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رحمانی, حدیثه, لکزیان, امیر, کریمی, علیرضا, حلاج نیا, اکرم. (1396). بررسی فعالیت و پایداری آنزیم لاکاز آزاد تثبیت شده در حضور کانی‌های مونتموریلونیت و زئولیت. سامانه مدیریت نشریات علمی, 5(1), 1-13. doi: 10.22092/sbj.2017.113095
حدیثه رحمانی; امیر لکزیان; علیرضا کریمی; اکرم حلاج نیا. "بررسی فعالیت و پایداری آنزیم لاکاز آزاد تثبیت شده در حضور کانی‌های مونتموریلونیت و زئولیت". سامانه مدیریت نشریات علمی, 5, 1, 1396, 1-13. doi: 10.22092/sbj.2017.113095
رحمانی, حدیثه, لکزیان, امیر, کریمی, علیرضا, حلاج نیا, اکرم. (1396). 'بررسی فعالیت و پایداری آنزیم لاکاز آزاد تثبیت شده در حضور کانی‌های مونتموریلونیت و زئولیت', سامانه مدیریت نشریات علمی, 5(1), pp. 1-13. doi: 10.22092/sbj.2017.113095
رحمانی, حدیثه, لکزیان, امیر, کریمی, علیرضا, حلاج نیا, اکرم. بررسی فعالیت و پایداری آنزیم لاکاز آزاد تثبیت شده در حضور کانی‌های مونتموریلونیت و زئولیت. سامانه مدیریت نشریات علمی, 1396; 5(1): 1-13. doi: 10.22092/sbj.2017.113095

بررسی فعالیت و پایداری آنزیم لاکاز آزاد تثبیت شده در حضور کانی‌های مونتموریلونیت و زئولیت

زیست شناسی خاک
مقاله 2، دوره 5، شماره 1، شهریور 1396، صفحه 1-13    اصل مقاله (1.12 M)
نوع مقاله: مقاله پژوهشی
شناسه دیجیتال (DOI): 10.22092/sbj.2017.113095
نویسندگان
حدیثه رحمانی1؛ امیر لکزیان* 2؛ علیرضا کریمی3؛ اکرم حلاج نیا4
1دانشجوی دکتری گروه علوم خاک، دانشکده کشاورزی، دانشگاه فردوسی مشهد
2استاد گروه علوم خاک، دانشکده کشاورزی، دانشگاه فردوسی مشهد
3دانشیار گروه علوم خاک، دانشکده کشاورزی، دانشگاه فردوسی مشهد
4استادیار گروه علوم خاک، دانشکده کشاورزی، دانشگاه فردوسی مشهد
چکیده
آنزیم لاکاز از گروه مهمترین آنزیم­هایی است که در سال­های گذشته به سبب توانایی آن در اکسید کردن ترکیب‌های گوناگون و آلاینده­های محیطی پایدار، نگاه بسیاری را در زمینه زیست بهسازی به سوی خود جلب کرده است. با نگاه به پایداری کم و هزینه­های ساخت و فراوری بالای آنزیم­ها، بی‌جنب­سازی آنها بر رویه نگهدارنده­ها می­تواند راهی شایسته در راستای افزایش پایداری کارکرد آنزیم باشد. برای بررسی برهم­کنش لاکاز گرفته شده از قارچ ترامتس ورسیکالر (Trametes versicolor) با کانی­های مونتموریلونیت و زئولیت سه آزمایش جداگانه در قالب طرح کاملاً تصادفی با دو تکرار در شرایط آزمایشگاهی انجام شد. آزمایش­ها به ترتیب شامل چهار سطح pH (5، 6، 7 و 8)، نه سطح دمایی (4 و80-10 درجه سانتیگراد) و هفت سطح زمان انکوباسیون (صفر، 1، 2، 5، 10، 20 و 30 روز) بودند. بر پایه آزمایش نخست، بالاترین اندازه جذب آنزیم بر رویه­های کانی­های بررسی شده در 5=pH دیده شد و با افزایش pH، جذب آنزیمی کاهش یافت. در آزمایش دوم، بالاترین اندازه فعالیت نسبی برای لاکاز آزاد در دمای 20 درجه سانتیگراد، برای لاکاز بی‌جنب­شده بر مونتموریلونیت در دماهای 80 و 4 درجه­سانتیگراد و برای لاکاز بی‌جنبش­شده بر زئولیت در دماهای 4 و 70 درجه­سانتیگراد بود. لاکاز بی جنبش­شده پایداری خوبی را در برابر دماهای پایین و بالا نشان داد. در آزمایش سوم، بالاترین اندازه فعالیت نسبی (100 درصد) برای لاکاز بی‌جنبش­شده بر مونتموریلونیت و زئولیت در زمان انکوباسیون 20 روز و برای لاکاز آزاد در زمان 5 روز دیده شد. برپایه این پژوهش، بی‌جنبش‌سازی پیامد شایسته‌ای را بر پایداری فعالیت آنزیم لاکاز نشان داد.
کلیدواژه‌ها
پایداری؛ زئولیت؛ بی‌جنبش‌سازی؛ فعالیت؛ لاکاز و مونتموریلونیت
عنوان مقاله [English]
Studying the activity and stability of Free and immobilized Laccase enzyme (Trametes versicolor) on Montmorillonite and zeolite minerals
نویسندگان [English]
H. Rahmani1؛ A. Lakzian2؛ A. R. Karimi3؛ A. Halajnia4
1PhD student, Department. of Soil Sciences, Faculty of Agriculture, Ferdowsi University of Mashhad
2Professor, Department. of Soil Sciences, Faculty of Agriculture, Ferdowsi University of Mashhad
3Associate professor, Department. of Soil Sciences, Faculty of Agriculture, Ferdowsi University of Mashhad
4Assistant professor, Department. of Soil Sciences, Faculty of Agriculture, Ferdowsi University of Mashhad
چکیده [English]
Laccase is among the most important enzymes that has attracted much attention in the field of bioremediation in recent years, due to its ability to oxidize various compounds and persistent environmental pollutants. Since free from of Laccase has low operational stability with high cost of production, there are some limitations on the commercial applications in industrial and environmental biotechnology. In this regard, immobilization of such enzymes on absorbent surfaces can be a good way to increase stability and operational life of the enzyme. In order to examine the interactions between Laccase (Trametes versicolor) with Montmorillonite and zeolite minerals, three different experiments were done separately in a completely randomized design with two replications in vitro conditions. Experiments were included four levels of pH (5, 6, 7 and 8),  nine levels of temperature (4 °C and 10-80 °C) and seven levels of incubation time (0, 1, 2, 5, 10, 20 and 30 days), respectively. Based on the results, the highest enzyme adsorption on the surface of studied minerals was observed in pH=5 and enzyme absorption decreased with increasing pH. Furthermore, the highest relative activities were obtained for free Laccase at 20 °C, for immobilized Laccase on Montmorillonite at 80 and 4 °C and for immobilized Laccase on zeolite at 4 and 70 °C. Immobilized Laccase showed a remarkable stability to low and high temperatures. Maximum relative activity (100%) for immobilized Laccase on Montmorillonite and zeolite was observed in 20th day of incubation time and for free Laccase in 5th day of incubation time. Indeed, immobilization indicated a proper effect on Laccase enzyme activity retention. 
کلیدواژه‌ها [English]
Activity, Immobilization, laccase, Montmorillonite, Stability, Zeolite
مراجع
  1. Addorisio, V., Sannino, F., Mateoa, C. and Guisan, J.M. 2013. Oxidation of phenyl compounds using strongly stable immobilized-stabilized laccase from Trametes versicolor. Process Biochemistry 48:1174–1180.
  2. Ahn, M.Y. Dec, J. Kim, J. E. and Bollag, J. M. 2002. Bioremediation and Biodegradation, Treatment of 2,4-Dichlorophenol Polluted Soil with Free and Immobilized Laccase. Journal of Environmental Quality 31:1509-1515.
  3. Anita, A., Sastry, C.A. and Hashim, M.A. 1997. Immobilization of urease on vermiculite. Bioprocess Engineering 16:375-380.
  4. Arica, M.Y., Altintas, B. and Bayramoglu, G. 2009. Immobilization of laccase onto spacer-arm attached non-porous poly(GMA/EGDMA) beads: application for textile dye degradation. Bioresource Technology 100:665–9.
  5. Arroyo, M. 1998. Inmovilización de enzimas. Fundamentos, métodos y aplicaciones. Ars Pharmaceutica 39:23–39.
  6. Bayramoglu, G., Yilmaz, M. and Arica, M.Y. 2010a. Preparation and characterization of epoxyfunctionalized magnetic chitosan beads: laccase immobilized for degradation of reactive dyes. Bioprocess and Biosystems Engineering 33:439–48.
  7. Bayramoglu, G., Yilmaz, M. and Arica, M.Y. 2010b. Reversible immobilization of laccase to poly(4-vinylpyridine) grafted and Cu(II) chelated magnetic beads: biodegradation of reactive dyes. Bioresource Technology 101:6615–21.
  8. Brandi, P., Annibale, A.D., Galli, C., Gentili, P. and Pontes, A.S.N. 2006. In search for practical advantages from the immobilisation of an enzyme: the case of laccase, Journal of Molecular Catalysis B: Enzymatic 41:61–69.
  9. Cabana, H., Ahamed, A. and Leduc, R. 2011. Conjugation of laccase from the white rot fungus Trametes versicolor to chitosan and its utilization for the elimination of triclosan. Bioresource Technology 102:1656–62.
  10. Camarero, S., García, O., Vidal, T., Colom, J., Del Río, J.C., Gutiérrez, A., Martínez, M.J. and Martínez, A.T. 2002. Flax pulp bleaching  and residual lignin modification by laccasemediator systems. Progress in Biotechnology 21:213–22.
  11. Cardoso, F.P., Neto, S.A., Ciancaglini, P. and De Andrade, A.R. 2012. The use of PAMAM dendrimers as a platform for laccase immobilization: kinetic characterization of the enzyme. Applied Biochemistry and Biotechnology 167:1854–64.
  12. Cerrone, F., Barghini, P., Pesciaroli, C. and Fenice, M. 2011. Efficient removal of pollutants from olive washing wastewater in bubble-column bioreactor by Trametes versicolor. Chemosphere 84:254–9.
  13. Cetinus, S.A. and Oztop, H.N. 2003. Immobilization of catalase into chemically cross-linked chitosan beads. Enzyme and Microbial Technology 32:889–894.
  14. Chea, V., Paolucci-Jeanjean, D., Belleville, M.P. and Sanchez, J. 2012. Optimization and characterization of an enzymatic membrane for the degradation of phenolic compounds. Catalysis Today 193:49–56.
  15. Fernández-Fernández, M., Sanromán, M.A. and Moldes, D. 2013. Recent developments and applications of immobilized laccase. Biotechnology Advances 31:1808–1825.
  16. Flip, H. and Claus, Z. K. 1995. Effects of soil minerals on the microbial formation of enzymes and their possible use in remediation of chemically polluted sites. p. 409-419. In: P. M. Huang et al. (ed.) Environmental impact of soil component interactions. Vol. 1. Natural and anthropogenic organics. CRC Press/Lewis Publ., Boca Raton, FL.
  17. Freire, R.S., Durán,  N. and Kubota, L.T. 2001. Effects of fungal laccase immobilization procedures for the development  of  a  biosensor  for  phenol  compounds.  Talanta 54:681–6.
  18. Georgieva, S., Godjevargova, T., Portaccio, M., Lepore, M. and Mita, D.G. 2008. Advantages in using non-isothermal bioreactors in bioremediation of water polluted by phenol by means of immobilized laccase from Rhus vernicifera. Journal of Molecular Catalysis B: Enzymatic 55:177–84.
  19. Gianfreda, L. and Bollag, J. M. 1994. Effect of Soils on the Behavior of Immobilized Enzymes. Soil Science Society of America Journal 58:1672-1681.
  20. Gianfreda, L. and Bollag. J.M. 1994. Effect of soils on the behavior of immobilized enzymes. Soil Science Society of America Journal 58:1672–1681.
  21. Goldstein, L. 1973. A new polymine carrier for immobilization of proteins of water insoluble derivatives of pepsin and trypsin. Biochimica et Biophysica Acta 327:132-137.
  22. Guo, M., Lu, F., Liu, M., Li, T., Pu, J., Wang, N., et al. 2008. Purification of recombinant laccase from Trametes versicolor in Pichia methanolica and its use for the decolorization of  anthraquinone dye. Biotechnology Letters 30:2091–6.
  23. Habeeb, A.F.S.A. and Hiramoto. R. 1968. Reaction  of  proteins  with  glutaraldehyde. Archives of Biochemistry and Biophysics 126:16-26.
  24. Hu, X., Zhao, X. and Hwang, H. 2007. Comparative study of immobilizedTrametes versicolorlaccase on nanoparticles and kaolinite. Chemosphere 66:1618–26.
  25. Hu, X., Zhao, X. and Hwang, H.M. 2007. Comparative study of immobilized Trametes versicolor laccase on nanoparticles and kaolinite. Chemosphere 66:1618–1626.
  26. Jansen, E.F., Tomimatsu, Y. and Olson, A.C. 1971. Cross-linking of α-chymotrypsin and other proteins by reaction with glutaraldehyde. Archives of Biochemistry and Biophysics 144:394-400.
  27. Jia, J.B., Zhang, S.P., Wang, P. and Wang, H.J. 2012. Degradation of high concentration 2,4-dichlorophenol by simultaneous photocatalytic-enzymatic process using TiO2/UV and laccase. Journal of Hazardous Materials 205:150–155.
  28. Jiang, D.S., Long, S.Y., Huang, J., Xiao, H.Y. and Zhou, J.Y. 2005. Immobilization of Pucnoporus sanguineus laccase on magnetic chitosan microspheres. Biochemical Engineering Journal 25:15–23.
  29. Kalkan, N.A., Aksoy, S., Aksoy, E.A. and Hasirci, N. 2012. Preparation of chitosan-coated magnetite nanoparticles and application for immobilization of laccase. Journal of Applied Polymer Science 123:707–16.
  30. Karagoz, B., Bayramoglu, G., Altintas, B., Bicak, N. and Arica, M.Y. 2011. Amine  functional monodisperse microbeads via precipitation polymerization of N-vinyl formamide: immobilized laccase for benzidine based dyes degradation. Bioresource  Technology 102:6783–90.
  31. Krajewska, B. 2009. Ureases. II. Properties and their customizing by enzyme immobilizations: A review. Journal of Molecular Catalysis B: Enzymatic 59:22–40.
  32. Kunamneni, A., Ghazi, I., Camarero, S., Ballesteros, A., Plou, F.J. and Alcalde, M. 2008. Decolorization of synthetic dyes by laccase immobilized on epoxy-activated carriers. Process Biochemistry 43:169–78.
  33. Kurniawati, S. and Nicell, J.A. 2008. Characterization of Trametes versicolor laccase for the transformation of aqueous phenol. Bioresource Technology 99:7825–34.
  34. Lai, C., Zeng, G.M., Huang, D.L., Zhao, M.H., Huang, H.L., Huang, C., Wei, Z., Li, N.J., Xu, P., Zhang, C. and Xie, G.X. 2013. Effect of ABTS on the adsorption of Trametes versicolor laccase on alkali lignin. International Biodeterioration and Biodegradation 82: 180-186.
  35. Leonowicz, A., Sarkar, J.M. and Bollag, J.M. 1988. Improvement in stability of an immobilized fungal laccase. Applied Microbiology and Biotechnology 29:129–135.
  36. Li, W.X., Sun, H.Y. and Zhang, R.F. 2015. Immobilization of laccase on a novel ZnO/SiO2 nano-composited support for dye decolorization. 2015 Global Conference on Polymer and Composite Materials (PCM 2015). IOP Conf. Series: Materials Science and Engineering 87 (2015) 012033.
  37. Loera, O., Pérez Pérez, M., Cristina, I., Barbosa Rodríguez, J.R. and Villaseñor Ortega, F. 2006. Laccases. Anonymous Advances in Agricultural and Food Biotechnology. Research Signpost p. 323–40.
  38. Lu, L., Zhao, M. and Wang, Y. 2007. Immobilization of laccase by alginate–chitosan microcapsules and its use in dye decolorization. World Journal of Microbiology and Biotechnology 23:159-166.
  39. Madhavi, V. and Lele, S. S. 2009. Laccase: Properties and Applications. BioResources 4:1694-1717.
  40. Majeau, J.A., Brar, S.K. and Tyagi, R.D. 2010. Laccases for removal of recalcitrant and emerging pollutants. Bioresource Technology 101:2331–50.
  41. Makboul, H. E. and Ottow, J. C. G. 1979. Michaelis Constant (Km) of Acid Phospatase as Affected byMontmorilionite, Illite, and Kaolinite Clay Minerals. Journal of Microbial Ecology 5:207-213.
  42. Mateo, C., Palomo, J.M., Fernandez-Lorente, G., Guisan, J.M. and Fernandez-Lafuente, R. 2007. Improvement of enzyme activity, stability and selectivity via immobilization techniques. Enzyme and Microbial Technology 40:1451–63.
  43. Matijoˇsyte, I., Arends, I.W.C.E., de Vries, S. and Sheldon, R.A. 2010. Preparation and use of cross-linked enzyme aggregates  (CLEAs)  of  laccases. Journal of  Molecular  Catalysis B: Enzyme 62:142–8.
  44. Missau, J., Scheid, A. J., Foletto, E. L., Jahn, S. L., Mazutti, M. A. and Kuhn, R. C. 2014. Immobilization of commercial inulinase on alginate–chitosan beads. Sustainable Chemical Processes. 2:13.
  45. Naidja, A., Huang, P.M. and Bollag, J.M. 1997. Activity of tyrosinase immobilized on hydroxyaluminum–montmorillonite complexes. Journal of Molecular Catalysis A: Chemical 115: 305–316.
  46. Naidja, A., Huang, P.M. and Bollag, J.M. 2000. Enzyme-Clay Interactions and Their Impact on Transformations of Natural and Anthropogenic Organic Compounds in Soil. Journal of Environmental Quality 29:677-691.
  47. Park, J.H., Xue, H., Jung, J.S. and Ryu, K. 2012. Immobilization of laccase on carbon nanomaterials. Korean Journal of Chemical Engineering 29:1409–12.
  48. Pazarlioglu, N.K., Akkaya, A., Akdogan, H.A. and Gungor, B. 2010. Biodegradation of direct blue 15 by free and immobilized Trametes versicolor. Water Environment Research 82:579–85.
  49. Piontek, K., Antorini, M. and Choinowski, T. 2002. Crystal structure of a laccase  from the fungus Trametes versicolor at 1.90˚ A resolution containing a full  complement  of coppers.  Journal of Biological Chemistry 277:37663-9. 
  50. Plagemann, R., Jonas, L. and Kragl, U. 2011. Ceramic honeycomb as support for covalent immobilization of laccase from Trametes versicolor and transformation of nuclear fast red. Applied Microbiology and Biotechnology 90:313–20.
  51. Prévoteau, A. and Faure, C. 2012. Effect  of  onion-type multilamellar liposomes on Trametes versicolor laccase activity and stability. Biochimie 94:59–65.
  52. Reku´c, A.,  Jastrzembska, B., Liesiene, J. and Bryjak, J. 2009. Comparative studies on immobilized laccase behaviour in packed-bed and batch reactors. Journal of Molecular Catalysis B: Enzymatic 57:216–223.
  53. Rekuć, A., Jastrzembska, B., Liesiene, J. and Bryjak, J. 2009. Comparative studies on immobilized laccase behaviour in packed-bed and batch reactors. Journal of Molecular Catalysis B: Enzymatic 57:216–23.
  54. Rodriguez -Couto, S. and Toca -Herrera, J.L. 2006. Industrial and biotechnological applications of laccases: A review. Biotechnology Advances 24:500–513.
  55. Ruggiero, P., Sarkar, J.M. and Bollag. J.M. 1989. Detoxification of 2,4-dichlorophenol by a laccase immobilized on soil or clay. Soil Science 147:361–370.
  56. Savolainen, A., Zhang, Y., Rochefort, D., Holopainen, U., Erho, T., Virtanen, J. et al. 2011. Printing of polymer microcapsules for enzyme immobilization on paper substrate. Biomacromolecules 12:2008–15.
  57. Shuttleworth, K.L. and Bollag, J-M. 1986. Soluble and immobilized laccase as catalysts for the transformation of substituted phenols. Enzyme and Microbial Technology 8:171–177.
  58. Singh, G., Bhalla, A., Capalash, N. and Sharma, P. 2010. Characterization of immobilized laccase from γ-proteobacterium JB: Approach towards the development of biosensor for the detection of phenolic compounds. Indian Journal of Science and Technology 3:48-53.
  59. Spinelli, D., Fatarella, E., Di Michele, A., Pogni, R. 2013. Immobilization of fungal (Trametes versicolor) laccase onto Amberlite IR-120 H beads: optimization and characterization. Process Biochemistry 48:218–23.
  60. Tarafdar, J.C. and Chhonkar, P.K. 1982. Urease Clay Interactions: I – adsorption of urease on clays saturated with different cations. Indian Society of Soil Science 30: 27–32.
  61. Tortolini, C., Rea, S., Carota, E., Cannistraro, S. and Mazzei, F. 2012. Influence of the immobilization procedures on the electroanalytical performances of Trametes versicolor laccase based bioelectrode. Microchemical Journal 100:8–13.
  62. Unal, A. and Kolankaya, N. 2013. Determination of Optimum Immobilization Conditions of Trametes versicolorLaccase with Sodium Alginate Beads. IUFS Journal of Biology 72:15-21.
  63. Unal, Y.D. and Pazarlioglu, N.K. 2011. Production and gelatin entrapment of laccase from Trametes versicolor and its application to quantitative determination of phenolic contents  of commercial fruit juices. Food Biotechnology 25:351–68.
  64. Virtanen, H., Orelma, H., Erho, T. and Smolander, M. 2012. Development  of  printable  bioactive paper  containing  laccase. Process  Biochemistry 47:1496–502.
  65. Wang, F., Guo, C. and Liu, C.Z. 2013. Immobilization of Trametes versicolor cultures for improving laccase production in bubble column reactor intensified by sonication. Journal of  Industrial Microbiology and Biotechnology 40:141–50.
  66. Wang, Q., Peng, L., Li, G., Zhang, P., Li, D., Huang, F. and Wei, Q. 2013. Activity of Laccase Immobilized on TiO2-Montmorillonite Complexes. International Journal of Molecular Sciences 14:12520-12532.
  67. Wang, Q., Peng, L., Li, G., Zhang, P., Li, D., Huang, F. and Wei, Q. 2013. Activity of Laccase Immobilized on TiO2-Montmorillonite Complexes. International Journal of  Molecular Sciences 14: 12520-12532.
  68. Weetall, H.H. 1974. Immobilized enzymes: analytical applications. Analytical Chemistry 46:602A-604A.
  69. Zhang, X., Zhang, S., Pan, B., Hua, M. and Zhao, X. 2012. Simple fabrication of  polymer-based Trametes versicolor laccase for decolorization of malachite green. Bioresource Technology 115:16–20.
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