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References [1]. R.P. Pogorilyi, I.V. Melnyk, Y.L. Zub, G.A. Seisenbaeva, V.G. Kessler, Enzyme immobilization on a nanoadsorbent for improved stability against heavy metal poisoning, Colloids Surf. B 144 (2016) 135-142. [2]. G. Pozniak, B. Krajewska, W. Trochimczuk, Urease immobilized on modified polysulphone membrane: Preparation and properties, Biomaterials 16 (1995) 129-134. [3]. A.K. De Brito, C.S. Nordi, L. Caseli, Algal polysaccharides as matrices for the immobilization of urease in lipid ultrathin films studied with tensiometry and vibrational spectroscopy


In the present study, rice husk ash, which is a renewable and abundant material, was utilized as a carrier for lipase immobilization for the first time. Poly (ε-caprolactone) synthesis was successfully achieved by the new enzymatic catalyst: Candida antarctica lipase B immobilized onto surface-modified rice husk ashes by covalent binding. It was aimed to obtain optimum polymerization conditions at which highest molecular weight was reached and characterize the polymer produced. Moreover, thermal stability and effectiveness of the new biocatalyst in non-aqueous media were also shown with successful polymerization reactions. In addition, by using the new enzyme preparation, ε-caprolactone was able to be polymerized even at 30°C, which was promising for an energy saving process. Consequently, this work provides a new alternative route for poly (ε-caprolactone) synthesis.


The efficiency of enzymatic depolymerization in a membrane reactor was investigated. The model analysis was performed on bovine serum albumin hydrolysis reaction led by three different enzymes, for which kinetic equations have different forms. Comparing to a classic reactor, the reaction yield turns out to be distinctly higher for all types of kinetics. The effect arises from increasing (thanks to the proper selectivity of the applied membrane) the concentration of reagents in the reaction volume. The investigations indicated the importance of membrane selectivity election, residence time and at non-competitive inhibition the substrate (biopolymer) concentration in feed stream. Presented analysis is helpful in these parameters choice for enzymatic hydrolysis of different biopolymers.


Permeabilization is one of the effective tools, used to increase the accessibility of intracellular enzymes. Immobilization is one of the best approaches to reuse the enzyme. Present investigation use both techniques to obtain a biocatalyst with high catalase activity. At the beginning the isopropyl alcohol was used to permeabilize cells of baker’s yeast in order to maximize the catalase activity within the treated cells. Afterwards the permeabilized cells were immobilized in calcium alginate beads and this biocatalyst was used for the degradation of hydrogen peroxide to oxygen and water. The optimal sodium alginate concentration and cell mass concentration for immobilization process were determined. The temperature and pH for maximum decomposition of hydrogen peroxide were assigned and are 20°C and 7 respectively. Prepared biocatalyst allowed 3.35-times faster decomposition as compared to alginate beads with non permeabilized cells. The immobilized biocatalyst lost ca. 30% activity after ten cycles of repeated use in batch operations. Each cycles duration was 10 minutes. Permeabilization and subsequent immobilization of the yeast cells allowed them to be transformed into biocatalysts with an enhanced catalase activity, which can be successfully used to decompose hydrogen peroxide.

. (2010). Graphene Oxide as a Matrix for Enzyme Immobilization. Langmuir 26(9), 6083–6085. DOI: 10.1021/la904014z. 7. Bolibok, P., Wisniewski, M., Roszek, K. & Terzyk, A.P. (2017). Controlling enzymatic activity by immobilization on graphene oxide, Sci. Nat . 104: 36. DOI: 10.1007/s00114-017-1459-3. 8. Kishore, D., Talat, M., Srivastava, O. & Kayastha, A. (2012). Immobilization of β-Galactosidase onto Functionalized Graphene Nano-sheets Using Response Surface Methodology and Its Analytical Applications, Plos One 7(7):e40708. DOI: 10.1371/journal.pone.0040708. 9

Nano, 4 (2010), 4324. [8] NGUYEN S.T., NGUYEN H.T., RINALDI A., NGUYEN N.P.V., FAN Z., DUONG H.M., Colloid. Surface. A, 414 (2012), 352. [9] COSNIER S., LE GOFF A., HOLZINGER M., Electrochem. Commun., 38 (2014), 19. [10] BILEWICZ R., OPALLO M., Biocathodes for dioxygen reduction in biofuel cells, in: WIECKOWSKI A., NORSKOV J.K. (Eds.), Fuel Cell Science:Theory, Fundamentals and Biocatalysis, John Wiley & Sons, Inc, Hoboken, New Jersey, 2010, p. 169. [11] MOEHLENBROCK M.J., MINTEER S.D., Introduction to the Field of Enzyme Immobilization and Stabilization, in: Minteer

Prospects, Stud Surf Sci Catal (Eds: J. Cejka, H. van Bekkum) 91. 5. Hartmann, M. (2005). Adsorption of vitamin E on mesoporous carbon molecular sieves. Chem. Mater. 17, 829–833. DOI: 10.1021/cm048564f. 6. Hartmann, M. & Jung, D. (2010). Biocatalysis with enzymes immobilized on mesoporous hosts: the status quo and future trends. J. Mater. Chem. 20, 844. DOI: 10.1039/B907869J. 7. Mumin, M.A., Khan, M.M.R., Akhter, K.F. & Uddin, M.J. (2007). Potentiality of open burnt clay as an adsorbent for the removal of Congo red from aqueous solution. Int. J. Environ. Sci. Tech. 4 (4

hematological parameters of blood in horses. Med. Weter., 67: 418–421. Bis-Wencel H., Lutnicki K., Rowicka A.Z., Nowakowicz-Dębek B., Bryl M. (2012). Effort of varying intensity as a factor influencing the variability of selected biochemical blood parameters of jumping horses. Bull. Vet. Inst. Pulawy, 56: 225–229. Bosco R., Leeuwenburgh S.C.G., Jansen J.A.,vanden Beucken J.J.J.P. (2014). Configurational effects of collagen/ALP coatings on enzyme immobilization and surface mineralization. Appl. Surf. Sci., 311: 292–299. Brzóska F., Strzetelski J.A., Borowiec F., Jamroz D

LITERATURE CITED 1. Ansari, S.A. & Husain, Q. (2012). Potential applications of enzymes immobilized on/in nano materials: A review. Biotechnol. Adv. 30(3), 512–523. DOI: 10.1016/j.biotechadv.2011.09.005. 2. Chibber, S., Ansari, S.A. & Satar, R. (2013). New vision to CuO, ZnO, and TiO 2 nanoparticles: their outcome and effects. J. Nan. Res. 15(4), 1–13. DOI: 10.1007/s11051-013-1492-x. 3. Rao, J.P. & Geckeler, K.E. (2011). Polymer nanoparticles: Preparation techniques and size-control parameters. Prog. Polym. Sci. 36(7), 887–913. DOI: 10.1016/j.progpolymsci.2011

, in Roadmap to Sustainable Textiles and Clothing. In S.S Muthu (Eds.), Eco-friendly Raw Materials, Technologies and Processing Methods, 217-219. Springer, ISBN 978-981-287-065-0. DOI: 10.1007/978-981-287-065-0. 9. Sarmiento, F., Peralta, R. & Blamey J.M. (2015). Cold and hot extremozymes: industrial relevance and current trends. Front. Bioeng. Biotechnol. 3, 1-15. DOI: 10.3389/fbioe.2015.00148. 10. Homaei, A.A., Sariri, R., Vianello, F. & Stevanato, R. (2013). Enzyme immobilization: an update. J. Chem. Biol. 6(4), 185-205. DOI: 10.1007/s12154-013-0102-9. 11. Dogac