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Construction and Characterization of a Nanostructured Biocatalyst Consisting of Immobilized Lipase on Mg-Amino-Clay

Published online by Cambridge University Press:  01 January 2024

Mingzhu Zhang ,
Shiyong Sun Open the ORCID record for Shiyong Sun [Opens in a new window] ,
Rui Lv ,
Yevgeny Aleksandrovich Golubev ,
Ke Wang ,
Faqin Dong ,
Olga Borisovna Kotova  and
Elena Leonidovna Kotova
Mingzhu Zhang
Affiliation:
Institute of Non-metallic Minerals, Key Laboratory of Solid Waste Treatment and Resource Recycle of Ministry of Education, School of Environment and Resource, Southwest University of Science and Technology, Mianyang, 621000, China
Shiyong Sun*
Affiliation:
Institute of Non-metallic Minerals, Key Laboratory of Solid Waste Treatment and Resource Recycle of Ministry of Education, School of Environment and Resource, Southwest University of Science and Technology, Mianyang, 621000, China
Rui Lv
Affiliation:
Institute of Non-metallic Minerals, Key Laboratory of Solid Waste Treatment and Resource Recycle of Ministry of Education, School of Environment and Resource, Southwest University of Science and Technology, Mianyang, 621000, China
Yevgeny Aleksandrovich Golubev
Affiliation:
Yushkin’s Institute of Geology, Komi Science Center, Ural Branch of RAS, ul. Pervomayskaya, 54, 167982, Syktyvkar, Russia
Ke Wang
Affiliation:
Institute of Non-metallic Minerals, Key Laboratory of Solid Waste Treatment and Resource Recycle of Ministry of Education, School of Environment and Resource, Southwest University of Science and Technology, Mianyang, 621000, China
Faqin Dong
Affiliation:
Institute of Non-metallic Minerals, Key Laboratory of Solid Waste Treatment and Resource Recycle of Ministry of Education, School of Environment and Resource, Southwest University of Science and Technology, Mianyang, 621000, China
Olga Borisovna Kotova
Affiliation:
Yushkin’s Institute of Geology, Komi Science Center, Ural Branch of RAS, ul. Pervomayskaya, 54, 167982, Syktyvkar, Russia
Elena Leonidovna Kotova
Affiliation:
Mining State University St. Petersburg, 21st Line, 199106 St. Petersburg, Russia
*
*E-mail address of corresponding author: shysun@swust.edu.cn
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Abstract

Lipase is an industrial enzyme, the catalytic efficiency of which is restricted by various environmental factors. To improve this efficiency, immobilization technology has been utilized in the past to improve the stability of lipase in harsh conditions. Immobilization technology can be divided into physical methods and chemical methods. Some unsolved problems remain in current immobilization technology. The interaction between enzyme and immobilization support is weak and reversible during physical adsorption, resulting in poor stability of the immobilized enzyme and the contamination of substrate solution by leached enzymes. In chemical methods, enzyme-active sites might be inactivated due to the chemical reactions between enzyme molecules and support, resulting in a decrease in the enzymes’ catalytic activity (Liu et al., 2018a). The objective of the current study was to construct a nanostructured lipase via Mg-amino-clay as a carrier and improve the catalytic activity and stability of lipase by immobilization. Lipase produced by Aspergillus oryzae was immobilized on aminopropyl functionalized magnesium phyllosilicate (a 2:1 trioctahedral talc-like silicate Mg-amino-clay) via a 1-(3-Dimethylaminopropyl)-3-ethyl-carbodiimide hydrochloride (EDC) coupling agent. The physical and chemical properties of the Mg-amino-clay and Mg-amino-clay-based nanostructured biocatalyst (Mg-clay-lipase) were characterized by X-ray diffraction, Fourier-transform infrared spectroscopy, and scanning electron microscopy. Optimal immobilization conditions were determined by taking into account the following variables: amount of initial lipase, EDC concentration, and reaction time. The results revealed that the optimum temperature, pH, and thermal stability of Mg-clay-lipase were greater than equivalent values for free lipase under optimal conditions (described below – Process for Immobilization of Lipase on Mg-amino-clay). The Michaelis-Menten constant (Km) values were 5.25 mM and 7.42 mM while the maximum reaction rates (vmax) were 30.58 mM/(L·min) and 55.87 mM/(L·min) for free lipase and Mg-clay-lipase, respectively. The present study provided a new nanostructured biocatalyst and demonstrated that the enzyme activity and stability of Mg-clay-lipase were superior to those of free lipase due to the mechanism of 'interface activation'.

Keywords

BiocatalystEnzyme immobilizationLipaseMg-amino-clay
Type
Article
Information
Clays and Clay Minerals , Volume 69 , Issue 4 , August 2021 , pp. 434 - 442
Copyright
Copyright © Clay Minerals Society 2021

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Footnotes

The paper is based on a presentation made during the 4th Asian Clay Conference, Thailand, June 2020.

References

Aghaei, H., Ghavi, M., Hashemkhani, G., & Keshavarz, M. (2020). Utilization of two modified layered doubled hydroxides as supports for immobilization of Candida rugosa lipase. International Journal of Biological Macromolecules, 162, 74–83. https://doi.org/10.1016/j.ijbiomac.2020.06.145.CrossRefGoogle ScholarPubMed
Akash, A., & Weatherley, L. R. (2018). The performance of microbial lipase immobilized onto polyolefin supports for hydrolysis of high oleate sunflower oil. Process Biochemistry, 68, 100–107.Google Scholar
Atiroğlu, V. (2020). Lipase immobilization on synthesized hyaluronic acid-coated magnetic nanoparticle-functionalized graphene oxide composites as new biocatalysts: Improved reusability, stability, and activity. International Journal of Biological Macromolecules, 145, 456–465. https://doi.org/10.1016/j.ijbiomac.2019.12.233.CrossRefGoogle ScholarPubMed
Badoei-dalfard, A., Malekabadi, S., Karami, Z., & Sargazi, G. (2019). Magnetic cross-linked enzyme aggregates of Km12 lipase: A stable nanobiocatalyst for biodiesel synthesis from waste cooking oil. Renewable Energy, 141, 874–882.CrossRefGoogle Scholar
Barse, L. Q., Graebin, N. G., Cipolatti, E.P., Robert, J. M., Pinto, M. C. C., Pinto, J. C. C. S., et al. (2019). Production and optimization of isopropyl palmitate via biocatalytic route using home-made enzymatic catalysts. Journal of Chemical Technology & Biotechnology, 94, 389–397.CrossRefGoogle Scholar
Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72, 248–254. https://doi.org/10.1006/abio.1976.9999.CrossRefGoogle ScholarPubMed
Brzozowski, A. M., Derewenda, U., Derewenda, Z. S., Dodson, G. G., Lawson, D. M., Turkenburg, J. P., et al. (1991). A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex. Nature, 351, 491–494. https://doi.org/10.1038/351491a0.CrossRefGoogle Scholar
Burkett, S. L., Press, A., & Mann, S. (1997). Synthesis, characterization, and reactivity of layered inorganic-organic nanocomposites based on 2: 1 trioctahedral phyllosilicates. Chemistry of Materials, 9, 1071–1073.CrossRefGoogle Scholar
Cipolatti, E. P., Manoel, E. A., Fernandez-Lafuente, R., & Freire, D. M. G. (2017). Support engineering: relation between development of new supports for immobilization of lipases and their applications. Biotechnology Research and Innovation, 1, 26–34.CrossRefGoogle Scholar
Datta, K. K. R., Achari, A., & Eswaramoorthy, M. (2013). Aminoclay: a functional layered material with multifaceted applications. Journal of Materials Chemistry, 1(6707), 6718. https://doi.org/10.1039/c3ta00100h.Google Scholar
de Barros, D. S. N., Fernandez-Lafuente, R., Aguieiras, E. C. G., & Freire, D. M. G. (2019). Production of lipases in cottonseed meal and application of the fermented solid as biocatalyst in esterification and transesterification reactions. Renewable Energy, 130, 574–581.Google Scholar
de Paula, A. V., dos Santos, J. C., Nunes, G. F. M., & de Castro, H. E. (2018). Performance of packed bed reactor on the enzymatic interesterification of milk fat with soybean oil to yield structure lipids. International Dairy Journal, 86, 1–8.CrossRefGoogle Scholar
Fernandez-Lafuente, R., Armisén, P., Sabuquillo, P., Fernández-Lorente, G., & Guisán, J. M. (1998). Immobilization of lipases by selective adsorption on hydrophobic supports. Chemistry and Physics of Lipids, 93, 185–197. https://doi.org/10.1016/s0009-3084(98)00042-5.CrossRefGoogle ScholarPubMed
Gupta, M. N., Jain, P., & Jain, S. (2005). A microwave-assisted microassay for lipases. Analytical and Bioanalytical Chemistry, 381, 1480–1482.Google Scholar
Hanefeld, U., Gardossi, L., & Magner, E. (2009). Understanding enzyme immobilisation. Chemical Society Reviews, 38, 453–468. https://doi.org/10.1039/b711564b.CrossRefGoogle ScholarPubMed
Hartmann, M., & Kostrov, X. (2013). Immobilization of enzymes on porous silicas – benefits and challenges. Chemical Society Reviews, 42, 6277–6289. https://doi.org/10.1039/c3cs60021a.CrossRefGoogle ScholarPubMed
Holmström, S., Patil, A. J., Butler, M., & Mann, S. (2007). Influence of polymer co-intercalation on guest release from aminopropyl-functionalized magnesium phyllosilicate mesolamellar nanocomposites. Journal of Materials Chemistry, 17, 3894–3900.CrossRefGoogle Scholar
Kavadia, M. R., Yadav, M. G., Odaneth, A. A., & Lali, A. M. (2018). Synthesis of designer triglycerides by enzymatic acidolysis. Biotechnol Rep (Amst), 18, e00246. https://doi.org/10.1016/j.btre.2018.e00246.Google ScholarPubMed
Kołodziejska, R., Studzińska, R., & Pawluk, H. (2018). Lipase-catalyzed enantioselective transesterification of prochiral 1-((1,3-dihydroxypropan-2-yloxy)methyl)-5,6,7,8-tetrahydroquinazoline-2,4(1H,3H)-dione in ionic liquids. Chirality, 30, 206–214. https://doi.org/10.1002/chir.22787.CrossRefGoogle Scholar
Li, Y., Li, J., & Dong, H. (2012). Improvement of catalytic activity and stability of lipase by immobilization on organobentonite. Chemical Engineering Journal, 181–182, 590–596.Google Scholar
Liu, D. M., Chen, J., & Shi, Y. P. (2018a). Advances on methods and easy separated support materials for enzymes immobilization. Trends in Analytical Chemistry, 102, 332–342. https://doi.org/10.1016/j.trac.2018.03.011.CrossRefGoogle Scholar
Liu, J., Guo, H., & Zhou, Q. (2013). Highly efficient enzymatic preparation for dimethyl carbonate catalyzed by lipase from Penicillium expansum immobilized on CMC-PVA film. Journal of Molecular Catalysis, B. Enzymatic, 96, 96–102.CrossRefGoogle Scholar
Liu, X., Fang, Y., Yang, X., Li, Y., & Wang, C. (2018b). Electrospun epoxy-based nanofibrous membrane containing biocompatible feather polypeptide for highly stable and active covalent immobilization of lipase. Colloids and Surfaces B: Biointerfaces, 166, 277–285. https://doi.org/10.1016/j.colsurfb.2018.03.037.CrossRefGoogle ScholarPubMed
Liu, J., Ma, R. T., & Shi, Y. P. (2020). “Recent advances on support materials for lipase immobilization and applicability as biocatalysts in inhibitors screening methods” – A review. Analytica Chimica Acta, 1101, 9–22. https://doi.org/10.1016/j.aca.2019.11.073.CrossRefGoogle ScholarPubMed
Löfgren, J., Görbe, T., Oschmann, M., Svedendahl Humble, M., & Bäckvall, J. E. (2019). Transesterification of a Tertiary Alcohol by Engineered Candida antarctica Lipase A. Chembiochem, 20, 1438–1443. https://doi.org/10.1002/cbic.201800792.CrossRefGoogle ScholarPubMed
Madhavan, A., Sindhu, R., Binod, P., Sukumaran, R. K., & Pandey, A. (2017). Strategies for design of improved biocatalysts for industrial applications. Bioresource Technology, 245, 1304.CrossRefGoogle ScholarPubMed
Manoel, E. A., Dos Santos, J. C., Freire, D. M., Rueda, N., & Fernandez-Lafuente, R. (2015). Immobilization of lipases on hydrophobic supports involves the open form of the enzyme. Enzyme and Microbial Technology, 71, 53–57. https://doi.org/10.1016/j.enzmictec.2015.02.001.CrossRefGoogle ScholarPubMed
Mehrasbi, M. R., Mohammadi, J., Peyda, M., & Mohammadi, M. (2017). Covalent immobilization of Candida antarctica lipase on core-shell magnetic nanoparticles for production of biodiesel from waste cooking oil. Renewable Energy, 101, 593–602.CrossRefGoogle Scholar
Öztürk, H., Pollet, E., Phalip, V., Güvenilir, Y., & Avérous, L. (2016). Nanoclays for lipase immobilization: biocatalyst characterization and activity in polyester synthesis. Polymers, 8, 416.CrossRefGoogle ScholarPubMed
Palomo, J. M., Femandez-Lorente, G., & Mateo, C. (2007). Improvement of enzyme activity, stability and selectivity via immobilization techniques. Enzyme and Microbial Technology, 40, 1451–1463.Google Scholar
Papadaki, A., Fernandes, K. V., Guimaraes Freire, D. M., Koutinas, A. A., Cavalcanti da Silva, J. A., & Fernandez-Lafuente, R. (2018). Enzymatic esterification of palm fatty-acid distillate for the production of polyol esters with biolubricant properties. Industrial Crops and Products, 116, 90–96.Google Scholar
Park, D., Lee, Y. C., & Hoang Bui, V. K. (2018). Aminoclays for biological and environmental applications: An updated review. Chemical Engineering Journal, 336, 757–772.Google Scholar
Patil, A. J., Muthusamy, E., & Mann, S. (2005). Fabrication of functional protein–organoclay lamellar nanocomposites bybiomolecule-induced assembly of exfoliated aminopropyl-functionalized magnesium phyllosilicates. Journal of Materials Chemistry, 15, 3838–3843.CrossRefGoogle Scholar
Patil, A. J., Li, M., Dujardin, E., & Mann, S. (2007). Novel bioinorganic nanostructures based on mesolamellar intercalation or single-molecule wrapping of DNA using organoclay building blocks. Nano Letters, 7, 2660–2665.CrossRefGoogle ScholarPubMed
Rehm, S., Trodler, P., & Pleiss, J. (2010). Solvent-induced lid opening in lipases: a molecular dynamics study. Protein Science: A Publication of the Protein Society, 19, 2122–2130. https://doi.org/10.1002/pro.493.CrossRefGoogle ScholarPubMed
Sheldon, R. A. (2007). Enzyme immobilization: The quest for optimum performance. Advanced Synthesis & Catalysis, 349, 1289–1307.CrossRefGoogle Scholar
Sugunan, S., & Gopinath, S. (2007). Enzymes immobilized on montmorillonite K10: Effect of adsorption and grafting on the surface properties and the enzyme activity. Applied Clay Science, 35, 67–75.Google Scholar
Tudorache, M., Coman, S., & Protesescu, L. (2012). Efficient bio-conversion of glycerol to glycerol carbonate catalyzed by lipase extracted from Aspergillus niger. Green Chemistry, 14, 478–482.CrossRefGoogle Scholar
Urrutia, P., Arrieta, R., Alvarez, L., Cardenas, C., Mesa, M., & Wilson, L. (2018). Immobilization of lipases in hydrophobic chitosan for selective hydrolysis of fish oil: The impact of support functionalization on lipase activity, selectivity and stability. International Journal of Biological Macromolecules, 108, 674–686. https://doi.org/10.1016/j.ijbiomac.2017.12.062.CrossRefGoogle ScholarPubMed
Wang, J., Zhao, G., & Yu, F. (2016). Facile preparation of Fe3O4@MOF core-shell microspheres for lipase immobilization. Journal of the Taiwan Institute of Chemical Engineers, 69, 139–145.CrossRefGoogle Scholar
Wang, R., Jing, G., Zhou, X., & Lv, B. (2017). Removal of chromium(VI) from wastewater by Mg-aminoclay coated nanoscale zero-valent iron. Journal of Water Process Engineering, 18, 134–143.CrossRefGoogle Scholar
Wang, K., Sun, S., Ma, B., Dong, F., Huo, T., Li, X., & 3 others (2019). Construction and characterization of a nanostructured biocatalyst consisting of immobilized lipase on aminopropyl-functionalized montmorillonite. Applied Clay Science, 183, 105329CrossRefGoogle Scholar
Wijnants, M., Cornet, I., & Bauwelinck, J. (2018). Investigation of the enzyme-catalysed transesterification of methyl acrylate and sterically hindered alcohol substrates. Chemistry Select, 3, 1–7.Google Scholar
Yong, Y., Bai, Y., Li, Y., Lin, L., Cui, Y., & Xia, C. (2008). Characterization of Candida rugosa lipase immobilized onto magnetic microspheres with hydrophilicity. Process Biochemistry, 43, 1179–1185.CrossRefGoogle Scholar
Zhu, W., Zhang, Y., Hou, C., Pan, D., He, J., & Zhu, H. (2016). Covalent immobilization of lipases on monodisperse magnetic microspheres modified with PAMAM-dendrimer. Journal of Nanoparticle Research, 18, 13.CrossRefGoogle Scholar