Cleaning; Fouling; Particulate soiling; Protein denaturation; Surface contaminants; XPS
Abstract :
[en] Glass and stainless steel (StSteel, AISI304-2R), previously cleaned with ethanol (-Eth) or with ethanol and UV–Ozone treatment (-UVO), were soiled with quartz suspensions in water and in a β-lactoglobulin (β-LGB) solution, and dried. The cleanability (ease of quartz particle detachment) in water was evaluated using a radial-flow cell. The soiling suspension containing β-LGB was used as such or after heating for 4h at 75°C, which provoked coagulation of about 75% of β-LGB. The substrate–solution interfaces were characterized by X-ray photoelectron spectroscopy (XPS) analysis of conditioned substrates and by contact angle measurements. The substrate surfaces are covered by a layer of organic contaminants which are not removed by pre-cleaning or are adsorbed from the surroundings. The presence of β-LGB in the soiling suspension leads to protein adsorption, but a significant amount of contaminants remains at the surface. For three of the substrates tested (Glass-Eth, Glass-UVO, StSteel-UVO) the increase of cleanability when the soiling suspension contained β-LGB may be explained by lower capillary forces acting upon drying. Capillary forces are proportional to the liquid surface tension and depend in a less important way on substrate contact angle. However the order of cleanability observed for the substrates soiled with a suspension of quartz particles in water (Glass-Eth≅Glass-UVO<StSteel-UVO<StSteel-Eth) and the influence of β-LGB on the cleanability of StSteel-Eth may not be explained only by computed capillary forces. The contact angle may exert a direct influence on droplet spreading and particle–substrate contact. The organic contaminants present on the surfaces, which are often neglected by supposing model solid surfaces, may have a significant influence on cleanability through physico-chemical processes which remain to be appreciated.
Sindic, Marianne ; Université de Liège > Agronomie, Bio-ingénierie et Chimie (AgroBioChem) > Laboratoire Qualité et sécurité des produits agro-aliment.
Dupont-Gillain, C. Christine; Institute of Condensed Matter and Nanosciences – Bio & Soft Matter, Université catholique de Louvain, Croix du Sud 1/L7.04.01, B-1348 Louvain-la-Neuve, Belgium
Matagne, André ; Université de Liège > Département des sciences de la vie > Enzymologie et repliement des protéines
Rouxhet, G. Paul; Institute of Condensed Matter and Nanosciences – Bio & Soft Matter, Université catholique de Louvain, Croix du Sud 1/L7.04.01, B-1348 Louvain-la-Neuve, Belgium
Language :
English
Title :
Influence of substrate nature and β-lactoglobulin on cleanability after soiling by suspension spraying and drying
Publication date :
16 May 2015
Journal title :
Chemical Engineering Science
ISSN :
0009-2509
eISSN :
1873-4405
Publisher :
Pergamon Press - An Imprint of Elsevier Science, Oxford, United Kingdom
Allain A.F., Paquin P., Subirade M. Relationships between conformation of beta-lactoglobulin in solution and gel states as revealed by attenuated total reflection Fourier transform infrared spectroscopy. Int. J. Biol. Macromol. 1999, 26(5):337-344.
Alsteens D., Dague E., Rouxhet P.G., Baulard A.R., Dufrêne Y.F. Direct measurement of hydrophobic forces on cell surfaces using AFM. Langmuir 2007, 23:11977-11979.
Bansal B., Chen X.D. Fouling of heat exchangers by dairy fluids - A review. Proceedings of 6th International Conference on Heat Exchanger Fouling and Cleaning - Challenges and Opportunities. Engineering Conferences International 2005, 149-157. Kloster Irsee, Germany, RP2. M.R. Malayeri, A.P. Watkinson (Eds.).
Bansal B., Chen X.D. A critical review of milk fouling in heat exchangers. Science 2006, 5(2):27-33.
Bansal, B., Chen, X.D., Lin, S.X.Q., 2005. Skim milk fouling during ohmic heating. In: Müller-Steinhagen, H., Malayeri, M.R., Watkinson, P.A. (Eds.), Proceedings of the 6th International Conference on Heat Exchanger Fouling and Cleaning - Challenges and Opportunities. Engineering Conference International, Kloster Irsee, Germany, RP2, pp. 133-140.
Blanpain-Avet P., Hédoux A., Guinet Y., Paccou L., Petit J., Six T., Delaplace G. Analysis by Raman spectroscopy of the conformational structure of whey proteins constituting fouling deposits during the processing in a heat exchanger. J. Food Eng. 2012, 110(1):86-94.
Carrotta R., Bauer R., Waninge R., Rischel C. Conformational characterization of oligomeric intermediates and aggregates in β-lactoglobulin heat aggregation. Protein Sci. 2001, 10(7):1312-1318.
Changani S.D., Belmar-Beiny M.T., Fryer P.J. Engineering and chemical factors associated with fouling and cleaning in milk processing. Exp. Therm. Fluid Sci. 1997, 14(4):392-406.
Detry J.G., Sindic M., Servais M.J., Adriaensen Y., Derclaye S., Deroanne C., Rouxhet P.G. Physico-chemical mechanisms governing the adherence of starch granules on materials with different hydrophobicities. J. Colloid Interface Sci. 2011, 355(1):210-221.
Detry J.G., Deroanne C., Sindic M., Jensen B.B.B. Laminar flow in radial flow cell with small aspect ratios: numerical and experimental study. Chem. Eng. Sci. 2009, 64(1):31-42.
Detry J.G., Rouxhet P.G., Boulangé-Petermann L., Deroanne C., Sindic M. Cleanability assessment of model solid surfaces with a radial-flow cell. Colloids Surf. A: Physicochem. Eng. Asp. 2007, 302(1-3):540-548.
Genet M.J., Dupont-gillain C.C., Rouxhet P.G. XPS analysis of biosystems and biomaterials. Medical Applications of Colloids 2008, 177-307. Springer, New York. E. Matijević (Ed.).
Goormaghtigh E., Ruysschaert J.-M., Raussens V. Evaluation of the information content in infrared spectra for protein secondary structure determination. Biophys. J. 2006, 90(8):2946-2957.
Ikeda S., Li-Chan E.C.Y. Raman spectroscopy of heat-induced fine-stranded and particulate β-lactoglobulin gels. Food Hydrocoll. 2004, 18(3):489-498.
Ikeda S. Heat-induced gelation of whey proteins observed by rheology, atomic force microscopy, and Raman scattering spectroscopy. Food Hydrocoll. 2003, 17(4):399-406.
Jensen B.B.B., Friis A. Critical wall shear stress for the EHEDG test method. Chem. Eng. Process. Process Intensif. 2004, 43(7):831-840.
Landoulsi J., Genet M.J., Richard C., Kirat K.E., Pulvin S., Rouxhet P.G. Evolution of the passive film and organic constituents at the surface of stainless steel immersed in fresh water. J. Colloid Interface Sci. 2008, 318(2):278-289.
Manavalan P., Johnson W.C. Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra. Anal. Biochem. 1987, 167:76-85.
McClellan S.J., Franses E.I. Effect of concentration and denaturation on adsorption and surface tension of bovine serum albumin. Colloids Surf. B: Biointerfaces 2003, 28(1):63-75.
Pierna J.A.F., Duponchel L., Ruckebusch C., Bertrand D., Baeten V., Dardenne P. Trappist beer identification by vibrational spectroscopy: a chemometric challenge posed at the "Chimiométrie 2010" congress. Chemom. Intell. Lab. Syst. 2012, 113:2-9.
Pitois O., Moucheront P., Château X. Liquid bridge between two moving spheres: an experimental study of viscosity effects. J. Colloid Interface Sci. 2000, 231(1):26-31.
Provencher S.W., Glockner J. Estimation of globular protein secondary structure from circular dichroism. Biochemistry 1981, 20:33-37.
Qi X.L., Holt C., Mcnulty David D., Clarke D.T., Brownlow S., Jones G.R. Effect of temperature on the secondary structure of β-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: a test of the molten globule hypothesis. Biochem. J. 1997, 346:341-346.
Rabinovich Y.I, Adler J.J., Esayanur M.S., Ata A., Singh R., Moudgil B.M. Capillary forces between surfaces with nanoscale roughness. Adv. Colloid Interface Sci. 2002, 96(1-3):213-230.
Robbins P.T., Elliott B.L., Fryer P.J., Belmar M.T., Hasting A.P.M. A comparison of milk and whey fouling in a pilot scale plate heat exchanger: implications for modelling and mechanistic studies. Food Bioprod. Process. 1999, 77(C2):97-106.
Rouxhet P.G. Contact angles and surface energy of solids: relevance and limitations. Advances in Contact Angle, Wettability and Adhesion 2013, 1:347-375. Schrivener Publishing LLC, Salem, MA, USA.
Rouxhet P.G., Misselyn-Bauduin A.M., Ahimou F., Genet M.J., Adriaensen Y., Desille T., Bodson P., Deroanne C. XPS analysis of food products: toward chemical functions and molecular compounds. Surf. Interface Anal. 2008, 40(3-4):718-724.
Schmitt C., Bovay C., Rouvet M., Shojaei-Rami S., Kolodziejczyk E. Whey protein soluble aggregates from heating with NaCl: physicochemical, interfacial, and foaming properties. Langmuir 2007, 23(8):4155-4166.
Speranza G., Gottardi G., Pederzolli C., Lunelli L., Canteri R., Pasquardini L., Carli E., Lui A., Maniglio D., Brugnara M., Anderle M. Role of chemical interactions in bacterial adhesion to polymer surfaces. Biomaterials 2004, 25(11):2029-2037.
Sreerema N., Woody R.W. A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal. Biochem. 1993, 209:32-44.
Sreerema N., Venyaminov S.Y., Woody R.W. Estimation of the number of helical and strand segments in proteins using CD spectroscopy. Protein Sci. 1999, 8:370-380.
Sreerama N., Woody R.W. Estimation of protein secondary structure from CD spectra: comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set. Anal. Biochem. 2000, 287(2):252-260.
Stănciuc N., Aprodu I., Râpeanu G., Bahrim G. Fluorescence spectroscopy and molecular modeling investigations on the thermally induced structural changes of bovine β-lactoglobulin. Innov. Food Sci. Emerg. Technol. 2012, 15:50-56.
Stanley C.G., Peter H.V.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 1989, 182:319-326.
Stefanov I., Baeten V., Abbas O., Vlaeminck B., De Baets B., Fievez V. Evaluation of FT-NIR and ATR-FTIR spectroscopy techniques for determination of minor odd- and branched-chain saturated and trans unsaturated milk fatty acids. J. Agric. Food Chem. 2013, 61(14):3403-3413.
Stephan O., Weisz N., Vieths S., Weiser T., Rabe B., Vatterott W. Protein quantification, sandwich ELISA, and real-time PCR used to monitor industrial cleaning procedures for contamination with peanut and celery allergens. J. AOAC Int. 2004, 87(6):1448-1457.
Tomasetti E., Derclaye S., Delvaux M.H., Rouxhet P.G. Study of material-water interactions using the Wilhelmy plate method. Advances in Contact Angle, Wettability and Adhesion 2013, 1:131-154. Schrivener Publishing LLC, Salem, MA, USA.
Touré Y., Genet M.J., Dupont-Gillain C.C., Sindic M., Rouxhet P.G. Conditioning materials with biomacromolecules: composition of the adlayer and influence on cleanability. J. Colloid Interface Sci. 2014, 432:158-169.
Touré Y., Rouxhet P.G., Dupont-Gillain C.C., Sindic M. Influence of whey protein denaturation on adherence of soiling particles to stainless steel. Fouling and Cleaning in Food Processing 2014, 30-37. Publishing Department of Chemical Engineering & Biotechnology, Cambridge, UK. D.I. Wilson, Y.M.J. Chew (Eds.).
Touré, Y., Rouxhet, P.G., Sindic, M., 2013. Influence of soluble proteins on the adherence of particulate soils. In: Malayeri, M.R., Müller-Steinhagen, H., Watkinson, A.P. (Eds.), Proceedings of the International Conference on Heat Exchanger Fouling and Cleaning, Budapest, Hungary, June 09-14, pp. 285-290, http://www.heatexchanger-fouling.com.
Touré, Y., Rouxhet, P.G., Dupont-Gillain, C.C., Sindic, M., 2011. Influence of soluble polysaccharide on the adherence of particulate soils. In: Malayeri, M.R., Müller-Steinhagen, H., Watkinson, A.P. (Eds.), Proceedings of the International Conference on Heat Exchanger Fouling and Cleaning, Crete Island, Greece, June 05-10, pp. 219-226, http://www.heatexchanger-fouling.com.
Van Stokkum I.H.M., Spoelder H.J.W., Bloemendal M., Van Grondelle R., Groen F.C.A. Estimation of protein secondary structure and error analysis from CD spectra. Anal. Biochem. 1990, 191:110-118.
Vetri V., Militello V. Thermal induced conformational changes involved in the aggregation pathways of beta-lactoglobulin. Biophys. Chem. 2005, 113(1):83-91.
Walstra P., Jenness R. Dairy Chemistry and Physics 1984, John Wiley and Sons, New York.
Whitmore L., Wallace B.A. Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers 2008, 89(5):392-400.
Whitmore L., Wallace B.A. DICHROWEB: an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 2004, 32:W668-W673.
Xiang B.Y., Ngadi M.O., Ochoa-Martinez L.A., Simpson M.V. Pulsed electric field-induced structural modification of whey protein isolate. Food Bioprocess Technol. 2011, 4(8):1341-1348.
Xu D., Yuan F., Jiang J., Wang X., Hou Z., Gao Y. Structural and conformational modification of whey proteins induced by supercritical carbon dioxide. Innov. Food Sci. Emerg. Technol. 2011, 12(1):32-37.
Yang J., Dunker A.K., Powers J.R., Clark S., Swanson B.G. Beta-lactoglobulin molten globule induced by high pressure. J. Agric. Food Chem. 2001, 49(7):3236-3243.
