Effect of Glutaraldehyde Concentration on Catalytic Efficacy of Candida rugosa Lipase Immobilized onto Silica from Oil Palm Leaves

https://doi.org/10.22146/ijc.42177

Emmanuel Onoja(1), Roswanira Abdul Wahab(2*)

(1) Department of Science Laboratory Technology, The Federal Polytechnic, Kaura Namoda, P.M.B. 1012, Zamfara State, Nigeria
(2) Department of Chemistry, Faculty of Science, Universiti Teknologi Malaysia, 81310, UTM Johor Bahru, Johor, Malaysia
(*) Corresponding Author

Abstract


Till date, studies that investigated the effect of glutaraldehyde concentration on catalytic efficacy of biocatalyst developed with silica-derived from oil palm leaves (OPL) as support, are unknown. The study presents the preparation of a support consisting of silica extracted from OPL coated over magnetite (G/A/SiO2-M) for the immobilization of Candida rugosa lipase (CRL). Herein, the effect of glutaraldehyde concentration on the catalytic efficacy of immobilized CRL was assessed by the enzymatic production of butyl butyrate as a model. Fourier transform infrared (FTIR) spectra and immobilization parameters indicated that covalent bound CRL on functionalized OPL-derived silica-magnetite composite activated with 4% (v/v) glutaraldehyde solution (100 mM, pH 7.0) (CRL/G/A/SiO2-M) and pretreated in toluene, resulted in a protein loading and an immobilization yield of 68.3 mg/g and 74.3%, respectively. The resultant CRL/G/A/SiO2-M biocatalyst which specific activity was 61.9 U/g catalyzed the esterification production of 76.5% butyl butyrate in just 3 h, as confirmed by analyses of the purified ester using FTIR and 1H NMR spectroscopy. Hence, the finding envisages the promising use of G/A/SiO2-M support fabricated from discarded OPL as a carrier for immobilization and activation of CRL, in conjunction to being a good alternative source of renewable silica.

Keywords


glutaraldehyde; oil palm leaves; silica; support matrix; butyl butyrate

Full Text:

Full Text PDF


References

[1] Marzuki, N.H.C., Mahat, N.A., Huyop, F., Aboul-Enein, H.Y., and Wahab, R.A., 2015, Sustainable production of the emulsifier methyl oleate by Candida rugosa lipase nanoconjugates, Food Bioprod. Process., 96, 211–220.

[2] Elias, N., Chandren, S., Attan, N., Mahat, N.A., Razak, F.I.A., Jamalis, J., and Wahab, R.A., 2017, Structure and properties of oil palm-based nanocellulose reinforced chitosan nanocomposite for efficient synthesis of butyl butyrate, Carbohydr. Polym., 176, 281–292.

[3] Onoja, E., Chandren, S., Razak, F.I.A., and Wahab, R.A., 2018, Extraction of nanosilica from oil palm leaves and its application as support for lipase immobilization, J. Biotechnol., 283, 81–96.

[4] Onoja, E., Chandren, S., Razak, F.I.A., and Wahab, R.A., 2018, Enzymatic synthesis of butyl butyrate by Candida rugosa lipase supported on magnetized-nanosilica from oil palm leaves: Process optimization, kinetic and thermodynamic study, J. Taiwan Inst. Chem. Eng., 91, 105–118.

[5] Sheldon, R.A., and van Pelt, S., 2013, Enzyme immobilisation in biocatalysis: Why, what and how, Chem. Soc. Rev., 42 (15), 6223–6235.

[6] Lima, L.C.D., Peres, D.G.C., and Mendes, A.A., 2018, Kinetic and thermodynamic studies on the enzymatic synthesis of wax ester catalyzed by lipase immobilized on glutaraldehyde-activated rice husk particles, Bioprocess. Biosyst. Eng., 41 (7), 991–1002.

[7] Bonazza, H.L., Manzo, R.M., dos Santos, J.C.S., and Mammarella, E.J., 2018, Operational and thermal stability analysis of Thermomyces lanuginosus lipase covalently immobilized onto modified chitosan supports, Appl. Biochem. Biotechnol., 184 (1), 182–196.

[8] Cao, L.P., Wang, J.J., Zhou, T., Ruan, R., and Liu, Y.Y., 2018, Bamboo (Phyllostachys pubescens) as a natural support for neutral protease immobilization, Appl. Biochem. Biotechnol., 186 (1), 109–121.

[9] Onoja, E., Attan, N., Chandren, S., Razak, F.I.A., Keyon, A.S.A., Mahat, N.A., and Wahab, R.A., 2017, Insights into the physicochemical properties of the Malaysian oil palm leaves as an alternative source of industrial materials and bioenergy, Malays. J. Fundam. Appl. Sci., 13 (4), 623–631.

[10] Hartmann, M., and Kostrov, X., 2013, Immobilization of enzymes on porous silicas – benefits and challenges, Chem. Soc. Rev., 42 (15), 6277–6289.

[11] Zhou, Z., and Hartmann, M., 2012, Recent progress in biocatalysis with enzymes immobilized on mesoporous hosts, Top. Catal., 55 (16-18), 1081–1100.

[12] Onoja, E., Chandren, S., Razak, F.I.A., Mahat, N.A., and Wahab, R.A., 2019, Oil palm (Elaeis guineensis) biomass in Malaysia: The present and future prospects, Waste Biomass Valorization, 10 (8), 2099–2117.

[13] 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 Microb. Technol., 40 (6), 1451–1463.

[14] Rodrigues, R.C., Ortiz, C., Berenguer-Murcia, Á., Torres, R., and Fernández-Lafuente, R., 2013, Modifying enzyme activity and selectivity by immobilization, Chem. Soc. Rev., 42 (15), 6290–6307.

[15] Manoel, E.A., dos Santos. J.C.S., Freire, D.M.G., Rueda, N., and Fernandez-Lafuente, R., 2015, Immobilization of lipases on hydrophobic supports involves the open form of the enzyme, Enzyme Microb. Technol., 71, 53–57.

[16] Sassolas, A., Blum, L.J., and Leca-Bouvier, B.D., 2012, Immobilization strategies to develop enzymatic biosensors, Biotechnol. Adv., 30 (3), 489–511.

[17] Rahman, I.N.A., Attan, N., Mahat, N.A., Jamalis, J., Keyon, A.S.A., and Kurniawan, C., 2018, Statistical optimization and operational stability of Rhizomucor miehei lipase supported on magnetic chitosan/chitin nanoparticles for synthesis of pentyl valerate, Int. J. Biol. Macromol., 115, 680–695.

[18] Mohamad, N.R., Huyop, F., Aboul-Enein, H.Y., Mahat, N.A., and Wahab, R.A., 2015, Response surface methodological approach for optimizing production of geranyl propionate catalysed by carbon nanotubes nanobioconjugates, Biotechnol. Biotechnol. Equip., 29 (4), 732–739.

[19] Liu, Y., and Hua, X., 2014, Production of biodiesel using a nanoscaled immobilized lipase as the catalyst, Catal. Lett., 144 (2), 248–251.

[20] Laveille, P., Falcimaigne, A., Chamouleau, F., Renard, G., Drone, J., Fajula, F., Pulvin, S., Thomas, D., Bailly, C., and Galarneau, A., 2010, Hemoglobin immobilized on mesoporous silica as effective material for the removal of polycyclic aromatic hydrocarbons pollutants from water, New J. Chem., 34 (10), 2153–2165.

[21] Spinelli, D., Coppi, S., Basosi, R., and Pogni, R., 2014, Biosynthesis of ethyl butyrate with immobilized Candida rugosa lipase onto modified Eupergit®C, Biocatalysis, 1 (1), 1–12.

[22] Barbosa, O., Ortiz, C., Berenguer-Murcia, A., Torres, R., Rodrigues, R.C., and Fernandez-Lafuente, R., 2014, Glutaraldehyde in bio-catalysts design: A useful crosslinker and a versatile tool in enzyme immobilization, RSC Adv., 4 (4), 1583–1600.

[23] Gunda, N.S.K., Singh, M., Norman, L., Kaur, K., and Mitra, S.K., 2014, Optimization and characterization of biomolecule immobilization on silicon substrates using (3-aminopropyl) triethoxysilane (APTES) and glutaraldehyde linker, Appl. Surf. Sci., 305, 522–530.

[24] Migneault, I., Dartiguenave, C., Bertrand, M.J., and Waldron, K.C., 2004, Glutaraldehyde: Behavior in aqueous solution, reaction with proteins, and application to enzyme crosslinking, Biotechniques, 37 (5), 790–802.

[25] Elias, N., Chandren, S., Razak, F.I.A., Jamalis, J., Widodo, N., and Wahab, R.A., 2018, Characterization, optimization and stability studies on Candida rugosa lipase supported on nanocellulose reinforced chitosan prepared from oil palm biomass, Int. J. Biol. Macromol., 114, 306–316.

[26] Johan, E., Ogami, K., Matsue, N., Itagaki, Y., and Aono, H., 2016, Fabrication of high purity silica from rice husk and its conversion into ZSM-5, ARPN J. Eng. Appl. Sci., 11 (6), 4006–4010.

[27] Dodson, J.R., Cooper, E.C., Hunt, A.J., Matharu, A., Cole, J., Minihan, A., Clark, J.H., and Macquarrie, D.J., 2013, Alkali silicates and structured mesoporous silicas from biomass power station wastes: The emergence of bio-MCMs, Green Chem., 15 (5), 1203–1210.

[28] Zhu, W., Zhang, Y., Hou, C., Pan, D., He, J., and Zhu, H., 2016, Covalent immobilization of lipases on monodisperse magnetic microspheres modified with PAMAM-dendrimer, J. Nanopart. Res., 18 (2), 32.

[29] 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.

[30] Zhang, G., Zhao, P., and Xu, Y., 2017, Development of amine-functionalized hierarchically porous silica for CO2 capture, J. Ind. Eng. Chem., 54, 59–68.

[31] Wu, C., Zhou, G., Jiang, X., Ma, J., Zhang, H., and Song, H., 2012, Active biocatalysts based on Candida rugosa lipase immobilized in vesicular silica, Process Biochem., 47 (6), 953–959.

[32] Motevalizadeh, S.F., Khoobi, M., Shabanian, M., Asadgol, Z., Faramarzi, M.A., and Shafiee, A., 2013, Polyacrolein/mesoporous silica nanocomposite: Synthesis, thermal stability and covalent lipase immobilization, Mater. Chem. Phys., 143 (1), 76–84.

[33] Majoul, N., Aouida, S., and Bessaïs, B., 2015, Progress of porous silicon APTES-functionalization by FTIR investigations, Appl. Surf. Sci., 331, 388–391.

[34] Isah, A.A., Mahat, N.A., Jamalis, J., Attan, N., Zakaria, I.I., Huyop, F., and Wahab, R.A., 2017, Synthesis of geranyl propionate in a solvent-free medium using Rhizomucor miehei lipase covalently immobilized on chitosan-graphene oxide beads, Prep. Biochem. Biotechnol., 47 (2), 199–210.

[35] Wahab, R.A., Basri, M., Rahman, M.B., Rahman, R.N., Salleh, A.B., and Leow, T.C., 2012, Combination of oxyanion Gln114 mutation and medium engineering to influence the enantioselectivity of thermophilic lipase from Geobacillus zalihae, Int. J. Mol. Sci., 13 (9), 11666–11680.

[36] Manan, F.M.A., Attan, N., Zakaria, Z., Keyon, A.S.A., and Wahab, R.A., 2018, Enzymatic esterification of eugenol and benzoic acid by a novel chitosan-chitin nanowhiskers supported Rhizomucor miehei lipase: Process optimization and kinetic assessments, Enzyme Microb. Technol., 108, 42–52.

[37] Stark, M.B., and Holmberg, K., 1989, Covalent immobilization of lipase in organic solvents, Biotechnol. Bioeng., 34 (7), 942–950.

[38] Öztürk, H., Pollet, E., Phalip, V., Güvenilir, Y., and Avérous, L., 2016, Nanoclays for lipase immobilization: Biocatalyst characterization and activity in polyester synthesis, Polymer, 8 (12), 416.

[39] Soares, I.P., Rezende, T.F., Pereira, R.C.C., dos Santos, C.G., and Fortes, I.C.P., 2011, Determination of biodiesel adulteration with raw vegetable oil from ATR-FTIR data using chemometric tools, J. Braz. Chem. Soc., 22 (7), 1229–1235.



DOI: https://doi.org/10.22146/ijc.42177

Article Metrics

Abstract views : 3864 | views : 2833


Copyright (c) 2019 Indonesian Journal of Chemistry

Creative Commons License
This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

 


Indonesian Journal of Chemistry (ISSN 1411-9420 /e-ISSN 2460-1578) - Chemistry Department, Universitas Gadjah Mada, Indonesia.

Web
Analytics View The Statistics of Indones. J. Chem.