OVALBÜMİNİN TİTANYUM OKSİT VE ZİRKONYA YÜZEYLERLERLE ETKİLEŞİMİ VE ADSORPSİYONUNUN ARAŞTIRILMASI

Yıl 2017, Cilt: 32 Sayı: 2, 0 - 0, 13.06.2017

Türkan Kopaç Erol Kulaç

https://doi.org/10.17341/gazimmfd.322174

Cited By: 2

Öz

 

ÖZ

Ovalbümin proteininin sulu çözelti ortamında TiO₂ ve ZrO₂ tozları ile etkileşimleri ve adsorpsiyonu kesikli sistemde araştırıldı. Adsorpsiyon deneyleri pH 5, 6.4, 8 ortamında 20, 25, 30 °C’de yapıldı. Bulgular, adsorplanan Ovalbümin miktarının, sıcaklık ve adsorbent miktarının artmasıyla arttığını, pH ile azaldığını gösterdi. Zeta potansiyel ölçümleri, Ovalbümin ile TiO₂ ve ZrO₂ arasındaki etkileşimlerin, proteinin izoelektrik noktasına yakın olan pH 5’de daha fazla olduğunu gösterdi. Ovalbüminin TiO₂ ve ZrO₂ üzerinde farklı sıcaklıklar ve çözelti pH’larındaki adsorpsiyonunun her iki adsorbent için de birinci mertebe kinetiği ile ilerlediği görüldü.

Anahtar Kelimeler

Ovalbumin, adsorpsiyon; adsorpsiyon kinetiği; TiO2; ZrO2

Kaynakça

• Lee, J.H., Oh, J.Y., Kim, D.M., “MMA/MPEOMA Copolymers as Coating Materials for Improved Blood Compatibility: Protein Adsorption Study”, J. Mater. Sci. - Mat. Med., Cilt 10, 629-634, 1999.
• Murthy, R., Shell, C.E., Grunlan, M.S., “The Influence of Poly(ethylene oxide) Grafting Via Siloxane Tethers on Protein Adsorption”, Biomaterials, Cilt 30, 2433-2439, 2009.
• Roth, C.M., Neal, B.L., Lenhoff, M., “Van der Waals Interactions Involving Proteins”, Biophys. J., Cilt 70, 1996, 977-987, 1996.
• Su, Y.L., Li, C., “The Reorientation of Poly (2-dimethylamino ethyl methacrylate) After Environment Stimuli Improves Hydrophilicity and Resistance of Protein Adsorption”, J. Colloid Interface Sci., Cilt 316, 344-349, 2007
• Serro, APVAD, Fernandes, A.C., Saramago, BDJV, “Bovine Serum Albumin Adsorption on Titania Surfaces and Its Relation to Wettability Aspects”, J. Biomed. Mater. Res. Part B: Applied Biomaterials, Cilt 46, 376-381, 1999.
• Imamura, K., Shimomura, M., Nagai, D., Akamatsu, M., Nakanishi K., “Adsorption Characteristics of Various Proteins to a Titanium Surfaces”, J. Biosci. Bioeng. Cilt 106, 273-278, 2008.
• Latour, R.A., Jr. Biomaterials: Protein-Surface Interactions. Encyclopedia of Biomaterials and Biomedical Engineering. Taylor & Francis, New York, A.B.D., 1–15, 2005.
• Latour, R.A., Jr., Trembley, S.D., Tian, Y., Lickfield, G.C., Wheeler, A.P., “Determination of Apparent Thermodynamic Parameters for Adsorption of a Midchain Peptidyl Residue onto a Glass Surface”, J. Biomed. Mater. Res., Cilt 49, No 1, 58-65, 2000.
• Poleunis, C., Rubio, C., Compere, C., Bertrand, P., “Role of Salts on the BSA Adsorption on Stainless Steel in Aqueous Solutions”, II. ToF-SIMS Spectral and Chemical Mapping Study, Surf. Interface Anal., Cilt 34, 55-58. 2002.
• Browne, M.M., Lubarsky, G.V., Davidson, M.R., Bradley, R.H., “Protein Adsorption onto Polystyrene Surfaces Studied by XPS and AFM”, Surf. Sci., Cilt 553, 155-167, 2004.
• Marchin, K., Phung, S., Berrie, C.L., “Evidence for Fibrinogen Mobility on Hydrophobic Surfaces”, e-J. Surf. Sci. Nanotech., Cilt 3, 173-178, 2005.
• Rezwan, K., Meier, L.P., Rezwan, M., Vörös, J., Textor, M., Gauckler, L.J., “Bovine Serum Albumin onto Colloidal Al2O3 Particles: A New Model Based on Zeta Potential and UV-Vis Measurements”, Langmuir, Cilt 20, No 23, 10055–10061, 2004.
• Okutucu, B., Dinçer, A., Habib, O., Zıhnıoğlu, F., “Comparison of Five Methods for Determination of Total Plasma Protein Concentration”, J. Biochem. Bioph. Methods, Cilt 70, 709-711, 2007.
• Fang, F., Szleifer, I., “Controlled Release of Proteins From Polymer-Modified Surfaces”, PNAS, Cilt 103, 5769-5774, 2006.
• Putman, B., Meeren, V.D., Thierens, D., “Reduced Bovine Serum Albumin Adsorption by Prephosphatation of Powdered Zirconium Oxide”, Colloids Surf., A - Physicochemical and Engineering Aspects, Cilt 121, 81-88, 1997.
• Nakanishi, K., Sakiyama, T., Imamura K., “On the Adsorption of Proteins on Solid Surfaces, A Common But Very Complicated Phenomenon”, J. Biosci. Bioeng., Cilt 91, 233-224, 2001.
• Fidelio, G.D., Austen, B.M., Chapman, D., Lucy, J.A., “Interactions of Ovalbumin and of its Putative Signal Sequence with Phospholipid Monolayers”, Biochem. J., Cilt 244, 295-301, 1987.
• Beeley, J.A., Stevenson, S.M., Beeley, J.G., Biochim. Biophys. Acta., Cilt 285, 293–300, 1972.
• Norde, W., MacRitchie, F., Nowicka, G., Lyklema, J., J. Coll. Int. Sci., Cilt 112, 447–456, 1986.
• Huntington, J.A., Stein, P.E., “Structure and Properties of Ovalbumin”, J Chromatogr B, Cilt 756, 189–198, 2001.
• Baynes, J., Dominiczak, M.H., Medical Biochemistry, 2nd ed. Mosby, St. Louis, 2005.
• Szewczuk-Karpisz, K., Wiśniewska, M., “Adsorption Properties of the Albumin–Chromium(III) Oxide System – Effect of Solution pH and Ionic Strength”, Soft Materials, Cilt 12:3, 268-276, 2014.
• Szewczuk-Karpisz, K., Wiśniewska, M., “Investigation of Removal Possibilities of Chromium(III) oxide from Water Solution in the Presence of Albumins”, Int. J. Environ. Sci. Technol., Cilt 12, 2947–2956, 2015.
• Reiman, C., Bredow, T., “Adsorption of Nitrogen and Ammonia at Zirconia Surfaces”, J. Mol. Struct.- THEOCHEM, Cilt 903, 89-99, 2009.
• Chen, X.B., Li, Y.C., Plessis, J.D., Hodgson, P.D., Wen, C., “Influence of Calcium Ion Deposition on Apatite-Inducing Ability of Porous Titanium for Biomedical Applications”, Acta Biomaterialia, Cilt 5, 1808-1820, 2009.
• Chen, J., Poon, C. S., “Photocatalytic Construction and Building Materials: From Fundamentals to Applications”, Building and Environment, Cilt 44, Sayı 9, 1899-1906, 2009.
• Ying, P., Viana, A.S., Abrantes, L.M., Jin, G., “Adsorption of Human Serum Albumin onto Gold: a Combined Electrochemical and Elipsometric Study”, J. Colloid Interface Sci., Cilt 279, 95-99, 2004.
• Barral, S., Villa-Garcia, M.A., Rendueles, M., Diaz, M., “Interactions Between Whey Proteins and Kaolinite Surfaces”, Acta Materialia, Cilt 56, 2784-2790, 2008.
• Li, S., Hu, J., Liu, B., “A Study on the Adsorption Behavior of Protein onto Functional Microspheres”, J. Chem. Technol. and Biotechnol., Cilt 80, 531-536, 2005.
• Shamim, N., Liang, H., Hidajat, K., Udin, M.S., “Adsorption, Desorption, and Conformational Changes of Lysozyme from Thermosensitive Nanomagnetic Particles”, J. Colloid Interface Sci., Cilt320, 2008. 15-21, 2008.
• Rezwan, K., Studart, A.R., Vörös, J., Gauckler, L.J., “Change of Zeta Potential of Biocompatible Colloidal Oxide Particles upon Adsorption of Bovine Serum Albumin and Lysozyme”, J. Phys Chem. B., Cilt 109, 14469-1447, 2005.
• Kopaç, T., Bozgeyik, K., Yener, J., “Effect of pH and Temperature on the Adsorption of Bovine Serum Albumin onto Titanium Dioxide”, Colloids Surf., A - Physicochem. Eng. Aspects, Cilt 322, 19-28, 2008.
• Kopaç, T., Bozgeyik, K., “Effect of Surface Area Enhancement on the Adsorption of Bovine Serum Albumin onto Titanium Dioxide”, Colloids Surf., B - Biointerfaces, Cilt 76, 265-271, 2010.
• Bozgeyik, K., Kopaç, T., “Adsorption of Bovine Serum Albumin onto Metal Oxides: Adsorption Equilibrium and Kinetics onto Alumina and Zirconia”, Int. J. Chemical Reactor Engineering, Cilt 8:A139, 1-26, 2010.
• Lowry, O. H., Rosebrough, N.L., Farr, A.L., Randall, R. J., “Protein measurement with the folin phenol reagent”. J. Biol. Chem., Cilt 193, 265-275, 1951.
• Gupta,G.S., Prasad, G., Singh, V.N., “Removal of Chromedye from Aqueous Solutions by Mixed Adsorbents: Fly Ash and Coal”, Water Res., Cilt 24, 45-50, 1990.
• Yener, J., Kopaç, T., Doğu, G., Doğu, T., “Adsorption of Basic Yellow 28 from Aqueous Solutions with Clinoptilolite and Amberlite”, J. Colloid Interface Sci., Cilt 294, 255–264, 2006.
• Imamura, K., Shimomura, M., Nagai, S., Akamutsu, M., Nakanishi, K., “Adsorption Charecteristics of Various Proteins to a Titanium Surfaces”, J. Biosci. Bioeng., Cilt 106, No. 3, 273-278, 2008.