Progresso recente em nanopartículas magnéticas e materiais mesoporosos para imobilização de enzimas: uma atualização

Ding, S.-S.; Zhu, J.-P.; Wang, Y.; Yu, Y.; Zhao, Z.

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Brazilian Journal of Biology

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Sumário

Original Article • Braz. J. Biol. 82 • 2022 • https://doi.org/10.1590/1519-6984.244496 copiar

Progresso recente em nanopartículas magnéticas e materiais mesoporosos para imobilização de enzimas: uma atualização

Autoria SCIMAGO INSTITUTIONS RANKINGS

Resumo

Enzimas imobilizadas em substratos com excelente seletividade e atividade apresentam alta estabilidade e podem suportar condições experimentais extremas, e seu desempenho foi mantido após repetidos usos. As aplicações de enzimas imobilizadas em vários campos se beneficiam de suas características únicas. Métodos comuns, incluindo adsorção, encapsulamento, ligação covalente e reticulação, e outras abordagens emergentes (por exemplo, MOFs) de imobilização de enzima, foram desenvolvidos principalmente nos últimos anos. De acordo com esses métodos de imobilização, a presente revisão elabora a aplicação de nanopartículas magnéticas separáveis e materiais mesoporosos funcionalizados SBA-15 e MCM-41 usados na imobilização de enzimas.

Palavras-chave:
material mesoporoso funcionado MCM-41 e SBA-15; nanopartícula magnética; imobilização enzimática

Immobilization Method	Support material	Enzyme	Improved Enzyme Properties	Ref
Covalent Bond	Fe₃O₄ nanoparticles	Candida antarctica lipase B	Stability	(Gkaniatsou et al., 2018GKANIATSOU, E., SICARD, C., RICOUX, R., BENAHMED, L., BOURDREUX, F., ZHANG, Q., SERRE, C., MAHY, J.P. and STEUNOU, N., 2018. Enzyme encapsulation in mesoporous metal–organic frameworks for selective biodegradation of harmful dye molecules. Angewandte Chemie, vol. 130, no. 49, pp. 16141-16146. http://dx.doi.org/10.1002/ange.201811327. PMid:30307095. http://dx.doi.org/10.1002/ange.201811327... )
Covalent Bond	Fe₃O₄ nanocomposites	Lipase	Hydrophilicity and biocompatibility	(Mahto et al., 2016MAHTO, T.K., CHOWDHURI, A.R., SAHOO, B. and SAHU, S.K., 2016. Polyaniline‐functionalized magnetic mesoporous nanocomposite: A smart material for the immobilization of lipase. Polymer Composites, vol. 37, no. 4, pp. 1152-1160. http://dx.doi.org/10.1002/pc.23278. http://dx.doi.org/10.1002/pc.23278... )
Crossing-linking	Tannic-acid-templated magnetic mesoporous silica nanoparticles (TA-MMSNs)	NHase	Yield	(Gao et al., 2017a)GAO, J., YU, H., ZHOU, L., HE, Y., MA, L. and JIANG, Y., 2017a. Formation of cross-linked nitrile hydratase aggregates in the pores of tannic-acid-templated magnetic mesoporous silica: characterization and catalytic application. Biochemical Engineering Journal, vol. 117, no. Pt A, pp. 92-101. http://dx.doi.org/10.1016/j.bej.2016.10.005. http://dx.doi.org/10.1016/j.bej.2016.10....
Crossing-linking	Polydopamine (PDA)-functionalized magnetic nanoparticle	DNA catalytic	Stability and reusability	(Yang et al., 2018YANG, Y., WANG, S., ZHOU, Z., ZHANG, R., SHEN, H., SONG, J., SU, P. and YANG, Y., 2018. Enhanced reusability and activity: DNA directed immobilization of enzyme on polydopamine modified magnetic nanoparticles. Biochemical Engineering Journal, vol. 137, pp. 108-115. http://dx.doi.org/10.1016/j.bej.2018.05.019. http://dx.doi.org/10.1016/j.bej.2018.05.... )
Crossing-linking	PAL-coated magnetic nanoparticles	Phenylalanine ammonia-lyase (PAL)	Reproducibility	(Ender et al., 2016ENDER, F., WEISER, D., NAGY, B., BENCZE, C. L., PAIZS, C., PÁLOVICS, P. and POPPE, L., 2016. Microfluidic multiple cell chip reactor filled with enzyme-coated magnetic nanoparticles—an efficient and flexible novel tool for enzyme catalyzed biotransformations. Journal of Flow Chemistry, vol. 6, no. 1, pp. 43-52.)
Crossing-linking	Dendritic polymer-modified nanoparticles	Lipase	Yield	(Li et al., 2018LI, K., WANG, J., HE, Y., CUI, G., ABDULRAZAQ, M.A. and YAN, Y., 2018. Enhancing enzyme activity and enantioselectivity of Burkholderia cepacia lipase via immobilization on melamine-glutaraldehyde dendrimer modified magnetic nanoparticles. Chemical Engineering Journal, vol. 351, pp. 258-268. http://dx.doi.org/10.1016/j.cej.2018.06.086. http://dx.doi.org/10.1016/j.cej.2018.06.... )

Immobilization Method	Support material	Enzyme	Improved Enzyme Properties	Ref
Cross-Linking	Epoxy functionalized SBA-15	Carbonic anhydrase	Storage stability	(Fei et al., 2016FEI, X., CHEN, S., LIU, D., HUANG, C. and ZHANG, Y., 2016. Comparison of amino and epoxy functionalized SBA-15 used for carbonic anhydrase immobilization. Journal of Bioscience and Bioengineering, vol. 122, no. 3, pp. 314-321. http://dx.doi.org/10.1016/j.jbiosc.2016.02.004. PMid:27215831. http://dx.doi.org/10.1016/j.jbiosc.2016.... )
Cross-Linking	Aminoy Functionalized SBA-15	Carbonic anhydrase	Storage stability	(Fei et al., 2016FEI, X., CHEN, S., LIU, D., HUANG, C. and ZHANG, Y., 2016. Comparison of amino and epoxy functionalized SBA-15 used for carbonic anhydrase immobilization. Journal of Bioscience and Bioengineering, vol. 122, no. 3, pp. 314-321. http://dx.doi.org/10.1016/j.jbiosc.2016.02.004. PMid:27215831. http://dx.doi.org/10.1016/j.jbiosc.2016.... )
Encapsulation	Mesoporous Silica SBA- 15	Alkaline protease	Enzyme Activity	(Kumari et al., 2015KUMARI, A., KAUR, B., SRIVASTAVA, R. and SANGWAN, R.S., 2015. Isolation and immobilization of alkaline protease on mesoporous silica and mesoporous ZSM-5 zeolite materials for improved catalytic properties. Biochemistry and Biophysics Reports, vol. 2, pp. 108-114. http://dx.doi.org/10.1016/j.bbrep.2015.05.009. PMid:29124151. http://dx.doi.org/10.1016/j.bbrep.2015.0... )
Cross-linking	Mesoporous Silica SBA- 15	Lysozyme	PH Resistance	(Lynch et al., 2016LYNCH, M.M., LIU, J., NIGRA, M. and COPPENS, M.-O., 2016. Chaperonin-inspired pH protection by mesoporous silica SBA-15 on myoglobin and lysozyme. Langmuir, vol. 32, no. 37, pp. 9604-9610. http://dx.doi.org/10.1021/acs.langmuir.6b02832. PMid:27564659. http://dx.doi.org/10.1021/acs.langmuir.6... )
Covalent bond	Aminofunctionalized SBA-15	Laccase	Biodegradation	(Bautista et al., 2015BAUTISTA, L. F., MORALES, G. and SANZ, R., 2015. Biodegradation of polycyclic aromatic hydrocarbons (PAHs) by laccase from Trametes versicolor covalently immobilized on amino-functionalized SBA-15. Chemosphere, 136, 273-280. https://doi.org/10.1016/j.chemosphere.2015.05.071. https://doi.org/10.1016/j.chemosphere.20... )
Adsorption	Mesoporous Silica SBA- 15	Candida rugosa lipase	Affinity and thermostability	(Živković et al., 2015ŽIVKOVIĆ, L.T.I., ŽIVKOVIĆ, L.S., BABIĆ, B.M., KOKUNEŠOSKI, M.J., JOKIĆ, B.M. and KARADŽIĆ, I.M., 2015. Immobilization of Candida rugosa lipase by adsorption onto biosafe meso/macroporous silica and zirconia. Biochemical Engineering Journal, vol. 93, pp. 73-83. http://dx.doi.org/10.1016/j.bej.2014.09.012. http://dx.doi.org/10.1016/j.bej.2014.09.... )
Adsorption	Mesoporous Silica SBA- 15	Candida antarctica Lipase B	Enzyme activity and stability	(Cai et al., 2016CAI, C., GAO, Y., LIU, Y., ZHONG, N. and LIU, N., 2016. Immobilization of Candida antarctica lipase B onto SBA-15 and their application in glycerolysis for diacylglycerols synthesis. Food Chemistry, vol. 212, pp. 205-212. http://dx.doi.org/10.1016/j.foodchem.2016.05.167. PMid:27374525. http://dx.doi.org/10.1016/j.foodchem.201... )
Covalent bond	Amino acid modified S BA-15	Porcine pancreases lipase	Heat resistance	(Zou et al., 2013ZOU, B., HU, Y., JIANG, L., JIA, R., and HUANG, H., 2013. Mesoporous material SBA-15 modified by amino acid ionic liquid to immobilize lipase via ionic bonding and cross-linking method. Industrial & Engineering Chemistry Research, vol. 52, no. 8, pp. 2844-2851.)
Adsorption	Magnetic Fe₃O₄/SBA-15	Candida rugosa lipase	Easily separated	(Rios et al., 2016RIOS, N.S., PINHEIRO, M.P., DOS SANTOS, J.C.S., FONSECA, T.S., LIMA, L.D., DE MATTOS, M.C., FREIRE, D.M., DA SILVA JÚNIOR, I.J., RODRÍGUEZ-AGUADO, E. and GONCALVES, L.R., 2016. Strategies of covalent immobilization of a recombinant Candida antarctica lipase B on pore-expanded SBA-15 and its application in the kinetic resolution of (R, S)-Phenylethyl acetate. Journal of Molecular Catalysis. B, Enzymatic, vol. 133, pp. 246-258. http://dx.doi.org/10.1016/j.molcatb.2016.08.009. http://dx.doi.org/10.1016/j.molcatb.2016... )
Adsorption	Mesoporous Silica SBA- 15	Candida antarctica lipase B	Thermal stability	(Rios et al., 2016RIOS, N.S., PINHEIRO, M.P., DOS SANTOS, J.C.S., FONSECA, T.S., LIMA, L.D., DE MATTOS, M.C., FREIRE, D.M., DA SILVA JÚNIOR, I.J., RODRÍGUEZ-AGUADO, E. and GONCALVES, L.R., 2016. Strategies of covalent immobilization of a recombinant Candida antarctica lipase B on pore-expanded SBA-15 and its application in the kinetic resolution of (R, S)-Phenylethyl acetate. Journal of Molecular Catalysis. B, Enzymatic, vol. 133, pp. 246-258. http://dx.doi.org/10.1016/j.molcatb.2016.08.009. http://dx.doi.org/10.1016/j.molcatb.2016... )
Cross-linking	SBA-15-LIPB-GA	Candida antarctica lipase B	High activity and stability	(Rios et al., 2018RIOS, N.S., PINHEIRO, M.P., LIMA, M.L.B., FREIRE, D.M.G., DA SILVA JÚNIOR, I.J., RODRÍGUEZ-CASTELLÓN, E., DE SANT’ANA, H.B., MACEDO, A.C. and GONÇALVES, L.R.B., 2018. Pore-expanded SBA-15 for the immobilization of a recombinant Candida antarctica lipase B: application in esterification and hydrolysis as model reactions. Chemical Engineering Research & Design, vol. 129, pp. 12-24. http://dx.doi.org/10.1016/j.cherd.2017.10.032. http://dx.doi.org/10.1016/j.cherd.2017.1... )
Cross-linking	NH₂-SBA-15	Acetylcholinesterase	Immobilization efficiency	(Rui et al., 2018RUI, Y., WU, X., MA, B. and XU, Y., 2018. Immobilization of acetylcholinesterase on functionalized SBA-15 mesoporous molecular sieve for detection of organophosphorus and carbamate pesticide. Chinese Chemical Letters, vol. 29, no. 9, pp. 1387-1390.)
Covalent bond	Mesoporous SBA-15 silica	Polyphenol oxidase	Enzyme efficiency	(Escuin et al., 2017ESCUIN, P. C., GARCÍA-BENNETT, A., ROS-LIS, J. V., FOIX, A. A., and ANDRÉS, A. J., 2017. Application of mesoporous silica materials for the immobilization of polyphenol oxidase. Food Chemistry, vol. 217, pp. 360-363. http://dx.doi.org/10.1016/j.foodchem.2016.08.02. http://dx.doi.org/10.1016/j.foodchem.201... )
Covalent bond	Ionic Liquids Modified SBA-15	Candida antarctica Lipase B	Enzymatic activity	(Zhong et al., 2018ZHONG, N., LI, Y., CAI, C., GAO, Y., LIU, N., LIU, G., TAN, W. and ZENG, Y., 2018. Enhancing the catalytic performance of Candida Antarctica lipase B by immobilization onto the ionic liquids modified SBA‐15. European Journal of Lipid Science and Technology, vol. 120, no. 4, pp. 1700357. http://dx.doi.org/10.1002/ejlt.201700357. http://dx.doi.org/10.1002/ejlt.201700357... )

Immobilization Method	Support material	Enzyme	Improved Enzyme Properties	Ref
Covalent Bond	Alanine Functionalized MCM-41	DL-Alanine functionalized MCM-41 catalyst	Substrate Selectivity	(Gkaniatsou et al., 2018GKANIATSOU, E., SICARD, C., RICOUX, R., BENAHMED, L., BOURDREUX, F., ZHANG, Q., SERRE, C., MAHY, J.P. and STEUNOU, N., 2018. Enzyme encapsulation in mesoporous metal–organic frameworks for selective biodegradation of harmful dye molecules. Angewandte Chemie, vol. 130, no. 49, pp. 16141-16146. http://dx.doi.org/10.1002/ange.201811327. PMid:30307095. http://dx.doi.org/10.1002/ange.201811327... )
Encapsulation	CPS/GO-Fe₃O₄@MCM-41	Porcine pancreas lipase	Reusability	(Mahto et al., 2016MAHTO, T.K., CHOWDHURI, A.R., SAHOO, B. and SAHU, S.K., 2016. Polyaniline‐functionalized magnetic mesoporous nanocomposite: A smart material for the immobilization of lipase. Polymer Composites, vol. 37, no. 4, pp. 1152-1160. http://dx.doi.org/10.1002/pc.23278. http://dx.doi.org/10.1002/pc.23278... )
Covalent Bond	MCM-41 coated with polyethylenimine	Rmomyces lanuginosa lipase	Stability and reusability	(Gao et al., 2017aGAO, J., YU, H., ZHOU, L., HE, Y., MA, L. and JIANG, Y., 2017a. Formation of cross-linked nitrile hydratase aggregates in the pores of tannic-acid-templated magnetic mesoporous silica: characterization and catalytic application. Biochemical Engineering Journal, vol. 117, no. Pt A, pp. 92-101. http://dx.doi.org/10.1016/j.bej.2016.10.005. http://dx.doi.org/10.1016/j.bej.2016.10.... )
Encapsulation	Fe₃O₄ -MCM-41	Candida rugosa lipase	Enzyme Activity	(Yang et al., 2018YANG, Y., WANG, S., ZHOU, Z., ZHANG, R., SHEN, H., SONG, J., SU, P. and YANG, Y., 2018. Enhanced reusability and activity: DNA directed immobilization of enzyme on polydopamine modified magnetic nanoparticles. Biochemical Engineering Journal, vol. 137, pp. 108-115. http://dx.doi.org/10.1016/j.bej.2018.05.019. http://dx.doi.org/10.1016/j.bej.2018.05.... )

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[1] ^#The authors contributed equally to the work.