Covalent immobilization of lipases on monodisperse magnetic microspheres modified with PAMAM-dendrimer
Source abstract
Abstract
This paper reported an immobilization of Candida rugosa lipase (CRL) onto PAMAM-dendrimer-grafted magnetic nanoparticles synthesized by a modified solvothermal reduction method. The dendritic magnetic nanoparticles were amply characterized by several instrumental measurements, and the CRL was covalently anchored on the three generation supports with glutaraldehyde as coupling reagent. The amount of immobilized enzyme was up to 150 mg/g support and the factors related with the enzyme activity were investigated. The immobilization of lipase improved their performance in wider ranges of pH and temperature. The immobilized lipase exhibited excellent thermal stability and reusability in comparison with free enzyme and can be reused 10 cycles with the enzymatic activity remained above 90 %. The properties of lipase improved obviously after being immobilized on the dendritic supports. The inactive immobilized lipase could be regenerated with glutaraldehyde and Cu2+, respectively. This synthetic strategy was facile and eco-friendly for applications in lipase immobilization.
Source: openaire · Quality: candidate unverified · Source record ↗
Research context
OpenAlex topics: Enzyme Catalysis and Immobilization · Electrochemical sensors and biosensors · Dendrimers and Hyperbranched Polymers
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
References (42)
Show source-provided references
1. Bagheri M, Rodríguez H, Swatloski RP, Spear SK, Daly DT, Rogers RD (2008) Ionic liquid-based preparation of cellulose-dendrimer films as solid supports for enzyme immobilization. Biomacromolecules 9:381–38710.1021/bm701023w ↗
2. Barbosa O, Torres R, Ortiz C, Berenguer-Murcia A, Rodrigues RC, Fernandez-Lafuente R (2013) Heterofunctional supports in enzyme immobilization: from traditional immobilization protocols to opportunities in tuning enzyme properties. Biomacromolecules 14:2433–246210.1021/bm400762h ↗
3. Barbosa O, Ortiz C, Berenguer-Murcia A, Torres R, Rodrigues RC, Fernandez-Lafuente R (2014) Glutaraldehyde in bio-catalysts design: a useful crosslinker and a versatile tool in enzyme immobilization. RSC Adv 4:1583–160010.1039/C3RA45991H ↗
4. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–25410.1016/0003-2697(76)90527-3 ↗
5. Brady D, Jordaan J (2009) Advances in enzyme immobilization. Biotechnol Lett 31:1639–165010.1007/s10529-009-0076-4 ↗
6. Bronstein LM, Shifrina ZB (2009) Nanoparticles in dendrimers: from synthesis to application. Nanotechnol Russ 4:576–60810.1134/S1995078009090031 ↗
7. Choudhury AK, Kitaoka M, Hayashi K (2003) Synthesis of a cellobiosylated dimer and trimer and of cellobiose-coated polyamidoamine (PAMAM) dendrimers to study accessibility of an enzyme, cellodextrin phosphorylase. Eur J Org Chem 2003:2462–247010.1002/ejoc.200300018 ↗
8. Crespilho FN, Ghica ME, Florescu M, Nart FC, Oliveira ON, Brett CM (2006) A strategy for enzyme immobilization on layer-by-layer dendrimer-gold nanoparticle electrocatalytic membrane incorporating redox mediator. Electrochem Commun 8:1665–167010.1016/j.elecom.2006.07.032 ↗
9. Crooks RM, Zhao M, Sun L, Chechik V, Yeung LK (2001) Dendrimer-encapsulated metal nanoparticles: synthesis, characterization, and applications to catalysis. Acc Chem Res 34:181–19010.1021/ar000110a ↗
10. Demircioǧlu H, Beyenal H, Tanyolaç A, Hasirci N (1994) Immobilization of urease and estimation of effective diffusion coefficients of urea in HEMA and VP copolymer matrices. Polym Int 35:321–32710.1002/pi.1994.210350404 ↗
11. Deng H, Li XL, Peng Q, Wang X, Chen JP, Li YD (2005) Soft nanotechnology with soft nanoparticles. Angew Chem Int Ed 44:278210.1002/anie.200462551 ↗
12. Garcia J, Zhang Y, Taylor H, Cespedes O, Webb ME, Zhou DJ (2011) Multilayer enzyme-coupled magnetic nanoparticles as efficient, reusable biocatalysts and biosensors. Nanoscale 3:3721–373010.1039/c1nr10411j ↗
13. Gardossi L, Bianchi D, Klibanov AM (1991) Selective acylation of peptides catalyzed by lipases in organic solvents. J Am Chem Soc 113:6328–632910.1021/ja00016a091 ↗
14. Grayson SM, Frechet JMJ (2001) Convergent dendrons and dendrimers: from synthesis to applications. Chem Rev 101:3819–386810.1021/cr990116h ↗
15. Gupta MN, Kaloti M, Kapoor M, Solanki K (2011) Nanomaterials as matrices for enzyme immobilization. Artif Cells Blood Substit Biotechnol 39:98–10910.3109/10731199.2010.516259 ↗
16. Hartmann M, Jung D (2010) Biocatalysis with enzymes immobilized on mesoporous hosts: the status quo and future trends. J Mater Chem 20:844–85710.1039/B907869J ↗
17. Hong J, Xu D, Gong P, Sun H, Dong L, Yao S (2007) Covalent binding of α-chymotrypsin on the magnetic nanogels covered by amino groups. J Mol Catal B Enzym 45:84–9010.1016/j.molcatb.2006.11.009 ↗
18. Hou C, Zhu H, Wu D, Li Y, Hou K, Jiang Y, Li Y (2014) Immobilized lipase on macroporous polystyrene modified by PAMAM-dendrimer and their enzymatic hydrolysis. Process Biochem 49:244–24910.1016/j.procbio.2013.10.019 ↗
19. Jaeger KE, Reetz MT (1998) Microbial lipases form versatile tools for biotechnology. Trends Biotechnol 16:396–40310.1016/S0167-7799(98)01195-0 ↗
20. Jiang DS, Long SY, Huang J, Xiao HY, Zhou JY (2005) Immobilization of Pycnoporus sanguineus laccase on magnetic chitosan microspheres. Biochem Eng J 25:15–2310.1016/j.bej.2005.03.007 ↗
21. Kunzmann A, Andersson B, Thurnherr T, Krug H, Scheynius A, Fadeel B, Scheyniusb A, Fadeel B et al (2011) Toxicology of engineered nanomaterials: focus on biocompatibility, biodistribution and biodegradation. BBA 1810:361–373
22. Li X, Zhu H, Feng J, Zhang J, Deng X, Zhou B,…, Peng Y (2013) One-pot polylol synthesis of graphene decorated with size-and density-tunable Fe3O4 nanoparticles for porcine pancreatic lipase immobilization. Carbon 60:488–49710.1016/j.carbon.2013.04.068 ↗
23. Mateo C, Palomo JM, Fernandez-Lorente G, Guisan JM, Fernandez-Lafuente R (2007) Improvement of enzyme activity, stability and selectivity via immobilization techniques. Enzym Microb Technol 40:1451–146310.1016/j.enzmictec.2007.01.018 ↗
24. Migneault I, Dartiguenave C, Bertrand MJ, Waldron KC (2004) Glutaraldehyde: behavior in aqueous solution, reaction with proteins, and application to enzyme crosslinking. Biotechniques 37:790–80610.2144/04375RV01 ↗
25. Monsan P (1978) Optimization of glutaraldehyde activation of a support for enzyme immobilization. J Mol Catal A 3:371–38410.1016/0304-5102(78)80026-1 ↗
26. Narayanan VV, Newkome GR (1998) Supramolecular chemistry within dendritic structures. Top Curr Chem 197:19–7710.1007/3-540-69779-9_2 ↗
27. Omprakash Y, Toyoko I (2005) Covalent-bonded immobilization of lipase on poly (phenylene sulfide) dendrimers and their hydrolysis ability. Biomacromolecules 6:2809–281410.1021/bm050285d ↗
28. Pahujani S, Kanwar S, Chauhan G, Gupta R (2008) Glutaraldehyde activation of polymer Nylon-6 for lipase immobilization: enzyme characteristics and stability. Bioresour Technol 99:2566–257010.1016/j.biortech.2007.04.042 ↗
29. Pfaff A, Müller AH (2011) Hyperbranched glycopolymer grafted microspheres. Macromolecules 44:1266–127210.1021/ma102794z ↗
30. Rodrigues RC, Ortiz C, Berenguer-Murcia A, Torres R, Fernández-Lafuente R (2013) Modifying enzyme activity and selectivity by immobilization. Chem Soc Rev 42:6290–630710.1039/C2CS35231A ↗
31. Schlüter AD, Rabe JP (2000) Dendronized polymers: synthesis, characterization, assembly at interfaces, and manipulation. Angew Chem Int Ed 39:864–88310.1002/(SICI)1521-3773(20000303)39:5<864::AID-ANIE864>3.0.CO;2-E ↗
32. Tomalia DA, Baker H, Dewald J, Hall M, Kallos G, Martin S, Smith P (1985) A new class of polymers: starburst-dendritic macromolecules. Polym J 17:117–13210.1295/polymj.17.117 ↗
33. Uzun K, Çevik E, Şenel M, Sözeri H, Baykal A, Abasıyanık MF, Toprak MS (2010) Covalent immobilization of invertase on PAMAM-dendrimer modified superparamagnetic iron oxide nanoparticles. J Nanopart Res 12:3057–306710.1007/s11051-010-9902-9 ↗
34. Vertegel AA, Siegel RW, Dordick JS (2004) Silica nanoparticle size influences the structure and enzymatic activity of adsorbed lysozyme. Langmuir 20:6800–680710.1021/la0497200 ↗
35. Wang P (2006) Nanoscale biocatalyst systems. Curr Opin Biotechnol 17:574–57910.1016/j.copbio.2006.10.009 ↗
36. Wang Y, Caruso F (2005) Mesoporous silica spheres as supports for enzyme immobilization and encapsulation. J Chem Mater 17:953–96110.1021/cm0483137 ↗
37. Wang S, Su P, Ding F, Yang Y (2013) Immobilization of ellulose on polyamidoamine dendrimer-grafted silica. J Mol Catal B Enzym 89:35–4010.1016/j.molcatb.2012.12.011 ↗
38. Watanabe N, Ota Y, Minoda Y, Yamada K (1977) Isolation and identification of alkaline lipase producing microorganisms, cultural conditions and some properties of crude enzymes. Agric Biol Chem 41:1353–135810.1271/bbb1961.41.1353 ↗
39. Zhao G, Wang J, Li Y, Chen X, Liu Y (2011) Enzymes immobilized on superparamagnetic Fe3O4@ clays nanocomposites: preparation, characterization, and a new strategy for the regeneration of supports. J Phys Chem C 115:6350–635910.1021/jp200156j ↗
40. Zhong T, Ai P, Zhou J (2011) Structures and properties of PAMAM dendrimer: a multi-scale simulation study. Fluid Phase Equilib 302:43–4710.1016/j.fluid.2010.09.037 ↗
41. Zhu H, Hou C, Li Y, Zhao G, Liu X, Hou K, Li Y (2013) One-pot solvothermal synthesis of highly water-dispersible size-tunable functionalized magnetite nanocrystal clusters for lipase immobilization. Chem Asian J 8:1447–145410.1002/asia.201300026 ↗
42. Zucca P, Sanjust E (2014) Inorganic materials as supports for covalent enzyme immobilization: methods and mechanisms. Molecules 19:14139–1419410.3390/molecules190914139 ↗