514
Views
9
CrossRef citations to date
0
Altmetric
Articles

Utilization of Catalytic Properties of the Encapsulated Lipase with Calix[4]arene-Adorned Sporopollenin

&
Pages 272-281 | Received 24 Apr 2016, Accepted 08 Jun 2016, Published online: 12 Dec 2016

References

  • Moreno, J. M., and J. V. Sinisterra. “Immobilization of Lipase from Candida Cylindracea on Inorganic Supports.” J. Mol. Catalysis B, Enzymatic 93 (1994): 357–69.
  • Matsumoto, M., N. Sumi, K. Ohmori, and K. Kondo. “Immobilization of Lipase in Microcapsules Prepared by Organic and Inorganic Materials.” Process Biochem. 33 (1998): 535–40.
  • Bódalo, A., J. Bastida, M. F. Máximo, M. C. Montiel, M. Gómez, and M. D. Murcia. “Production of Ricinoleic Acid Estolide with Free and Immobilized Lipase from Candida Rugosa.” Biochem. Eng. J. 39 (2008): 450–6.
  • Gotor-Fernández, V., R. Brieva, and V. Gotor. “Lipases: Useful Biocatalysts for the Preparation of Pharmaceuticals.” J. Mol. Catalysis B, Enzymatic 40 (2006): 111–20.
  • Koeller, K. M., and C. H. Wong. “Enzymes for Chemical Synthesis.” Nature 409 (2001): 232–40.
  • Ozyilmaz, E., and S. Sayin. “Preparation of New Calix[4]arene-Immobilized Biopolymers for Enhancing Catalytic Properties of Candida Rugosa Lipase by Sol–Gel Encapsulation.” App. Biochem. Biotechnol. 170 (2013): 1871–84.
  • Silva, J. A., G. P. Macedo, D. S. Rodrigues, R. L. C. Giordano, and L. R. B. Goncalves. “Immobilization of Candida Antarctica Lipase B by Covalent Attachment on Chitosan-based Hydrogels using Different Support Activation Strategies.” Biochem. Eng. J. 60 (2012): 16–24.
  • Sayin, S., E. Yilmaz, and M. Yilmaz. “Improvement of Catalytic Properties of Candida Rugosa Lipase by Sol–gel Encapsulation in the Presence of Magnetic calix[4]arene Nanoparticles.” Org. Biomol. Chem. 9 (2011): 4021–4.
  • Ozyilmaz, E., S. Sayin, M. Arslan, and M. Yilmaz. “Improving Catalytic Hydrolysis Reaction Efficiency of Sol–gel-Encapsulated Candida Rugosa Lipase with Magnetic Beta-Cyclodextrin Nanoparticles.” Colloids Surf. B, Biointerfaces 113 (2014): 182–9.
  • Ferreira-Dias, S., A. C. Correia, and F. O. Baptista. “Activity and Batch Operational Stability of Candida Rugosa Lipase Immobilized in Different Hydrophilic Polyurethane foams During Hydrolysis in a Biphasic Medium.” Bioprocess Eng. 21 (1999): 517–24.
  • Kartal, F., and A. Kilinc. “Immobilization of Pancreatic Lipase on Polyvinyl Alcohol by Cyanuric Chloride.” Preparative Biochem. Biotechnol. 36 (2006): 139–51.
  • Miller, C., H. Austin, L. Posorske, and J. Gonzlez. “Characteristics of an Immobilized Lipase for the Commercial Synthesis of Esters.” J. Am. Oil Chemists' Soc. 65 (1988): 927–31.
  • Siqueiraa, N. M., K. C. Garciaa, R. Bussamarab, F. S. Bothb, M. H. Vainsteinb, and R. M. D. Soares. “Poly (lactic acid)/Chitosan Fiber Mats: Investigation of Effects of the Support on Lipase Immobilization.” Int. J. Biol. Macromol. 72 (2015): 998–1004.
  • Brooks, J., and G. Shaw. “Identity of Sporopollenin with Older Kerogen and New Evidence for the Possible Biological Source of Chemicals in Sedimentary Rocks.” Nature 220 (1968): 678–9.
  • Vural, U. S., M. Ersoz, and M. Pehlivan. “Ligand Sorption Kinetics of Aromatic Amines on New Ligand-exchanger Sporopollenin in Cobalt Ion Form.” J. App. Polym. Sci. 58 (1995): 2423–8.
  • Tutar, H., E. Yilmaz, E. Pehlivan, and M. Yilmaz. “Immobilization of Candida Rugosa Lipase on Sporopollenin from Lycopodium Clavatum.” Int. J. Biol. Macromol. 45 (2009): 315–20.
  • Brooks, J., P. R. Grant, M. Muir, and P. Van Gijzel. in Sporopollenin, ed. G. Shaw (London: Academic Press, 1971), 305–48.
  • Yilmaz, E., M. Sezgin, and M. Yilmaz. “Enantioselective Hydrolysis of Rasemic Naproxen Methyl Ester with Sol–gel Encapsulated Lipase in the Presence of Sporopollenin.” J. Mol. Catalysis B, Enzymatic 62 (2010): 162–8.
  • Yilmaz, E. “Enantioselective Enzymatic Hydrolysis of Racemic Drugs by Encapsulation in Sol–gel Magnetic Sporopollenin.” Bioprocess Biosystems Eng. 35 (2012): 493–502.
  • Ciaccia, M., I. Tosi, R. Cacciapaglia, A. Casnati, L. Baldini, and S. D. Stefano. “One-shot Preparation of an Inherently Chiral Trifunctional Calix[4]arene from An Easily Available Cone-triformylcalix[4]arene.” Org. Biomol. Chem. 11 (2013): 3642–8.
  • Sayin, S., and M. Yilmaz. “The synthesis of New Calix[n]arene Quaternary Ammonium Salts and Investigation of their Catalytic Affinities for three Component Mannich-type Reactions in Water.” RSC Advances 4 (2014): 2219–25.
  • Memon, S., A. A. Bhatti, and N. Memon. “New Calix[4]arene appended Amberlite XAD-4 Resin with Versatile Perchlorate Removal Efficiency.” J. Chem. Eng. Data 58 (2013): 2819–27.
  • Cardona, F., G. Isoldi, F. Sansone, A. Casnati, and A. Goti. “Building Multivalent Iminosugar-based Ligands on Calixarene Cores Via Nitrone Cycloadditions.” J. Org. Chem. 77 (2012): 6980–8.
  • Holub, J., V. Eigner, L. Vrzal, H. Dvoøáková, and P. Lhoták. “Calix[4]arenes with Intramolecularly Bridged Meta Positions Prepared via Pd-catalysed Double C-H Activation.” Chem. Commun. 49 (2013): 2798–800.
  • Akkus, G. U., S. Memon, D. E. Gürka°, S. Aslan, and M. Yilmaz. “The Synthesis and Metal Cation Extraction Studies of Novel Polymer-Bound Calix(Aza)Crowns.” Reactive Funct. Polym. 68 (2008): 125–32.
  • Ozyilmaz, E., and S. Sayin. “A Magnetically Separable Biocatalyst for Resolution of Racemic Naproxen Methyl Ester.” Bioprocess Biosyst. Eng. 36 (2013): 1803–06.
  • Pehlivan, E., M. Ersoz, M. Pehlivan, S. Yildiz, and H. Duncan. “The Effects of pH and Temperature on the Sorption of Zinc(II), Cadmium(II), and Aluminium(III) onto New Metal-Ligand Complexes of Sporopollenin.” J. Colloid Interface Sci. 170 (1995): 320–25.
  • Vidinha, P., V. Augusto, M. Almeida, I. Fonseca, A. Fidalgo, L. Ilharco, J. M. S. Cabral, and S. Barreiros. “Sol-gel Encapsulation: An Efficient and Versatile Immobilization Technique for Cutinase in Non-aqueous Media.” J. Biotechnol. 121 (2006): 23–33.
  • Reetz, M. T., P. Tielmann, W. Wisenhofer, W. Konen, and A. Zonta. “Second Generation Sol–gel Encapsulated Lipases: Robust Heterogeneous Biocatalysts.” Adv. Synth. Catalysis 345 (2003): 717–28.
  • Sayin, S., I. H. Gubbuk, and M. Yilmaz. “Preparation of Calix4arene-based Sporopollenin and Examination of Its Dichromate Sorption Ability.” J. Inclusion Phenom. Macrocyclic Chem. 75 (2013): 111–8.
  • Gutsche, C. D., and K. C. Nam. “Synthesis, Properties, and Metal Complexation of Aminocalixarenes.” J. Am. Chem. Soc. 110 (1988): 6153–62.
  • Collins, E. M., M. A. McKervey, E. Madigan, M. B. Moran, M. Owens, G. Ferguson, and S. J. Harris. “Chemically Modified Calix[4]arenes-regioselective Synthesis of 1,3-(distal) Derivatives and Related Compounds-X-ray Crystal Structure of a Diphenol-dinitrile.” Perkin Trans 1 12 (1991): 3137–42.
  • Alekseeva, E. A., V. A. Bacherikov, and A. I. Gren. “Synthesis of p-tert-butylcalix[4]arene Derivatives Containing Amino Acid Residues.” Russ. J. Gen. Chem. 70 (2000): 490–2.
  • Bradford, M. M. “A Rapid and Sensitive Method for Quantitation of Microgram Quantities of Protein Utilizing Principle of Protein-dye Binding.” Anal. Biochem. 72 (1976): 248–54.
  • Chiou, S. H., and W. T. Wu. “Immobilization of Candida Rugosa Lipase on Chitosan with Activation of the Hydroxyl Groups.” Biomaterials 25 (2004): 197–204.
  • Bonnet, M., C. Leroux, Y. Chilliard, and P. Martin. “A Fluorescent Reverse Transcription-polymerase Chain Reaction Assay to Quantify the Lipoprotein Lipase Messenger RNA.” Mol. Cell. Probes 15 (2001): 187–94.
  • Sayin, S., E. Akoz, and M. Yilmaz. “Enhanced Catalysis and Enantioselective Resolution of Racemic Naproxen Methyl Ester by Lipase Encapsulated within Iron Oxide Nanoparticles Coated with Calix[8]arene Valeric Acid Complexes.” Org. Biomol. Chem. 12 (2014): 6634–42.
  • Chen, C. S., Y. Fujimoto, G. Girdaukas, and C. J. Sih. “Quantitative Analyses of Biochemical Kinetic Resolutions of Enantiomers.” J. Am. Chem. Soc. 104 (1982): 7294–9.
  • Giuliani, M., I. Morbioli, F. Sansone, and A. Casnati. “Moulding Calixarenes for Biomacromolecule Targeting.” Chem. Commun. 51 (2015): 14140–59.
  • Ozyilmaz, E., M. Bayrakci, and M. Yilmaz. “Improvement of Catalytic Activity of Candida rugosa Lipase in the Presence of calix[4]arene Bearing Iminodicarboxylic/phosphonic Acid Complexes Modified Iron Oxide Nanoparticles.” Bioorganic Chem. 65 (2016): 1–8.
  • Sahin, O., S. Erdemir, A. Uyanik, and M. Yilmaz. “Enantioselective Hydrolysis of (R/S)-naproxen Methyl Ester with Sol-gel Encapculated Lipase in Presence of Calixnarene Derivatives.” App. Catalysis A, Gen. 369 (2009): 36–41.
  • Yilmaz, E., M. Sezgin, and M. Yilmaz. “Immobilization of Candida Rugosa Lipase on Magnetic Sol-gel Composite Supports for Enzymatic Resolution (R,S)-naproxen Methyl Ester.” J. Mol. Catalysis B, Enzymatic 69 (2011): 35–41.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.