Advertisement

BioNanoScience

, Volume 9, Issue 3, pp 672–682 | Cite as

Thermodynamics, Kinetics, and Adsorption Properties of Biomolecules onto Carbon-Based Materials Obtained from Food Wastes

  • Özkan Demirbaş
  • Mehmet Harbi Çalımlı
  • Buse Demirkan
  • Mehmet Hakkı Alma
  • Mehmet Salih NasEmail author
  • Anish KhanEmail author
  • Abdullah M. AsiriEmail author
  • Fatih ŞenEmail author
Article
  • 42 Downloads

Abstract

In this research, adsorption of Candida rugosa lipase enzyme (CRLE) onto activated carbon obtained from apple bark was carried out, and the thermodynamic parameters of adsorption process were investigated. The surface structural change of lipase enzyme and activated carbon was studied. The thermodynamic functions such as enthalpy, entropy, Gibbs free energy, and activation energy were investigated in their experimental work. The thermodynamic parameters of ΔG, Ea, ΔH, and ΔS were calculated as − 75.56, 13.42, − 15.29 kJ mol−1, and 202.2 J mol−1 K−1 for CRLE adsorption, respectively. The experiment results showed that the adsorption process of CRLE on activated carbon is spontaneous and exothermic. The maximum adsorption capacity according to CRLE was 5.5 pH. The maximum adsorption capacity of active carbon was found to be 96.2 mg/g at pH 5.5, 309.5 K, and initial enzyme concentration of 5.0 × 10−3 M. The protein molecules at this point are very stable that is close to the isoelectric point of lipase enzyme. As a result, we can say that the activated carbon can be used as an effective adsorbent for the adsorption of CRLE.

Keywords

Activated carbon Adsorption Lipase enzyme Thermodynamic parameters 

Notes

References

  1. 1.
    Daşdelen, Z., Yıldız, Y., Eriş, S., & Şen, F. (2017). Enhanced electrocatalytic activity and durability of Pt nanoparticles decorated on GO-PVP hybrid material for methanol oxidation reaction. Applied Catalysis B: Environmental, 219, 511–516.  https://doi.org/10.1016/j.apcatb.2017.08.014.CrossRefGoogle Scholar
  2. 2.
    Bozkurt, S., Tosun, B., Sen, B., Akocak, S., Savk, A., Ebeoğlugil, M. F., & Sen, F. (2017). A hydrogen peroxide sensor based on TNM functionalized reduced graphene oxide grafted with highly monodisperse Pd nanoparticles. Analytica Chimica Acta, 989, 88–94.  https://doi.org/10.1016/j.aca.2017.07.051.CrossRefGoogle Scholar
  3. 3.
    Goksu, H., Sert, H., Kilbas, B., & Sen, F. (2017). Recent advances in the reduction of nitro compounds by heterogenous catalysts. Current Organic Chemistry, 21, 794–820.  https://doi.org/10.2174/1385272820666160525123907.CrossRefGoogle Scholar
  4. 4.
    Demirbaş Ö., Çalımlı M.H., Kuyuldar E., Halil B.İ., Nas M.S., Şen F. (2019) Thermodynamic kinetics and sorption of bovine serum albumin with different clay materials. In: Inamuddin (eds) applications of ion exchange materials in biomedical industries. Springer, Cham. doi.org/10.1007/978-3-030-06082-4_6.
  5. 5.
    Aday, B., Pamuk, H., Kaya, M., & Sen, F. (2016). Graphene oxide as highly effective and readily recyclable catalyst using for the one-pot synthesis of 1,8-dioxoacridine derivatives. Journal of Nanoscience and Nanotechnology, 16, 6498–6504.  https://doi.org/10.1166/jnn.2016.12432.CrossRefGoogle Scholar
  6. 6.
    Eris, S., Daşdelen, Z., & Sen, F. (2018). Enhanced electrocatalytic activity and stability of monodisperse Pt nanocomposites for direct methanol fuel cells. Journal of Colloid and Interface Science, 513, 767–773.  https://doi.org/10.1016/j.jcis.2017.11.085.CrossRefGoogle Scholar
  7. 7.
    Akocak, S., Şen, B., Lolak, N., Şavk, A., Koca, M., Kuzu, S., & Şen, F. (2017). One-pot three-component synthesis of 2-amino-4H-chromene derivatives by using monodisperse Pd nanomaterials anchored graphene oxide as highly efficient and recyclable catalyst. Nano-Structures & Nano-Objects, 11, 25–31.  https://doi.org/10.1016/j.nanoso.2017.06.002.CrossRefGoogle Scholar
  8. 8.
    Demirbas, O., Calimli, M.H., Kuyuldar, E. et al. (2019) Equilibrium, kinetics, and thermodynamic of adsorption of enzymes on diatomite clay materials. BioNanoScience.  https://doi.org/10.1007/s12668-019-00615-1.
  9. 9.
    Erken, E., Pamuk, H., Karatepe, Ö., Başkaya, G., Sert, H., Kalfa, O. M., & Şen, F. (2016). New Pt(0) nanoparticles as highly active and reusable catalysts in the C1–C3 alcohol oxidation and the room temperature dehydrocoupling of dimethylamine-borane (DMAB). Journal of Cluster Science, 27, 9–23.  https://doi.org/10.1007/s10876-015-0892-8.CrossRefGoogle Scholar
  10. 10.
    Ayranci, R., Başkaya, G., Güzel, M., Bozkurt, S., Şen, F., & Ak, M. (2017). Carbon based nanomaterials for high performance optoelectrochemical systems. ChemistrySelect, 2, 1548–1555.  https://doi.org/10.1002/slct.201601632.CrossRefGoogle Scholar
  11. 11.
    Çalımlı, M. H., Demirbaş, Ö., Aygün, A., et al. (2018). Immobilization kinetics and mechanism of bovine serum albumin on diatomite clay from aqueous solutions. Applied Water Science, 8, 209.  https://doi.org/10.1007/s13201-018-0858-8.CrossRefGoogle Scholar
  12. 12.
    Karatepe, Ö., Yıldız, Y., Pamuk, H., Eris, S., Dasdelen, Z., & Sen, F. (2016). Enhanced electrocatalytic activity and durability of highly monodisperse Pt@PPy–PANI nanocomposites as a novel catalyst for the electro-oxidation of methanol. RSC Advances, 6, 50851–50857.  https://doi.org/10.1039/C6RA06210E.CrossRefGoogle Scholar
  13. 13.
    Şen, F., Demirbaş, Ö., Çalımlı, M. H., et al. (2018). The dye removal from aqueous solution using polymer composite films. Applied Water Science, 8, 206.  https://doi.org/10.1007/s13201-018-0856-x.Google Scholar
  14. 14.
    Abrahamson, J. T., Sempere, B., Walsh, M. P., Forman, J. M., Şen, F., Şen, S., Mahajan, S. G., Paulus, G. L. C., Wang, Q. H., Choi, W., & Strano, M. S. (2013). Excess thermopower and the theory of thermopower waves. ACS Nano, 7, 6533–6544.  https://doi.org/10.1021/nn402411k.CrossRefGoogle Scholar
  15. 15.
    Demirbaş, Ö., & Nas, M. S. (2016). Kinetics and mechanism of the adsorption of methylene blue from aqueous solution onto Turkish green clay. Archives of Current Research International, 6(3), 1–10.  https://doi.org/10.9734/ACRI/2016/30677.CrossRefGoogle Scholar
  16. 16.
    Bujdák, J., & Rode, B. M. (1997). Silica, alumina, and clay-catalyzed alanine peptide bond formation. Journal of Molecular Evolution, 45, 457–466.  https://doi.org/10.1007/PL00006250.CrossRefGoogle Scholar
  17. 17.
    Bujdák, J., Le, S. H., & Rode, B. M. (1996). Montmorillonite catalyzed peptide bond formation: the effect of exchangeable cations. Journal of Inorganic Biochemistry, 63, 119–124.  https://doi.org/10.1016/0162-0134(95)00186-7.CrossRefGoogle Scholar
  18. 18.
    Causserand, C., Jover, K., Aimar, P., & Meireles, M. (1997). Modification of clay cake permeability by adsorption of protein. J Memb Sci, 137, 31–44.  https://doi.org/10.1016/S0376-7388(97)00181-6.CrossRefGoogle Scholar
  19. 19.
    Ding, X., & Henrichs, S. M. (2002). Adsorption and desorption of proteins and polyamino acids by clay minerals and marine sediments. Marine Chemistry, 77, 225–237.  https://doi.org/10.1016/S0304-4203(01)00085-8.CrossRefGoogle Scholar
  20. 20.
    Fusi, P., Ristori, G. G., Calamai, L., & Stotzky, G. (1989). Adsorption and binding of protein on “clean” (homoionic) and “dirty” (coated with Fe oxyhydroxides) montmorillonite, illite and kaolinite. Soil Biology and Biochemistry, 21, 911–920.  https://doi.org/10.1016/0038-0717(89)90080-1.CrossRefGoogle Scholar
  21. 21.
    Gupta, A., Loew, G. H., & Lawless, J. (1983). Interaction of metal ions and amino acids: possible mechanisms for the adsorption of amino acids on homoionic smectite clays. Inorganic Chemistry, 22, 111–120.  https://doi.org/10.1021/ic00143a025.CrossRefGoogle Scholar
  22. 22.
    Quiquampoix, H., Staunton, S., Baron, M. H., & Ratcliffe, R. G. (1993). Interpretation of the pH dependence of protein adsorption on clay mineral surfaces and its relevance to the understanding of extracellular enzyme activity in soil. Colloids and Surfaces A: Physicochemical and Engineering Aspects, 75, 85–93.  https://doi.org/10.1016/0927-7757(93)80419-F.CrossRefGoogle Scholar
  23. 23.
    Rigou, P., Rezaei, H., Grosclaude, J., Staunton, S., & Quiquampoix, H. (2006). Fate of prions in soil: adsorption and extraction by electroelution of recombinant ovine prion protein from montmorillonite and natural soils. Environmental Science & Technology, 40, 1497–1503.  https://doi.org/10.1021/es0516965.CrossRefGoogle Scholar
  24. 24.
    Violante, A. (1995). Physicochemical properties of protein-smectite and protein-Al(OH)x-smectite complexes. Clay Minerals, 30, 325–336.  https://doi.org/10.1180/claymin.1995.030.4.06.CrossRefGoogle Scholar
  25. 25.
    Schmid, R. D., & Verger, R. (1998). Lipases: interfacial enzymes with attractive applications. Angewandte Chemie International Edition, 37, 1608–1633.  https://doi.org/10.1002/(SICI)1521-3773(19980703)37:12<1608::AID-ANIE1608>3.0.CO;2-V.CrossRefGoogle Scholar
  26. 26.
    Albertsson, A., & Srivastava, R. (2008). Recent developments in enzyme-catalyzed ring-opening polymerization☆. Advanced Drug Delivery Reviews, 60, 1077–1093.  https://doi.org/10.1016/j.addr.2008.02.007.CrossRefGoogle Scholar
  27. 27.
    Gitlesen, T., Bauer, M., & Adlercreutz, P. (1997). Adsorption of lipase on polypropylene powder. Biochimica et Biophysica Acta, Lipids and Lipid Metabolism, 1345, 188–196.  https://doi.org/10.1016/S0005-2760(96)00176-2.CrossRefGoogle Scholar
  28. 28.
    Cao, L. (2005) Carrier-bound immobilized enzymes. doi:  https://doi.org/10.1002/3527607668.
  29. 29.
    Yu, W. H., Li, N., Tong, D. S., Zhou, C. H., Lin, C. X., & Xu, C. Y. (2013). Adsorption of proteins and nucleic acids on clay minerals and their interactions: a review. Applied Clay Science, 80–81, 443–452.  https://doi.org/10.1016/j.clay.2013.06.003.CrossRefGoogle Scholar
  30. 30.
    Blanco, R. M., Terreros, P., Fernández-Pérez, M., et al. (2004). Functionalization of mesoporous silica for lipase immobilization. Journal of Molecular Catalysis B: Enzymatic, 30, 83–93.  https://doi.org/10.1016/j.molcatb.2004.03.012.CrossRefGoogle Scholar
  31. 31.
    Hook, F., Rodahl, M., Kasemo, B., & Brzezinski, P. (1998). Structural changes in hemoglobin during adsorption to solid surfaces: effects of pH, ionic strength, and ligand binding. Proceedings of the National Academy of Sciences, 95, 12271–12276.  https://doi.org/10.1073/pnas.95.21.12271.CrossRefGoogle Scholar
  32. 32.
    Oliva, F. Y., Avalle, L. B., Cámara, O. R., & De Pauli, C. P. (2003). Adsorption of human serum albumin (HSA) onto colloidal TiO2 particles, part I. Journal of Colloid and Interface Science, 261, 299–311.  https://doi.org/10.1016/S0021-9797(03)00029-8.CrossRefGoogle Scholar
  33. 33.
    Sternik, D., Staszczuk, P., Grodzicka, G., Pękalska, J., & Skrzypiec, K. (2004). Studies of physicochemical properties of the surfaces with the chemically bonded phase of BSA. Journal of Thermal Analysis and Calorimetry, 77, 171–182.  https://doi.org/10.1023/B:JTAN.0000033201.86803.fa.CrossRefGoogle Scholar
  34. 34.
    Vroman, L., & Adams, A. L. (1969). Findings with the recording ellipsometer suggesting rapid exchange of specific plasma proteins at liquid/solid interfaces. Surface Science, 16, 438–446.  https://doi.org/10.1016/0039-6028(69)90037-5.CrossRefGoogle Scholar
  35. 35.
    Aygün, A., Yenisoy-Karakaş, S., & Duman, I. (2003). Production of granular activated carbon from fruit stones and nutshells and evaluation of their physical, chemical and adsorption properties. Microporous and Mesoporous Materials, 66, 189–195.  https://doi.org/10.1016/j.micromeso.2003.08.028.CrossRefGoogle Scholar
  36. 36.
    Rajeshwarisivaraj, Sivakumar, S., Senthilkumar, P., & Subburam, V. (2001). Carbon from cassava peel, an agricultural waste, as an adsorbent in the removal of dyes and metal ions from aqueous solution. Bioresource Technology, 80, 233–235.  https://doi.org/10.1016/S0960-8524(00)00179-6.CrossRefGoogle Scholar
  37. 37.
    Avom, J., Mbadcam, J. K., Noubactep, C., & Germain, P. (1997). Adsorption of methylene blue from an aqueous solution on to activated carbons from palm-tree cobs. Carbon N Y, 35, 365–369.  https://doi.org/10.1016/S0008-6223(96)00158-3.CrossRefGoogle Scholar
  38. 38.
    El-Sheikh, A. H., Newman, A. P., Al-Daffaee, H. K., Phull, S., & Cresswell, N. (2004). Characterization of activated carbon prepared from a single cultivar of Jordanian olive stones by chemical and physicochemical techniques. Journal of Analytical and Applied Pyrolysis, 71, 151–164.  https://doi.org/10.1016/S0165-2370(03)00061-5.CrossRefGoogle Scholar
  39. 39.
    Wu, F. (1999). Pore structure and adsorption performance of the activated carbons prepared from plum kernels. Journal of Hazardous Materials, 69, 287–302.  https://doi.org/10.1016/S0304-3894(99)00116-8.CrossRefGoogle Scholar
  40. 40.
    Tsai, W., Chang, C., Lin, M., Chien, S., Sun, H., & Hsieh, M. (2001). Adsorption of acid dye onto activated carbons prepared from agricultural waste bagasse by ZnCl2 activation. Chemosphere, 45, 51–58.  https://doi.org/10.1016/S0045-6535(01)00016-9.CrossRefGoogle Scholar
  41. 41.
    Senthilkumaar, S., Varadarajan, P. R., Porkodi, K., & Subbhuraam, C. V. (2005). Adsorption of methylene blue onto jute fiber carbon: kinetics and equilibrium studies. Journal of Colloid and Interface Science, 284, 78–82.  https://doi.org/10.1016/j.jcis.2004.09.027.CrossRefGoogle Scholar
  42. 42.
    Yalçın, N., & Sevinç, V. (2000). Studies of the surface area and porosity of activated carbons prepared from rice husks. Carbon N Y, 38, 1943–1945.  https://doi.org/10.1016/S0008-6223(00)00029-4.CrossRefGoogle Scholar
  43. 43.
    Girgis, B. S., & El-Hendawy, A.-N. A. (2002). Porosity development in activated carbons obtained from date pits under chemical activation with phosphoric acid. Microporous and Mesoporous Materials, 52, 105–117.  https://doi.org/10.1016/S1387-1811(01)00481-4.CrossRefGoogle Scholar
  44. 44.
    Chang, Y. K., Chu, L., Tsai, J. C., & Chiu, S. J. (2006). Kinetic study of immobilized lysozyme on the extrudate-shaped NaY zeolite. Process Biochemistry, 41, 1864–1874.  https://doi.org/10.1016/j.procbio.2006.03.039.CrossRefGoogle Scholar
  45. 45.
    https://www.tarimbilgisi.com, date of access:23.09.2018.
  46. 46.
    Amuda, O. S., Giwa, A. A., & Bello, I. A. (2007). Removal of heavy metal from industrial wastewater using modified activated coconut shell carbon. Biochemical Engineering Journal, 36, 174–181.  https://doi.org/10.1016/j.bej.2007.02.013.CrossRefGoogle Scholar
  47. 47.
    Guo, Y., & Bustin, R. (1998). FTIR spectroscopy and reflectance of modern charcoals and fungal decayed woods: implications for studies of inertinite in coals. International Journal of Coal Geology, 37, 29–53.  https://doi.org/10.1016/S0166-5162(98)00019-6.CrossRefGoogle Scholar
  48. 48.
    Figueiredo, J., Pereira, M. F., Freitas, M. M., & Órfão, J. J. (1999). Modification of the surface chemistry of activated carbons. Carbon N Y, 37, 1379–1389.  https://doi.org/10.1016/S0008-6223(98)00333-9.CrossRefGoogle Scholar
  49. 49.
    Natalello, A., Ami, D., Brocca, S., Lotti, M., & Doglia, S. M. (2005). Secondary structure, conformational stability and glycosylation of a recombinant Candida rugosa lipase studied by Fourier-transform infrared spectroscopy. The Biochemical Journal, 385, 511–517.  https://doi.org/10.1042/BJ20041296.CrossRefGoogle Scholar
  50. 50.
    Vinu, A., Murugesan, V., & Hartmann, M. (2004). Adsorption of lysozyme over mesoporous molecular sieves MCM-41 and SBA-15: influence of pH and aluminum incorporation. The Journal of Physical Chemistry. B, 108, 7323–7330.  https://doi.org/10.1021/jp037303a.CrossRefGoogle Scholar
  51. 51.
    Sreeramamurthy, R., & Menon, P. G. (1975). Oxidation of H2S on active carbon catalyst. Journal of Catalysis, 37, 287–296.CrossRefGoogle Scholar
  52. 52.
    Reshmi R.S.S. (2007) Immobilization and characteristics of Candida rugosa lipase onto siliceous mesoporous molecular sieves and montmorillonite K-10 for synthesis of flavour esters. In: Proc. Int. Conf. Adv. Mater. Compos. India: NIIST, pp 819–824.Google Scholar
  53. 53.
    Tekin, N., Demirbaş, Ö., & Alkan, M. (2005). Adsorption of cationic polyacrylamide onto kaolinite. Microporous and Mesoporous Materials, 85, 340–350.  https://doi.org/10.1016/j.micromeso.2005.07.004.CrossRefGoogle Scholar
  54. 54.
    Vermöhlen, K., Lewandowski, H., Narres, H. D., & Schwuger, M. (2000). Adsorption of polyelectrolytes onto oxides — the influence of ionic strength, molar mass, and Ca2+ ions. Colloids and Surfaces A: Physicochemical and Engineering Aspects, 163, 45–53.  https://doi.org/10.1016/S0927-7757(99)00429-X.CrossRefGoogle Scholar
  55. 55.
    Dalla, V. R., Sebrão, D., Nascimento, M., & Soldi, V. (2005). Carboxymethyl cellulose and poly(vinyl alcohol) used as a film support for lipases immobilization. Process Biochemistry, 40, 2677–2682.  https://doi.org/10.1016/j.procbio.2004.12.004.CrossRefGoogle Scholar
  56. 56.
    Pronk, W., Kerkhof, P., Van Helden, C., & van’T Riet, K. (1988). The hydrolysis of triglycerides by immobilized lipase in a hydrophiiic membrane reactor. Biotechnology and Bioengineering, 32, 512–518.  https://doi.org/10.1002/bit.260320414.CrossRefGoogle Scholar
  57. 57.
    Gregory, J. (1994) Introduction to modern colloid science, Robert J. Hunter. Oxford University press, Oxford, 1993. Pp. viii + 338, price £14.95 (paperback). ISBN 0-19-855386-2. Polymer International 35:105–106. doi:  https://doi.org/10.1002/pi.1994.210350115.
  58. 58.
    Doğan, M., Alkan, M., Demirbaş, Ö., Özdemir, Y., & Özmetin, C. (2006). Adsorption kinetics of maxilon blue GRL onto sepiolite from aqueous solutions. Chemical Engineering Journal, 124, 89–101.  https://doi.org/10.1016/j.cej.2006.08.016.CrossRefGoogle Scholar
  59. 59.
    Lee, D. C., & Chapman, D. (1986). Infrared spectroscopic studies of biomembranes and model membranes. Bioscience Reports, 6, 335–356.CrossRefGoogle Scholar
  60. 60.
    Demirbas, O. (2006) Methyl violetine biosorption on casein surface.Google Scholar
  61. 61.
    Ho, Y., & McKay, G. (1999). The sorption of lead(II) ions on peat. Water Research, 33, 578–584.  https://doi.org/10.1016/S0043-1354(98)00207-3.CrossRefGoogle Scholar
  62. 62.
    Ozturk, N., & Kavak, D. (2005). Adsorption of boron from aqueous solutions using fly ash: batch and column studies. Journal of Hazardous Materials, 127, 81–88.  https://doi.org/10.1016/j.jhazmat.2005.06.026.CrossRefGoogle Scholar
  63. 63.
    Aharoni, C., Sideman, S., & Hoffer, E. (2007). Adsorption of phosphate ions by collodion-coated alumina. Journal of Chemical Technology and Biotechnology, 29, 404–412.  https://doi.org/10.1002/jctb.503290703.CrossRefGoogle Scholar
  64. 64.
    Ho, Y. S., & McKay, G. (1998). Sorption of dye from aqueous solution by peat. Chemical Engineering Journal, 70, 115–124.  https://doi.org/10.1016/S0923-0467(98)00076-1.CrossRefGoogle Scholar
  65. 65.
    Basyaruddin, M., Rahman, A., Basri, M., Hussein, M. Z., et al. (2003). Activated carbon as support for lipase immobilization. Eurasian ChemTech Journal, 5, 115–119.Google Scholar
  66. 66.
    Fagain, C.O. (1997) Manipulating protein stability in stabilizing proteins functions, Heidelberg, Berlin, Springer, New York. 67.Google Scholar
  67. 67.
    Karthikeyan, T., Rajgopal, S., & Miranda, L. (2005). Chromium(VI) adsorption from aqueous solution by sawdust activated carbon. Journal of Hazardous Materials, 124, 192–199.  https://doi.org/10.1016/j.jhazmat.2005.05.003.CrossRefGoogle Scholar
  68. 68.
    Bhattacharya, A., Naiya, T., Mandal, S., & Das, S. (2007). Adsorption, kinetics and equilibrium studies on removal of Cr(VI) from aqueous solutions using different low-cost adsorbents. Chemical Engineering Journal, 137, 529–541.  https://doi.org/10.1016/j.cej.2007.05.021.Google Scholar
  69. 69.
    Sharma, Y. C. (2001). Effect of temperature on interfacial adsorption of Cr(VI) on Wollastonite. Journal of Colloid and Interface Science, 233, 265–270.  https://doi.org/10.1006/jcis.2000.7232.CrossRefGoogle Scholar
  70. 70.
    Sariri, R. B. T. (1996). Effect of surface chemistry on protein interaction with hydrogel contact lenses. Iranian Polymer Journal, 5, 266.Google Scholar
  71. 71.
    Xu, H., Li, M., & He, B. (1995). Immobilization of Candida cylindracea lipase on methyl acrylate-divinyl benzene copolymer and its derivatives. Enzyme and Microbial Technology, 17, 194–199.  https://doi.org/10.1016/0141-0229(94)00038-S.CrossRefGoogle Scholar
  72. 72.
    Lian, L., Guo, L., & Guo, C. (2009). Adsorption of Congo red from aqueous solutions onto ca-bentonite. Journal of Hazardous Materials, 161, 126–131.  https://doi.org/10.1016/j.jhazmat.2008.03.063.CrossRefGoogle Scholar
  73. 73.
    Montero, S., Blanco, A., Virto, M. D., Carlos, L. L., Agud, I., Solozabal, R., Lascaray, J., de Renobales, M., Llama, M. J., & Serra, J. L. (1993). Immobilization of Candida rugosa lipase and some properties of the immobilized enzyme. Enzyme and Microbial Technology, 15, 239–247.  https://doi.org/10.1016/0141-0229(93)90144-Q.CrossRefGoogle Scholar
  74. 74.
    Guncheva, M., Paunova, K., Dimitrov, M., & Yancheva, D. (2014). Stabilization of Candida rugosa lipase on nanosized zirconia-based materials. Journal of Molecular Catalysis B: Enzymatic, 108, 43–50.CrossRefGoogle Scholar
  75. 75.
    Demiral, H., Demiral, İ., Tümsek, F., & Karabacakoğlu, B. (2008). Adsorption of chromium(VI) from aqueous solution by activated carbon derived from olive bagasse and applicability of different adsorption models. Chemical Engineering Journal, 144, 188–196.  https://doi.org/10.1016/j.cej.2008.01.020.CrossRefGoogle Scholar
  76. 76.
    Salis, A., Cugia, F., Setzu, S., Mula, G., & Monduzzi, M. (2010). Effect of oxidation level of n+ type mesoporous silicon surface on the adsorption and the catalytic activity of Candida rugosa lipase. Journal of Colloid and Interface Science, 345, 448–453.CrossRefGoogle Scholar
  77. 77.
    Lu, P., & Hsieh, Y. L. (2009). Lipase bound cellulose nanofibrous membrane via cibacron blue F3GA affinity ligand. Journal of Membrane Science, 330, 288–296.CrossRefGoogle Scholar
  78. 78.
    Amirkhani, L., Moghaddas, J., & Malmiri, H. J. (2016). Candida rugosa lipase immobilization on magnetic silica aerogel nanodispersion. RSC Advances, 6, 12676–12687.CrossRefGoogle Scholar
  79. 79.
    Alves, M., Aracri, F., Cren, É., & Mendes, A. (2017). Isotherm, kinetic, mechanism and thermodynamic studies of adsorption of a microbial lipase on a mesoporous and hydrophobic resin. Chemical Engineering Journal, 311, 1–12.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2019

Authors and Affiliations

  1. 1.Department of Chemistry, Faculty of Science and LiteratureUniversity of BalikesirBalikesirTurkey
  2. 2.Tuzluca Vocational High SchoolIgdir UniversityIgdirTurkey
  3. 3.Sen Research Group, Department of Biochemistry, Faculty of Arts and ScienceDumlupınar UniversityKütahyaTurkey
  4. 4.Department of Environmental, Faculty of EngineeringUniversity of IgdirIgdirTurkey
  5. 5.Chemistry Department, Faculty of ScienceKing Abdulaziz UniversityJeddahSaudi Arabia
  6. 6.Center of Excellence for Advanced Materials ResearchKing Abdulaziz UniversityJeddahSaudi Arabia

Personalised recommendations