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Research Article

Stabilization and optimization of purified diamine oxidase by immobilization onto activated PVC membrane

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References

  • Anwar, M. Z., D. J. Kim, A. Kumar, S. K. Patel, S. Otari, P. Mardina, J. H. Jeong, J. H. Sohn, J. H. Kim, J. T. Park, et al. 2017. SnO2 hollow nanotubes: A novel and efficient support matrix for enzyme immobilization. Sci. Rep. 7 (1):15333. doi:10.1038/s41598-017-15550-y.
  • Biro, E., D. Budugan, A. Todea, F. Peter, S. Klebert, and T. Feczko. 2016. Recyclable solid-phase biocatalyst with improved stability by sol–gel entrapment of β-d-galactosidase. J. Mol. Catal. B, Enzym. 123:81–90.
  • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1–2):248–254. doi:10.1016/0003-2697(76)90527-3.
  • Cacicedo, M. L., R. M. Manzo, S. Municoy, H. L. Bonazza, G. A. Islan, M. Desimone, M. Bellino, E. J. Mammarella, and G. R. Castro. 2019. Chapter 7 - Immobilized enzymes and their applications. In Biomass, biofuels, biochemicals: advances in enzyme technology, ed. R. S. Singh, R. R. Singhania, A. Pandey, and C. Larroche, 169–200. Amsterdam, Netherlands: Elsevier.
  • Carelli, D., D. Centonze, C. Palermo, M. Quinto, and T. Rotunno. 2007. An interference free amperometric biosensor for the detection of biogenic amines in food products. Biosens. Bioelectron. 23 (5):640–647. doi:10.1016/j.bios.2007.07.008.
  • Cui, C., N. Guan, C. Xing, B. Chen, and T. Tan. 2016. Immobilization of Yarrowia lipolytica lipase Ylip2 for the biocatalytic synthesis of phytosterol ester in a water activity controlled reactor. Colloids Surf. B. 146:490–497. doi:10.1016/j.colsurfb.2016.05.083.
  • Deveci, N., and Y. A. Güvenilir. 1995. Purification and Properties of the diamine oxidase of pea seedlings. Appl. Biochem. Biotechnol. 53 (1):83. doi:10.1007/BF02783484.
  • Dwevedi, A. 2016. Basics of enzyme immobilization. In Enzyme immobilization, ed. A. Dwevedi, 21–44. Cham: Springer.
  • Eldin, M. M., M. R. El‐Aassar, A. E. Zatahry, and M. M. Al‐Sabah. 2013. Covalent immobilization of β‐galactosidase onto amino‐functionalized polyvinyl chloride microspheres: enzyme immobilization and characterization. Adv. Polym. Technol. 1 (33):21379-21390.
  • Elmore, B. O., J. A. Bollinger, and D. M. Dooley. 2002. Human kidney diamine oxidase: Heterologous expression, purification, and characterization. J. Biol. Inorg. Chem. 7 (6):565–579. doi:10.1007/s00775-001-0331-1.
  • Fatarella, E., D. Spinelli, M. Ruzzante, and R. Pogni. 2014. Nylon 6 film and nanofiber carriers: Preparation and laccase immobilization performance. J. Mol. Catal. B, Enzym. 102:41–47. doi:10.1016/j.molcatb.2014.01.012.
  • Floris, G., A. Giartosio, and A. Rinaldi. 1983. Diamine oxidase from Lens esculenta seedlings: Purification and properties. Phytochemistry 22 (9):1871–1874. doi:10.1016/0031-9422(83)80004-1.
  • Gomes, F. M., E. B. Pereira, and H. F. de Castro. 2004. Immobilization of lipase on chitin and its use in nonconventional biocatalysis. Biomacromolecules 5 (1):17–23. doi:10.1021/bm0342077.
  • Hsieh, H. J., P. C. Liu, and W. J. Liao. 2000. Immobilization of invertase via carbohydrate moiety on chitosan to enhance its thermal stability. Biotechnol. Lett. 22 (18):1459–1464. doi:10.1023/A:1005602812037.
  • Ispas, C., I. Sokolov, and S. Andreescu. 2009. Enzyme-functionalized mesoporous silica for bioanalytical applications. Anal. Bioanal. Chem. 393 (2):543–554.
  • Karim, A., A. W. Wahab, I. Raya, H. Natsir, and A. R. Arif. 2018. Utilization of diamine oxidase enzyme from mung bean sprouts (Vignaradiata L) for histamine biosensors. Journal of Physics: Conference Series 979:012014. IOP Publishing Ltd.
  • Kaur, K., and P. Kaushal. 2019. Chapter 10 - enzymes as analytical tools for the assessment of food quality and food safety. In Biomass, biofuels, biochemicals: advances in enzyme technology, ed. R. S. Singh, R. R. Singhania, A. Pandey, and C. Larroche, 273–292. Amsterdam, Netherlands: Elsevier.
  • Krajewska, B., M. Leszko, and W. Zaborska. 1990. Urease immobilized on chitosan membrane: Preparation and properties. J. Chem. Technol. Biotechnol. 48 (3):337–350. doi:10.1002/jctb.280480309.
  • Kumar, S., A. Dwevedi, and A. M. Kayastha. 2009. Immobilization of soybean (Glycine max) urease on alginate and chitosan beads showing improved stability: Analytical applications. J. Mol. Catal. B, Enzym. 58 (1–4):138–145. doi:10.1016/j.molcatb.2008.12.006.
  • Li, Y., X. Y. Wang, X. P. Jiang, J. J. Ye, Y. W. Zhang, and X. Y. Zhang. 2015. Fabrication of graphene oxide decorated with Fe3O4@SiO2 for immobilization of cellulase. J. Nanoparticle Res. 17 (1):8. doi:10.1007/s11051-014-2826-z.
  • Marques, M. E., A. A. Mansur, and H. S. Mansur. 2013. Chemical functionalization of surfaces for building three-dimensional engineered biosensors. Appl. Surf. Sci. 275:347–360. doi:10.1016/j.apsusc.2012.12.099.
  • Mateo, C., J. M. Palomo, G. Fernandez-Lorente, J. M. Guisan, and R. Fernandez-Lafuente. 2007. Improvement of enzyme activity, stability and selectivity via immobilization techniques. Enzyme Microb. Technol. 40 (6):1451–1463. doi:10.1016/j.enzmictec.2007.01.018.
  • Mehdi, W. A., A. A. Mehde, M. Ozacar, and Z. Ozacar. 2018. Characterization and immobilization of protease and lipase on chitin-starch material as a novel matrix. Int. J. Biol. Macromol. 117:947–958. doi:10.1016/j.ijbiomac.2018.04.195.
  • Mehta, J., N. Bhardwaj, S. K. Bhardwaj, K. H. Kim, and A. Deep. 2016. Recent advances in enzyme immobilization techniques: Metal-organic frameworks as novel substrates. Coord. Chem. Rev. 322:30–40. doi:10.1016/j.ccr.2016.05.007.
  • Melo, A. F., E. F. Mauricio, A. M. Salgado, F. L. Pessoa, M. C. Damaso, and S. Couri. 2011. Assessment of catalytic properties in aqueous and media of Aspergillus niger lipase immobilized on supports vitreous. Chem. Eng. Trans. 24:973–978.
  • Milani, M. M., A. S. Lotfi, A. Mohsenifar, P. Mikaili, N. Kamelipour, and J. Dehghan. 2015. Enhancing organophosphorus hydrolase stability by immobilization on chitosan beads containing glutaraldehyde. Res. J. Environ. Toxicol. 9 (1):34–44. doi:10.3923/rjet.2015.34.44.
  • Mizuguchi, H., I. Imamura, M. Takemura, and H. Fukui. 1994. Purification and Characteristics of Diamine Oxidase from rat small intestine. J. Biochem. 116 (3):631–635. doi:10.1093/oxfordjournals.jbchem.a124572.
  • Moelans, D., P. Cool, J. Baeyens, and E. F. Vansant. 2005. Using mesoporous silica materials to immobilize biocatalysis-enzymes. Catal. Commun. 6 (4):307–311. doi:10.1016/j.catcom.2005.02.005.
  • Mohamad, N. R., N. H. Marzuki, N. A. Buang, F. Huyop, and R. A. Wahab. 2015. An overview of technologies for immobilization of enzymes and surface analysis techniques for immobilized enzymes. Biotechnol. Biotechnol. Equip. 29 (2):205–220. doi:10.1080/13102818.2015.1008192.
  • Mohamed, S. A., J. A. Khan, O. A. Al-Bar, and R. M. El-Shishtawy. 2014. Immobilization of trichoderma harzianum α-Amylase on treated wool: Optimization and characterization. Molecules 19 (6):8027–8038. doi:10.3390/molecules19068027.
  • Mohamed, S. A., M. H. Al-Harbi, Y. Q. Almulaiky, I. H. Ibrahim, and R. M. El-Shishtawy. 2017. Immobilization of horseradish peroxidase on Fe3O4 magnetic nanoparticles. Electron. J. Biotechnol. 27:84–90. doi:10.1016/j.ejbt.2017.03.010.
  • Mohamed, S. A., S. S. Al-Ghamdia, and R. M. El-Shishtawy. 2016. Immobilization of horseradish peroxidase on amidoximated acrylicpolymer activated by cyanuric chloride. Int. J. Biol. Macromol. 91:663–670. doi:10.1016/j.ijbiomac.2016.06.002.
  • Muresan, L., R. R. Valera, I. Frebort, I. C. Popescu, E. Csoregi, and M. Nistor. 2008. Amine oxidase amperometric biosensor coupled to liquid chromatography for biogenic amines determination. Microchim. Acta. 163 (3–4):219–225. doi:10.1007/s00604-008-0033-2.
  • Naik, B. I., R. G. Goswami, and S. K. Srivastava. 1981. A rapid and sensitive colorimetric assay of amine oxidase. Anal. Biochem. 111 (1):146–148. doi:10.1016/0003-2697(81)90242-6.
  • Nawaz, M. A., A. Karim, A. Aman, R. Marchetti, S. A. Qader, and A. Molinaro. 2015. Continuous degradation of maltose: Improvement in stability and catalytic properties of maltase (α-glucosidase) through immobilization using agar-agar gel as a support. Bioproc. Biosyst. Eng. 38 (4):631–638. doi:10.1007/s00449-014-1302-6.
  • Podrepšek, G. H., M. Primožič, Ž. Knez, and M. Habulin. 2012. Immobilization of cellulase for industrial production. Chem. Eng. 27:235–240.
  • Pundir, C. S., N. S. Chauhan, and M. Bhambi. 2008. Activation of polyvinyl chloride sheet surface for covalent immobilization of oxalate oxidase and its evaluation as inert support in urinary oxalate determination. Anal. Biochem. 374 (2):272–277. doi:10.1016/j.ab.2007.11.008.
  • Rehman, H. U., A. Aman, M. A. Nawaz, and S. A. Qader. 2015. Characterization of pectin degrading polygalacturonase produced by Bacillus licheniformis KIBGE-IB21. Food Hydrocoll 43:819–824. doi:10.1016/j.foodhyd.2014.08.018.
  • Rinaldi, A., G. Floris, and A. Finazzi‐agro. 1982. Purification and properties of diamine oxidase from Euphorbia latex. Eur. J. Biochem. 127 (2):417–422. doi:10.1111/j.1432-1033.1982.tb06888.x.
  • Rueda, N., C. S. Dos Santos, M. D. Rodriguez, T. L. Albuquerque, O. Barbosa, R. Torres, C. Ortiz, and R. Fernandez-Lafuente. 2016. Reversible immobilization of lipases on octyl- glutamic agarose beads: A mixed adsorption that reinforces enzyme immobilization. J. Mol. Catal. B, Enzym. 128:10–18. doi:10.1016/j.molcatb.2016.03.002.
  • Santos, J. C., O. Barbosa, C. Ortiz, A. Berenguer‐Murcia, R. C. Rodrigues, and R. Fernandez‐Lafuente. 2015. Importance of the support properties for immobilization or purification of enzymes. Chem. Cat. Chem. 7 (16):2413–2432.
  • Schwelberger, H. G., and E. Bodner. 1997. Purification and characterization of diamine oxidase from porcine kidney and intestine. Biochimic. Biophys. Acta. 1340 (1):152–164. doi:10.1016/S0167-4838(97)00039-3.
  • Sharifi, M., S. M. Robatjazi, M. Sadri, and J. M. Mosaabadi. 2018. Covalent immobilization of organophosphorus hydrolase enzyme on chemically modified cellulose microfibers: Statistical optimization and characterization. React. Funct. Polym. 124:162–170. doi:10.1016/j.reactfunctpolym.2018.01.019.
  • Sheldon, R. A. 2007. Enzyme immobilization: The quest for optimum performance. Adv. Synth. Catal. 349 (8–9):1289–1307. doi:10.1002/adsc.200700082.
  • Singh, K., and A. M. Kayastha. 2014. Optimal immobilization of α-amylase from wheat (Triticum aestivum) onto DEAE-cellulose using response surface methodology and its characterization. J. Mol. Catal. B, Enzym. 104:75–81. doi:10.1016/j.molcatb.2014.03.014.
  • Vaillant, F., A. Millan, P. Millan, M. Dornier, M. Decloux, and M. Reynes. 2000. Co-immobilized pectinlyase and endocellulase on chitin and nylon supports. Process Biochem 35 (9):989–996. doi:10.1016/S0032-9592(00)00131-X.
  • Verma, N., V. Hooda, A. Gahlaut, A. Gothwal, and V. Hooda. 2019. Enzymatic biosensors for the quantification of biogenic amines: A literature update. Crit. Rev. Biotechnol. 40 (1):1–14. doi:10.1080/07388551.2019.1680600.
  • Walt, D. R., and V. I. Agayn. 1994. The chemistry of enzyme and protein immobilization with glutaraldehyde. Trend Anal. Chem. 13 (10):425–430. doi:10.1016/0165-9936(94)85023-2.
  • Yanagisawa, H., E. Hirasawa, and Y. Suzuki. 1981. Purification and properties of diamine oxidase from pea epicotyls. Phytochemistry 20 (9):2105–2108. doi:10.1016/0031-9422(81)80094-5.

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