperature and pH. LWT-Food Science and Technology 2005, 38(1), 77–80.
   Web of Science ®Google Scholar
• Parris, N.; Baginski, M.A. A rapid method for the determination of whey-protein denaturation. Journal of Dairy Science 1991, 74(1), 58–64.
   Web of Science ®Google Scholar
• Anandharamakrishnan, C.; Rielly, C.D.; Stapley, A.G.F. Loss of solubility of α-lactalbumin and β-lactoglobulin during the spray drying of whey proteins. LWT - Food Science and Technology 2008, 41(2), 270–277.
   Web of Science ®Google Scholar
• Ferreira, I.; Cacote, H. Detection and quantification of bovine, ovine and caprine milk percentages in protected denomination of origin cheeses by reversed-phase high-performance liquid chromatography of beta-lactoglobulins. Journal of Chromatography A 2003, 1015(1–2), 111–118.
   PubMed Web of Science ®Google Scholar
• Chen, X.D. The basics of a reaction engineering approach to modeling air-drying of small droplets or thin-layer materials. Drying Technology 2008, 26(6), 627–639.
   Web of Science ®Google Scholar
• Chen, X.D.; Xie, G.Z. Fingerprints of the drying behaviour of particulate or thin layer food materials established using a reaction engineering model. Food and Bioproducts Processing 1997, 75(4), 213–222.
   Web of Science ®Google Scholar
• Putranto, A.; Chen, X.D.; Webley, P.A. Infrared and convective drying of thin layer of polyvinyl alcohol (PVA)/glycerol/water mixture—The reaction engineering approach (REA). Chemical Engineering and Processing 2010, 49(4), 348–357.
   Web of Science ®Google Scholar
• Griffin, W.G.; Griffin, M.C.A.; Martin, S.R.; Price, J. Molecular-basis of thermal aggregation of bovine beta-lactoglobulin-A. Journal of the Chemical Society-Faraday Transactions 1993, 89(18), 3395–3406.
   Google Scholar
• Verheul, M.; Roefs, S.; de Kruif, K.G. Kinetics of heat-induced aggregation of β-lactoglobulin. Journal of Agricultural and Food Chemistry 1998, 46(3), 896–903.
   Web of Science ®Google Scholar
• Sawyer, W.H.; Norton, R.S.; Nichol, L.W.; McKenzie, G.H. Thermodenaturation of bovine beta-lactoglobulin kinetics and introduction of beta-structure. Biochimica et Biophysica Acta 1971, 243(1), 19–30.
   PubMed Web of Science ®Google Scholar
• Dupont, M. Study of a reversible stage in the thermodenaturation of bovine beta-lactoglobulin A. Biochimica et Biophysica Acta 1965, 102(2), 500–513.
   PubMed Web of Science ®Google Scholar
• Sothornvit, R.; Krochta, J.M. Plasticizer effect on mechanical properties of beta-lactoglobulin films. Journal of Food Engineering 2001, 50(3), 149–155.
   Web of Science ®Google Scholar
• Owens, D.; Wendt, R. Estimation of the surface free energy of polymers. Journal of Applied Polymer Science 1969, 13, 1741–1747.
   Web of Science ®Google Scholar
• Rabel, W. Einige Aspekte der Benetzungstheorie und ihre Anwendung auf die Untersuchung und Veränderung der Oberflächeneigenschaften von Polymeren. Farbe und Lack 1971, 77(10), 997–1005.
   Google Scholar
• Kaelble, D. H. Dispersion-polar surface tension properties of organic solids. Journal of Adhesion 1970, 2, 66–81.
   Web of Science ®Google Scholar
• Testing of Plastics and Elastomer Films, Paper, Board and Other Sheet Materials—Determination of Water Vapour Transmission—Part 1: Gravimetric Method. DIN 53122-1:2001-08. Deutsches Institut für Normung e.V.: Berlin, 2001 (in German).
   Google Scholar
• Testing of Plastics—Determination of Gas Transmission Rate—Part 3: Oxygen-Specific Carrier Gas Method for Testing of Plastic Films and Plastics Mouldings. DIN 53380-3:1998-07. Deutsches Institut für Normung e.V: Berlin, 1998 (in German).
   Google Scholar
• Yu, K.; Sharp, I.; Guo, Y.J. Ground-Based Wireless Positioning. Wiley: Hoboken, NJ, 2009.
   Google Scholar
• Grubbs, F.E. Procedures for detecting outlying observations in samples. Technometrics 1969 11(1), 1–21.
   Web of Science ®Google Scholar
• Oldfield, D.J.; Taylor, M.W.; Singh, H. Effect of preheating and other process parameters on whey protein reactions during skim milk powder manufacture. International Dairy Journal 2005, 15(5), 501–511.
   Web of Science ®Google Scholar
• Wang, W. Instability, stabilization, and formulation of liquid protein pharmaceuticals. International Journal of Pharmaceutics 1999, 185(2), 129–188.
   PubMed Web of Science ®Google Scholar
• Ferreira, I.M.; Mendes, E.; Ferreira, M.A. HPLC/UV analysis of proteins in dairy products using a hydrophobic interaction chromatographic column. Analytical Sciences 2001, 17(4), 499–501.
   PubMed Web of Science ®Google Scholar
• Calvo, M.M.; Leaver, J.; Banks, J.M. Influence of other whey proteins on the heat-induced aggregation of α-lactalbumin. International Dairy Journal 1993, 3(8), 719–727.
   Web of Science ®Google Scholar
• Schokker, E.P.; Singh, H.; Creamer, L.K. Heat-induced aggregation of beta-lactoglobulin A and B with alpha-lactalbumin. International Dairy Journal 2000, 10(12), 843–853.
   Web of Science ®Google Scholar
• Dalgleish, D.G.; Senaratne, V.; Francois, S. Interactions between alpha-lactalbumin and beta-lactoglobulin in the early stages of heat denaturation. Journal of Agricultural and Food Chemistry 1997, 45(9), 3459–3464.
   Web of Science ®Google Scholar
• Bernal, V.; Jelen, P. Thermal stability of whey proteins—A calorimetric study. Journal of Dairy Science 1985, 68(11), 2847–2852.
   Web of Science ®Google Scholar
• Brown, R.J. Milk coagulation and protein denaturation. In Fundamentals of Dairy Chemistry; Jenness, R.; Marth, E.H.; Wong, N.P.; Keeney, M. Eds.; Aspen Publishers: New York, 1988; 583–601.
   Google Scholar
• Kessler, H.-G.; Beyer, H.-J. Thermal denaturation of whey proteins and its effect in dairy technology. International Journal of Biological Macromolecules 1991, 13(3), 165–173.
   PubMed Web of Science ®Google Scholar
• Dannenberg, F.; Kessler, H.G. Reaction kinetics of the denaturation of whey proteins in milk. Journal of Food Science 1988, 53(1), 258–263.
   Web of Science ®Google Scholar
• Hines, M.E.; Foegeding, E.A. Interactions of alpha-lactalbumin and bovine serum-albumin with beta-lactoglobulin in thermally induced gelation. Journal of Agricultural and Food Chemistry 1993, 41(3), 341–346.
   Web of Science ®Google Scholar
• Considine, T.; Patel, H.A.; Anema, S.G.; Singh, H.; Creamer, L.K. Interactions of milk proteins during heat and high hydrostatic pressure treatments—A review. Innovative Food Science and Emerging Technologies 2007, 8(1), 1–23.
   Web of Science ®Google Scholar
• Maa, Y.F.; Hsu, C.C. Protein denaturation by combined effect of shear and air–liquid interface. Biotechnology and Bioengineering 1997, 54(6), 503–512.
   PubMed Web of Science ®Google Scholar
• Maa, Y.F.; Nguyen, P.A.; Hsu, C.C. Spray-coating of rhDNase on lactose: Effect of system design, operational parameters and protein formulation. International Journal of Pharmaceutics 1996, 144(1), 47–59.
   Web of Science ®Google Scholar
• Gezimati, J.; Singh, H.; Creamer, L.K. Heat-induced interactions and gelation of mixtures of bovine β-lactoglobulin and serum albumin. Journal of Agricultural and Food Chemistry 1996, 44(3), 804–810.
   Web of Science ®Google Scholar
• Havea, P.; Singh, H.; Creamer, L.K. Characterization of heat-induced aggregates of beta-lactoglobulin, alpha-lactalbumin and bovine serum albumin in a whey protein concentrate environment. Journal of Dairy Research 2001, 68(3), 483–497.
   PubMed Web of Science ®Google Scholar
• Havea, P.; Singh, H.; Creamer, L.K. Formation of new protein structures in heated mixtures of BSA and alpha-lactalbumin. Journal of Agricultural and Food Chemistry 2000, 48(5), 1548–1556.
   PubMed Web of Science ®Google Scholar
• de Wit, J.N. Thermal behaviour of bovine beta-lactoglobulin at temperatures up to 150°C. A review. Trends in Food Science & Technology 2009, 20(1), 27–34.
   Web of Science ®Google Scholar
• Hillier, R.M.; Lyster, R.L.J. Whey protein denaturation in heated milk and cheese whey. Journal of Dairy Research 1979, 46(1), 95–102.
   Web of Science ®Google Scholar
• Dannenberg, F.; Kessler, H.G. Application of reaction-kinetics to the denaturation of whey proteins in heated milk. Milchwissenschaft-Milk Science International 1988, 43(1), 3–7.
   Web of Science ®Google Scholar
• Manji, B.; Kakuda, Y. Thermal denaturation of whey proteins in skim milk. Canadian Institute of Food Science and Technology 1986, 19(4), 163–166.
   Web of Science ®Google Scholar
• Panick, G.; Malessa, R.; Winter, R. Differences between the pressure- and temperature-induced denaturation and aggregation of beta-lactoglobulin A, B, and AB monitored by FT-IR spectroscopy and small-angle X-ray scattering. Biochemistry 1999, 38(20), 6512–6519.
   PubMed Web of Science ®Google Scholar
• Gough, P.; Jenness, R. Heat denaturation of β-lactoglobulins A and B. Journal of Dairy Science 1962, 45(9), 1033–1039.
   Web of Science ®Google Scholar
• Lyster, R.L.J. The denaturation of α-lactalbumin and β-lactoglobulin in heated milk. Journal of Dairy Research 1970, 37(2), 233–243.
   Web of Science ®Google Scholar
• Ruegg, M.; Moor, U.; Blanc, B. Calorimetric study of thermal-denaturation of whey proteins in simulated milk ultrafiltrate. Journal of Dairy Research 1977, 44(3), 509–520.
   Web of Science ®Google Scholar
• Tolkach, A.; Kulozik, U. Reaction kinetic pathway of reversible and irreversible thermal denaturation of β-lactoglobulin. Lait 2007, 87(4–5), 301–315.
   Google Scholar
• Schmid, M. Properties of cast films made from different ratios of whey protein isolate, hydrolysed whey protein isolate and glycerol. Materials 2013, 6(8), 3245–3269.
   Web of Science ®Google Scholar
• Pérez-Gago, M.B.; Nadaud, P.; Krochta, J.M. Water vapor permeability, solubility, and tensile properties of heat-denatured versus native whey protein films. Journal of Food Science 1999, 64(6), 1034–1037.
   Web of Science ®Google Scholar
• Schmid, M.; Sängerlaub, S.; Wege, L.; Stäbler, A. Properties of transglutaminase crosslinked whey protein isolate coatings and cast films. Packaging Technology and Science 2014, 27(10), 799–817.
   Web of Science ®Google Scholar
• Guckian, S.; Dwyer, C.; O'Sullivan, M.; O'Riordan, E.D.; Monahan, F.J. Properties of and mechanisms of protein interactions in films formed from different proportions of heated and unheated whey protein solutions. European Food Research and Technology 2006, 223(1), 91–95.
   Web of Science ®Google Scholar
• Hong, S.I.; Krochta, J.M. Whey protein isolate coating on LDPE film as a novel oxygen barrier in the composite structure. Packaging Technology and Science 2004, 17(1), 13–21.
   Web of Science ®Google Scholar
• Hong, Y.H.; Creamer, L.K. Changed protein structures of bovine beta-lactoglobulin B and alpha-lactalbumin as a consequence of heat treatment. International Dairy Journal 2002, 12(4), 345–359.
   Web of Science ®Google Scholar
• Mate, J.I.; Krochta, J.M. Comparison of oxygen and water vapor permeabilities of whey protein isolate and β-lactoglobulin edible films. Journal of Agricultural and Food Chemistry 1996, 44(10), 3001–3004.
   Web of Science ®Google Scholar