Abstract
The nonaqueous catalysis of lipases is significant for synthesis of high pure esters, but they usually behave low catalytic activity due to denaturation and aggregation of enzyme protein in organic phases. To improve the nonaqueous catalysis, the inexpensive copper phthalocyanine was taken as a new carrier on which Pseudomonas cepacia lipase was immobilized by physical absorption, and used for synthesis of hexyl acetate, an important flavor, via transesterification of hexanol and vinyl acetate. Results showed that the desired loading was 10 mg lipase immobilized on 10 mg copper phthalocyanine powder. When the immobilized lipase was employed in the reaction system consisted of 1.5 mL hexanol and 1.5 mL vinyl acetate at 37℃ and 160 rpm, the conversion was five fold of that catalyzed by native lipase after 1 h, and reached 99.0% after 8 h. Undergoing six times of 8-h reuses, the immobilized lipase had an activity attenuation rate 1.22% h− 1, lower than 1.77% h− 1 of native lipase, which meant that the immobilized lipase was more stable. Even at the room temperature and the static state without shaking or stirring, the immobilized lipase could bring conversion 42.8% after 10 h and the native lipase gave 20.1%. Obviously, the immobilized lipase is an available biocatalyst in organic phase and has great potential in food industry.
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27 June 2023
This article has been retracted. Please see the Retraction Notice for more detail: https://doi.org/10.1007/s12010-023-04616-5
References
Bauer, K., Garbe, D., & Surburg, H. (2008). Common fragrance and flavor materials: Preparation, properties and uses 3rd Edition. Wiley-VCH Publishers.
Yu, Z. R., Chang, S. W., Wang, H. Y., & Shieh, C. J. (2003). Study on synthesis parameters of lipase-catalyzed hexyl acetate in supercritical CO2 by response surface methodology. Journal of The American Oil Chemists Society, 80(2), 139–144.
Patel, D., & Saha, B. (2007). Heterogeneous kinetics and residue curve map (RCM) determination for synthesis of n-hexyl acetate using ion-exchange resins as catalysts. Industrial and Engineering Chemistry Research, 46, 3157–3169.
Yang, Z., Pan, Y., Mei, Z., & Zhang, W. (2012). Preparation of mesoporous MnO2/C catalyst for n-hexyl acetate synthesis. Applied Surface Science, 258, 4756–4763.
Colombo, C., & Bennet, A. J. (2019). The physical organic chemistry of glycopyranosyl transfer reactions in solution and enzyme-catalyzed. Current Opinion in Chemical Biology, 53, 145–157.
Cai, X., Wang, W., Lin, L., He, D., Shen, Y., Wei, W., & Wei, D. Z. (2017). Cinnamyl esters synthesis by lipase-catalyzed transesterification in a non-aqueous system. Catalysis Letters, 147, 946–952.
Yang, B. (2006). Lipase-catalyzed synthesis of hexyl acetate in non-aqueous medium. Science and Technology of Food Industry, 27(6), 144–147.
Murcia, M. D., Gómez, M., Gómez, E., Gómez, J. L., Hidalgo, A. M., Sánchez, A., & Vergara, P. (2018). Kinetic modelling and kinetic parameters calculation in the lipase-catalysed synthesis of geranyl acetate. Chemical Engineering Research and Design, 138, 135–143.
Wackett, L. P., & Robinson, S. L. (2020). The ever-expanding limits of enzyme catalysis and biodegradation: polyaromatic, polychlorinated, polyfluorinated, and polymeric compounds. The Biochemical Journal, 477, 2875–2891.
Fonseca, A. M., Freitas, Í. B., Soares, N. B., Araújo, F. A. M., Gaieta, E. M., Santos, J. C. S., Sobrinho, A. C. N., Marinho, E. S., & Colares, R. P. (2022). Synthesis, biological activity, and in silico study of bioesters derived from bixin by the CALB Enzyme. Biointerface Research in Applied Chemistry, 12(5), 5901–5917.
Mota, G. F., Sousa, I. G., Oliveira, A. L. B., Cavalcante, A. L. G., Moreira, K. S., Cavalcante, F. T. T., Souza, J. E. S., Falcão, Í. R. A., Rocha, T. G., Valério, R. B. R., Carvalho, S. C. F., Neto, F. S., Serpa, J. F., Lima, R. K. C., Souza, M. C. M., & Santos, J. C. S. (2022). Biodiesel production from microalgae using lipase-based catalysts: Current challenges and prospects. Algal Research, 62, 102616.
Lima, G. V., Silva, M., Thiago, D., Lima, L. D., Oliveira, M. D., Lemos, T. D., Zampieri, D., Santos, J. C. S., Rios, N. S., Gonçalves, L. R. B., Molinari, F., & Mattos, M. C. (2017). Chemoenzymatic synthesis of (S)-Pindolol using lipases. Applied Catalysis A: General, 546, 7–14.
Verdasco-Martín, C. M., Villalba, M., Santos, J. C. S. D., Tobajas, M., Fernandez-Lafuente, R., & Otero, C. (2016). Effect of chemical modification of Novozym 435 on its performance in the alcoholysis of camelina oil. Biochemical Engineering Journal, 111, 75–86.
Moreira, K. S., Oliveira, A. L. B., Júnior, L. S. M., Sousa, I. G., Cavalcante, A. L. G., Neto, F. S., Valério, R. B. R., Chaves, A. V., Fonseca, T. S., Cruz, D. M. V., Lima, G. V., Oliveira, G. P., Souza, M. C. M., Fechine, P. B. A., Mattos, M. C., Fonseca, A. M., & Santos, J. C. S. (2022). Taguchi design-assisted co-immobilization of lipase A and B from Candida antarctica onto chitosan: Characterization, kinetic resolution application, and docking studies. Chemical Engineering Research and Design, 177, 223–244.
Lima, P., Silva, R. M. D., Neto, C., Silva, N., Souza, J., Nunes, Y. L., & Santos, J. C. S. (2021). An overview on the conversion of glycerol to value-added industrial products via chemical and biochemical routes. Biotechnology and Applied Biochemistry. https://doi.org/10.1002/bab.2098
Cavalcante, F., Neto, F. S., Falco, I., Souza, J., & Santos, J. (2020). Opportunities for improving biodiesel production via lipase catalysis. Fuel, 288, 119577.
Valério, R. B. R., Cavalcante, A. L. G., Mota, G. F., Sousa, I. G., Souza, J. E. S., Cavalcante, F. T. T., Moreira, K. S., Falcão, I. R. A., Neto, F. S., & Santos, J. C. S. (2022). Understanding the biocatalytic potential of lipase from Rhizopus chinensis. Biointerface Research in Applied Chemistry, 12(3), 4230–4260.
Moreira, K., Oliveira, A., Júnior, L. S. D. M., Monteiro, R., & Santos, J. (2020). Lipase from Rhizomucor miehei immobilized on magnetic nanoparticles: Performance in fatty acid ethyl ester (FAEE) optimized production by the Taguchi method. Frontiers in Bioengineering and Biotechnology, 8, 693.
Fernandez-Lopez, L., Bartolome-Cabrero, R., Rodriguez, M. D., Santos, C., Rueda, N., & Fernandez-Lafuente, R. (2015). Stabilizing effects of cations on lipases depend on the immobilization protocol. RSC Advances, 5, 83868–83875.
Rios, N. S., Neto, D., Santos, J., Fechine, P., & Gonalves, L. (2019). Comparison of the immobilization of lipase from Pseudomonas fluorescens on divinylsulfone or p-benzoquinone activated support. International Journal Of Biological Macromolecules, 134, 936–945.
Collu, M., Carucci, C., & Salis, A. (2020). Specific anion effects on lipase adsorption and enzymatic synthesis of biodiesel in nonaqueous media. Langmuir, 36, 9465–9471.
Xiong, J., Huang, Y. J., & Zhang, H. (2012). Lipase-catalyzed transesterification synthesis of citronellyl acetate in a solvent-free system and its reaction kinetics. European Food Research and Technology, 235, 907–914.
Cao, W., Cong, F., Kang, J., Zhang, S., Li, X., Wang, X., Li, P., & Yu, J. (2020). A simple room temperature-static bioreactor for effective synthesis of hexyl acetate. Green Processing and Synthesis, 9, 48–55.
Yadav, G. D., & Borkar, I. V. (2009). Kinetic and mechanistic investigation of microwave-assisted lipase catalyzed synthesis of citronellyl acetate. Industrial and Engineering Chemistry Research, 48, 7915–7922.
Hu, X., Qin, H., Hu, B., Cheng, H., Chen, L., & Qi, Z. (2019). A rate-based method for dynamic analysis and optimal design of reactive extraction: n-Hexyl acetate esterification as an example. The Chinese Journal of Chemical Engineering, 28(1), 76–83.
Ou, J., Yuan, X., Liu, Y., Zhang, P., & Tang, K. (2020). Lipase from Pseudomonas cepacia immobilized into zif-8 as bio-catalyst for enantioselective hydrolysis and transesterification. Process Biochemistry, 102, 132–140.
Cao, Y. P., Zhi, G. Y., Han, L., Chen, Q., & Zhang, D. H. (2021). Biosynthesis of benzyl cinnamate using an efficient immobilized lipase entrapped in nano-molecular cages. Food Chemistry, 364, 130428.
Winkler, F. K., D’Arcy, A., & Hunziker, W. (1990). Structure of human pancreatic lipase. Nature, 343, 771–774.
Silveira, R. L., Knott, B. C., Pereira, C. S., Crowley, M. F., & Beckham, G. T. (2021). Transition path sampling study of the feruloyl esterase mechanism. The Journal Of Physical Chemistry B, 125, 2018–2030.
Souza, T., Fonseca, T., Silva, J., Lima, P., & Gonalves, L. (2020). Modulation of lipase B from Candida antarctica properties via covalent immobilization on eco-friendly support for enzymatic kinetic resolution of rac-indanyl acetate. Bioprocess and Biosystems Engineering, 43, 2253–2268.
Mateo, C., Palomo, J. M., Fernandez-Lorente, G., Guisan, J. M., & Fernandez-Lafuente, R. (2007). Improvement of enzyme activity, stability and selectivity via immobilization techniques. Enzyme and Microbial Technology, 40, 1451–1463.
Zhong, L., Feng, Y., Wang, G., Wang, Z., Bilal, M., Lv, H., Jia, S., & Cui, J. (2020). Production and use of immobilized lipases in/on nanomaterials: A review from the waste to biodiesel production. International Journal of Biological Macromolecules, 152, 207–222.
Zahirinejad, S., Hemmati, R., Homaei, A., Dinari, A., Hosseinkhani, S., Mohammadi, S., & Vianello, F. (2021). Nano-organic supports for enzyme immobilization: Scopes and perspectives. Colloid Surface B, 204(4), 111774.
Arana-Pea, S., Rios, N. S., Carballares, D., Gonalves, L., & Fernandez-Lafuente, R. (2021). Immobilization of lipases via interfacial activation on hydrophobic supports: Production of biocatalysts libraries by altering the immobilization conditions. Catalysis Today, 362, 130–140.
Mehta, J., Bhardwaj, N., Bhardwaj, S. K., Kim, K. H., & Deep, A. (2016). Recent advances in enzyme immobilization techniques: Metal-organic frameworks as novel substrates. Coordination Chemistry Reviews, 322, 30–40.
Verma, C., Ebenso, E. E., Quraishi, M. A., & Rhee, K. Y. (2021). Phthalocyanine, naphthalocyanine and their derivatives as corrosion inhibitors: A review. Journal of Molecular Liquids, 334, 116441.
Kurliandski, B. A., Braude, E. V., Kliachkina, A. M., Torshina, N. L., & Khokhlova, S. B. (1985). Toxicity of copper phthalocyanine. Gigiena i Sanitariia, (1), 92–93.
Li, M., Hu, Q., Shan, H., Yu, W., & Xu, Z. X. (2020). Fabrication of copper phthalocyanine/reduced graphene oxide nanocomposites for efficient photocatalytic reduction of hexavalent chromium. Chemosphere, 263, 128250.
Zhou, W., Zhang, W., & Cai, Y. (2021). Laccase immobilization for water purification: A comprehensive review. Chemical Engineering Journal, 403, 126272.
Zhong, H., Wang, K., & Chen, H. Y. (2004). Protein analysis with tetra-substituted sulfonated cobalt phthalocyanine by the technique of rayleigh light scattering. Analytical Biochemistry, 330(1), 37–42.
Nunes, Y. L., Menezes, F., Sousa, I., Cavalcante, A., & Santos, J. (2021). Chemical and physical chitosan modification for designing enzymatic industrial biocatalysts: How to choose the best strategy? International Journal of Biological Macromolecules, 181, 1124–1170.
Liu, D. M., & Dong, C. (2020). Recent advances in nano-carrier immobilized enzymes and their applications. Process Biochemistry, 92, 464–475.
Sharath, A. K., Haque, N., & Prabhu, N. P. (2020). Spontaneous lid closure and substrate-induced lid opening dynamics of human pancreatic lipase-related protein 2: A computational study. Journal of Molecular Structure, 1217, 128365.
Fonseca, A. M., Santos, J. C. S., Souza, M. C. M., Oliveira, M. M., Colares, R. P., Lemos, T. L. G., & Braz-Filho, R. (2020). The use of new hydrogel microcapsules in coconut juice as biocatalyst system for the reaction of quinine. Industrial Crops and Products, 145, 111890.
Ghani, F., Gojzewski, H., & Riegler, H. (2015). Nucleation and growth of copper phthalocyanine aggregates deposited from solution on planar surfaces. Applied Surface Science, 351, 969–976.
Saik, A. Y. H., Lim, Y. Y., Stanslas, J., & Choo, W. S. (2020). Biosynthesis of quercetin palmitate esters and evaluation of their physico-chemical properties and stability. Journal of the American Oil Chemists Society, 97(9), 977–988.
Jaladi, H., Katiyar, A., Thiel, S. W., Guliants, V. V., & Pinto, N. G. (2009). Effect of pore diffusional resistance on biocatalytic activity of Burkholderia cepacia lipase immobilized on SBA-15 hosts. Chemical Engineering Science, 64, 1474–1479.
Reetz, M. T., & Jiao, N. (2006). Copper-phthalocyanine conjugates of serum albumins as enantioselective catalysts in Diels-Alder reactions. Angewandte Chemie International Edition, 45(15), 2416–2419.
Farahmand, S., Ghiaci, M., & Razavizadeh, J. S. (2019). Copper phthalocyanine as an efficient and reusable heterogeneous catalyst for direct hydroxylation of benzene to phenol under mild conditions. Inorganica Chimica Acta, 484, 174–179.
Castro, K. A. D. F., Figueira, F., Paz, F. A. A., Tomé, J. P. C., Silva, R. S., Nakagaki, S., Neves, M. G. P. M. S., Cavaleiro, J. A. S., & Simões, M. M. Q. (2019). Copper-phthalocyanine coordination polymer as a reusable catechol oxidase biomimetic catalyst. Dalton Transactions, 48(23), 8144–8152.
Sanchez, A., Cruz, J., Rueda, N., Santos, J. C. S., Torres, R., Ortiz, C., Villalonga, R., & Lafuente, R. F. (2016). Inactivation of immobilized trypsin under dissimilar conditions produces trypsin molecules with different structures. RSC Advances, 6(33), 27329–27334.
Pinheiro, M. P., Rios, N. S., Thiago, D., Francisco, D., Rodríguez-Castellón, E., Fernandez-Lafuente, R., Mattos, M. C., Santos, J. C. S., & Gonçalvesa, L. R. B. (2018). Kinetic resolution of drug intermediates catalyzed by lipase B from Candida antarctica immobilized on immobead-350. Biotechnology Progress, 34(4), 878–889.
Manoel, E. A., Pinto, M., Santos, J. D., Tacias-Pascacio, V. G., Freire, D., Pinto, J. C., & Fernandez-Lafuente, R. (2016). Design of a core–shell support to improve lipase features by immobilization. RSC Advances, 6(67), 62814–62824.
Bhuiyan, A. H., Nagakawa, T., Zakaria, M., & Nakane, K. (2021). Utilization of polyvinyl butyral-zirconium alkoxide hybrid hollow tube as an enzyme immobilization carrier. Journal Materials Science, 56, 1–11.
Solanki, K., & Gupta, M. N. (2011). A chemically modified lipase preparation for catalyzing the transesterification reaction in even highly polar organic solvents. Bioorganic & Medicinal Chemistry Letters, 21(10), 2934–2936.
Wang, X., Wang, X., Cong, F., Xu, Y., Kang, J., Zhang, Y., Zhou, M., Xing, K., Zhang, G. & Pan, H. (2018). Synthesis of cinnamyl acetate catalysed by highly reusable cotton-immobilized Pseudomonas fluorescens lipase. Biocatalysis and Biotransformation, 36(4), 332–339.
Galvão, W. S., Pinheiro, B. B., Golçalves, L. R. B., Mattos, M. C., Fonseca, T. S., Regis, T., Zampieri, D., Santos, J. C. S., Costa, L. S., Correa, M. A., Bohn F., & Fechine, P. B. A. (2018). Novel nanohybrid biocatalyst: Application in the kinetic resolution of secondary alcohols. The Journal of Materials Science, 53, 14121–14137.
Yan, Q., Li, L., Cong, F., Liu, H., Zhou, X., Xing, K., Kong, X., & Zhao, R. (2015). Catalyzed synthesis of hexyl acetate in immobilized lipase bioreactor. Science and Technology of Food Industry, 36(9), 171–174.
Wang, S., Wang, S., Cong, F., Hu, X., Xing, K., Wang, Y., & Zhang, Y. (2015). Polyacrylic resin mediated catalysis of Pseudomonas cepacia lipase. Food Science & Technology, 40(10), 211–215.
Lei, L., Bai, Y., Li, Y., Yi, L., Yang, Y., & Xia, C. (2009). Study on immobilization of lipase onto magnetic microspheres with epoxy groups. Journal of Magnetism and Magnetic Materials, 321, 252–258.
Shieh, C. J., & Chang, S. W. (2001). Optimized synthesis of lipase-catalyzed hexyl acetate in n-hexane by response surface methodology. Journal of Agriculture and Food Chemistry, 49, 1203–1207.
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This work was supported by the National Key R & D Program of China (2019YFC1605305), the Key Project of Tianjin Natural Science Foundation (18JCZDJC97800), the Technical System of Freshwater Aquaculture Industry in Tianjin (ITTFRS2021000), the Open Fund of Tianjin Key Lab of Aquatic Ecology and Aquaculture (TJAE201802).
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All authors contributed to the study conception and design. Material preparation and data collection were performed by Xinran Liu (65), Mengyao Han (10), Liwang Zhang (10), Zhongli Wang (5), Lu Jiang (5), and Bingqian Liu (5). Analysis was performed by Xinran Liu (30), Fangdi Cong (30), Shulin Zhang (10), Wei Yang (10), Yongpeng Su (5), Tao Li (5), Yingchao Wang (5), and Daying Liu (5). The first draft of the manuscript was written by Fangdi Cong and all authors commented on previous versions of the manuscript. All authors read and approved the final manuscript.
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Liu, X., Cong, F., Han, M. et al. RETRACTED ARTICLE: Copper Phthalocyanine Improving Nonaqueous Catalysis of Pseudomonas cepacia Lipase for Ester Synthesis. Appl Biochem Biotechnol 194, 6302–6318 (2022). https://doi.org/10.1007/s12010-022-04080-7
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DOI: https://doi.org/10.1007/s12010-022-04080-7