Fabrication of Rhizomucormiehei lipase reinforced nanobioconjugates as biocatalysts for a statistically optimized production of eugenol benzoate
Abstract
The chemical synthesis ofeugenol benzoate is associated with numerous environmentally unfavorable practices viz. the use toxic chemicals, tedious separation process and liberation of harmful by-products. On this standpoint, an alternative approach utilizing Rhizomucormieheilipase (RML) immobilized onto activated chitosan-multiwalled carbon nanotubes (RML/CS/MWCNTs) is suggested. The properties of the biocatalyst were characterized using Fourier-Transform Infrared Spectroscopy (FTIR), Field Emission Scanning Electron Microscopy (FESEM)and thermogravimetric analysis (TGA). Response surface methodology employing central composite design (CCD) based on four relevant parameters (incubation time, temperature, substrate molar ratio, and enzyme loading) was used to optimize the experimental conditions for the enzymatic synthesis to produce eugenol benzoate. The study found the high conversion of eugenol benzoate is greatly affected by temperature and incubation time. The highest yield of eugenol benzoate was 56.13 %, under optimized conditions of 60 °C, incubation time of 6 hr, enzyme loading of 150 IU and molar ratio of eugenol/benzoic acid of 4:1. The findings suggest that the RML/CS/MWCNTs biocatalyst developed here is a promising alternative to overcome shortcomings associated with the chemically produced esters.
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Abdul Rahman, M.B., Chaibakhsh, N., Basri, M., Rahman, R.N.Z.A., Salleh, A.B., (2008).Modelling and optimization of lipase-catalyzed synthesis of dilauryladipate ester by response surface methodology. Journal of Chemical Technology and Biotechnology. 83, 1534-1540.
Al-Khatib, Ma AnFahmi Rashid Alam, Md. Zahangir and Mohammed, Rasha (2012). Statistical modellingoptimisation of cellulase enzyme immobilisation on functionalised multi-walled carbon nanotubes for empty fruit bunches degradation. Australian Journal of Basic and Applied Sciences, 6, 30-38.
Campos Carneiro, L.A.B., Costa-Silva, T.A., Fernandes Souza, C.R., Bachmann, L., Oliveira, W.P., and Said, S., (2014). Immobilization of lipases produced by the endophyticfungus Cercosporakikuchii on chitosan microparticles. Brazillian Archives of Biology and Technology. 57(4), 578-586.
Cesar, M, Jose, M.P., Gloria, F.L., Jose, M.G., and Roberto F.L., (2007).Improvement of enzyme activity, stability and selectivity via immobilization techniques.Enzyme and Microbial Technology. 40, 1451–1463.
Chaibakhsh, N., Basri, M., Hani, M.A., Abdul Rahman, M.B., and Rezayee, M., (2012).Optimization of enzymatic synthesis of eugenol ester using statistical approaches.Biocatalysis and Agricultural Biotechnology. 1, 226-231.
Chaibakhsh, N., Basri, M., Hani, M.A., Abdul Rahman, M.B., and Rezayee, M., (2012).Optimization of enzymatic synthesis of eugenol ester using statistical approaches.Biocatalysis and Agricultural Biotechnology. 1, 226-231.
Charpe, T.W and Rathod, V.K., (2011). Biodiesel production using waste frying oil.Waste Management. 31, 85–90.
Collins, S.E., Lassalle, V., and Ferreira, M.L., (2011).FTIR-ATR characterization of free Rhizomucormeihei lipase (RML), Lipozyme RM IM and chitosan-immobilized RML. Journal of Molecular Catalysis B: Enzymatic. 72(3–4), 220–228.
Diaconu, M., Litescu, S.C., and Radu, G.L., (2010).Laccase–MWCNT–chitosan biosensor—A new tool for total polyphenolic content evaluation from in vitro cultivated plants. Sensors and Actuators B. 145, 800–806.
Hedge, K. and Veeranki, V. D., (2014). Studies on immobilization of cutinases from Thermobifidafusca on gluteraldehyde activated chitosan beads. British Biotechnology Journal. 4(10), 1049-1063.
Horchani, H., Ben Salem, N., Zarai, Z., Sayari, A., Gargouri, Y., and Chaâbouni, M., (2010). Enzymatic synthesis of eugenol benzoate by immobilized Staphylococcus aureus lipase: Optimization using response surface methodology and determination of antioxidant activity. Bioresource Technology. 101, 2809-2817.
Kroustalli, A., Zisimopoulou, A.E., Koch, S., Rongen, L., Deligianni, D., Diamantouros, S., Athanassiou, G., Kokozidou, M., Mavrilas, D., and Jockenhoevel, S., (2013). Carbon nanotubes reinforced chitosan films: mechanical properties and cell response of a novel biomaterial for cardiovascular tissue engineering. Journal of Materials Science Materials in Medicine. 24(12), 2889-2896.
Lau, S.C., Lim, H.N., Basri, M., FardMasoumi, H.R., Ahmad Tajudin, A., Huang, N.M., Andou, Y. (2014).Enhanced Biocatalytic Esterification with Lipase-Immobilized Chitosan/Graphene Oxide Beads.PLoS ONE, 9(8), e104695. doi:10.1371/journal.pone.0104695.
Mohamad, N.R., Buang, N.A., Mahat, N.A., Lok, Y.Y., Huyop, F., Aboul-Enein, H.Y., and Abdul Wahab, R., (2015). A facile enzymatic synthesis of geranyl propionate by physically adsorbed Candida rugosa lipase onto multi-walled carbon nanotubes. Enzyme and Microbial Technology. 72, 49–55.
Mubarak, N.M., Wonga, J.R., Tana, K.W., Sahuc, J.N., Abdullah, E.C., Jayakumar, N.S., and Ganesan, P., (2014). Immobilization of cellulase enzyme on functionalized multiwall carbon nanotubes. Journal of Molecular Catalysis B: Enzymatic. 107, 124-131.
Radzi, S.M., Mustafa, W.A.F., Othman, S.S., and Noor, H.M., (2011). Green synthesis of butyl acetate: A pineapple flavor via lipase catalyzed reaction. World Academy of Science, English, and Technology. 59, 677-680.
Raghavendra, T., Basak, A., Manocha, L.M., Shah, A.R., and Madamwara, D., (2013). Robust nanobioconjugates of Candida antarctica lipase B – Multiwalled carbon nanotubes: Characterization and application for multiple usages in non-aqueous biocatalysis. Bioresource Technology. 140, 103–110.
Skoronski, E., Padoin, N., Soares, C., and Furigo, Jr.A., (2014). Stability of immobillizedRhizomucormiehei lipase for the synthesis of pentyloctanoate in a continuous packed bed bioreactor.Brazilian Journal of Chemical Engineering. 31(3), 633-641.
Solanki, P.R., Kaushik, A., Ansari, A.A., Tiwari, A., and Malhotra, B.D., (2009). Multi-walled carbon nanotubes/sol–gel-derived silica/chitosan nanobiocomposite for total cholesterol sensor. Sensors and Actuators B: Chemical. 137, 727-735.
Spahn, C. and Minteer, S.D., (2008).Enzyme Immobilization in Biotechnology.Recent Patents on Engineering. 2, 195-200.
Verissimo, L.A.A., Soares, W.C.L., Mol, P.C.G., Minim, V.P.R., da Silva, M.C.H., and Minim, L.A., (2015). Optimization of flavor ester synthesis catalysed by Aspergillusniger lipase. African Journal of Microbiology Research. 9(13), 922-928.
Wahab, R., Abdul Rahman, M.B., Chaibakhsh, N., Leow, T.C., Basri, M., Abdul Rahman, R.N.Z., and Salleh, A.B., (2014).Enzymatic production of a solvent-free menthyl butyrate via response surface methodology catalyzed by a novel thermostable lipase from Geobacilluszalihae.Biotechnology & Biotechnological Equipment. http://dx.doi.org/10.1080/13102818.2014.978220.
Yudianti, R., Onggo, H., Sudirman, Saito, Y., Iwata, T., and Azuma, J., (2011). Analysis of functional group sited on multi-wall carbon nanotube surface. The Open Materials Science Journal. 5, 242-247.
Zou, B, Hu, Y, Yu, D., (2010). Immobilization of porcine pancreatic lipase onto ionic liquid modified mesoporous silica SBA-15.Biochemical Engineering Journal. 53(1), 150–153.
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