Facile, high efficiency immobilization of lipase enzyme on magnetic iron oxide nanoparticles via a biomimetic coating
Open accessAbstract
BACKGROUND: Immobilization of lipase on appropriate solid supports is one way to improve their stability and activity, and can be reused for large scale applications. A sample, cost- effective and high loading capacity method is still challenging. RESULTS: A facile method of lipase immobilization was developed in this study, by the use of polydopamine coated magnetic nanoparticles (PD-MNPs). Under optimal conditions, 73.9% of the available lipase was immobilized on PD-MNPs, yielding a lipase loading capacity as high as 429 mg/g. Enzyme assays revealed that lipase immobilized on PD-MNPs displayed enhanced pH and thermal stability compared to free lipase. Furthermore, lipase immobilized on PD-MNPs was easily isolated from the reaction medium by magnetic separation and retained more than 70% of initial activity after 21 repeated cycles of enzyme reaction followed by magnetic separation. CONCLUSIONS: Immobilization of enzyme onto magnetic iron oxide nanoparticles via poly-dopamine film is economical, facile and efficient.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Biomacromolecules such as proteins, peptides, and DNA can anchor on the surface of biosubstitutes via the polydopamine coating layer.
“In addition, biomacromolecules, such as proteins, peptides, and DNA, can anchor on the surface of biosubstitutes via the PDA coating layer [50, 57–60].”
From Polydopamine-Assisted Surface Modification for Bone Biosubstitutes (2016) · cites this paper as [60]
The Background and Results and discussion (‘Lipase immobilization onto PD-MNPs’; page unavailable) say that polydopamine coatings immobilize biomolecules and demonstrate attachment of lipase, a protein, to magnetic iron oxide nanoparticles. Our copy does not specifically establish attachment of peptides or DNA, or address surfaces described as ‘biosubstitutes.’ (LLM, conf=0.85)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302 · see citing works
Mussel-inspired surface chemistry for multifunctional coatings
Lee, H., Dellatore, S. M., Miller, W. M., & Messersmith, P. B. (2007) · Science · doi:10.1126/science.1147241 · Cited by 10,965 · see citing works
Self-citationImprovement of enzyme activity, stability and selectivity via immobilization techniques
Mateo, C., Palomo, J. M., Fernández‐Lorente, G., Guisan, J. M., & Fernández‐Lafuente, R. (2007) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2007.01.018 · Cited by 3,385 · see citing works
Single-molecule mechanics of mussel adhesion
Lee, H., Scherer, N. F., & Messersmith, P. B. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605552103 · Cited by 2,112 · see citing works
Self-citationFacile Conjugation of Biomolecules onto Surfaces via Mussel Adhesive Protein Inspired Coatings
Lee, H., Rho, J., & Messersmith, P. B. (2009) · Advanced Materials · doi:10.1002/adma.200801222 · Cited by 1,495 · see citing works
Self-citationXu, C., Xu, K., Gu, H., Zheng, R., Liu, H., Zhang, X., Guo, Z., & Xu, B. (2004) · Journal of the American Chemical Society · doi:10.1021/ja0464802 · Cited by 886 · see citing works
Immobilised enzymes: science or art?
Cao, L. (2005) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2005.02.014 · Cited by 634 · see citing works
Iron oxide nanoparticles–chitosan composite based glucose biosensor
Kaushik, A. K., Khan, R., Solanki, P. R., Pandey, P., Alam, J., Ahmad, S., & Malhotra, B. D. (2008) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2008.06.032 · Cited by 462 · see citing works
Amstad, E., Gillich, T., Bilecka, I., Textor, M., & Reimhult, E. (2009) · Nano Letters · doi:10.1021/nl902212q · Cited by 454 · see citing works
Magnetic Nanoparticles and Their Applications in Medicine
Duguet, É., Vasseur, S., Mornet, S., & Devoisselle, J. (2006) · Nanomedicine · doi:10.2217/17435889.1.2.157 · Cited by 396 · see citing works
Multifunctional magnetic nanoparticles for medical imaging applications
Fang, C., & Zhang, M. (2009) · Journal of Materials Chemistry · doi:10.1039/b902182e · Cited by 315 · see citing works
Jiang, Y., Guo, C., Xia, H., Mahmood, I., Liu, C., & Liu, H. (2008) · Journal of Molecular Catalysis B Enzymatic · doi:10.1016/j.molcatb.2008.12.001 · Cited by 262 · see citing works
Targeted Delivery of Multifunctional Magnetic Nanoparticles
McCarthy, J. R., Kelly, K. A., Sun, E. Y., & Weissleder, R. (2007) · Nanomedicine · doi:10.2217/17435889.2.2.153 · Cited by 254 · see citing works
Wu, Y., Wang, Y., Luo, G., & Dai, Y. (2009) · Bioresource Technology · doi:10.1016/j.biortech.2009.02.018 · Cited by 195 · see citing works
Immobilization of lipase on hydrophobic nano-sized magnetite particles
Lee, D. G., Ponvel, K. M., Kim, M., Hwang, S., Ahn, I., & Lee, C. (2008) · Journal of Molecular Catalysis B Enzymatic · doi:10.1016/j.molcatb.2008.06.017 · Cited by 167 · see citing works
Self-citationCharacterization of Candida rugosa lipase immobilized onto magnetic microspheres with hydrophilicity
Yong, Y., Bai, Y., Li, Y., Lei, L., Cui, Y., & Xia, C. (2008) · Process Biochemistry · doi:10.1016/j.procbio.2008.05.019 · Cited by 147 · see citing works
Zhang, L., Xue, H., Gao, C., Carr, L. R., Wang, J., Chu, B., & Jiang, S. (2010) · Biomaterials · doi:10.1016/j.biomaterials.2010.05.018 · Cited by 127 · see citing works
Study on immobilization of lipase onto magnetic microspheres with epoxy groups
Lei, L., Bai, Y., Li, Y., Yi, L.-X., Yang, Y., & Xia, C. (2008) · Journal of Magnetism and Magnetic Materials · doi:10.1016/j.jmmm.2008.08.047 · Cited by 116 · see citing works
Liu, Y., & Simon, J. D. (2003) · Pigment Cell Research · doi:10.1034/j.1600-0749.2003.00009.x · Cited by 115 · see citing works
Immobilization of lipases for non-aqueous synthesis
Petkar, M., Lali, A. M., Caimi, P., & Daminati, M. (2006) · Journal of Molecular Catalysis B Enzymatic · doi:10.1016/j.molcatb.2006.01.034 · Cited by 113 · see citing works
Lipase immobilization on modified zirconia nanoparticles: Studies on the effects of modifiers
Chen, Y. Z., Ching, C. B., & Xu, R. Q. (2009) · Process Biochemistry · doi:10.1016/j.procbio.2009.06.023 · Cited by 41 · see citing works
Bhushan, I., Parshad, R., Qazi, G. N., Ingavle, G. C., Rajan, C. R., Ponrathnam, S., & Gupta, V. K. (2008) · Process Biochemistry · doi:10.1016/j.procbio.2007.11.019 · Cited by 31 · see citing works
Wu, J. C., Ho, P., Poh, T. Y., Chow, Y. Y. S., Talukder, M., & Choi, W. J. (2007) · Korean Journal of Chemical Engineering · doi:10.1007/s11814-007-0018-6 · Cited by 7 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Non‐Covalent Self‐Assembly and Covalent Polymerization Co‐Contribute to Polydopamine Formation
Hong, S., Na, Y. S., Choi, S., Song, I. T., Kim, W. Y., & Lee, H. (2012) · Advanced Functional Materials · doi:10.1002/adfm.201201156 · Cited by 1,352 · see citing works
Structure of Polydopamine: A Never-Ending Story?
Liebscher, J., Mrówczyński, R., Scheidt, H. A., Filip, C., Hădade, N. D., Turcu, R., Bende, A., & Beck, S. (2013) · Langmuir · doi:10.1021/la4020288 · Cited by 1,058 · see citing works
Microbial lipases and their industrial applications: a comprehensive review
Chandra, P., Enespa, Singh, R. P., & Arora, P. K. (2020) · Microbial Cell Factories · doi:10.1186/s12934-020-01428-8 · Cited by 922 · see citing works
Surface Modification of Water Purification Membranes
Miller, D. J., Dreyer, D. R., Bielawski, C. W., Paul, D. R., & Freeman, B. D. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201601509 · Cited by 749 · see citing works
Recent approaches in designing bioadhesive materials inspired by mussel adhesive protein
Kord Forooshani, P., & Lee, B. P. (2017) · Journal of Polymer Science Part A: Polymer Chemistry · doi:10.1002/pola.28368 · Cited by 632 · see citing works
Magnetic nanoparticles as versatile carriers for enzymes immobilization: A review
Bilal, M., Zhao, Y., Rasheed, T., & Iqbal, H. M. N. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.09.025 · Cited by 485 · see citing works
Wu, W. H., Jiang, C., & Roy, V. A. L. (2016) · Nanoscale · doi:10.1039/c6nr07542h · Cited by 420 · see citing works
Polydopamine-Based Simple and Versatile Surface Modification of Polymeric Nano Drug Carriers
Park, J., Brust, T. F., Lee, H. J., Lee, S. C., Watts, V. J., & Yeo, Y. (2014) · ACS Nano · doi:10.1021/nn405809c · Cited by 407 · see citing works
Zhao, X., Qi, F., Yuan, C., Du, W., & Liu, D. (2015) · Renewable and Sustainable Energy Reviews · doi:10.1016/j.rser.2014.12.021 · Cited by 392 · see citing works
Du, X. Z., Li, L. X., Li, J. S., Yang, C., Frenkel, N., Welle, A., Heißler, S., Nefedov, A., Grunze, M., & Levkin, P. A. (2014) · Advanced Materials · doi:10.1002/adma.201403709 · Cited by 370 · see citing works
Superparamagnetic nanoparticles as versatile carriers and supporting materials for enzymes
Netto, C. G. C. M., Toma, H. E., & Andrade, L. H. (2012) · Journal of Molecular Catalysis B Enzymatic · doi:10.1016/j.molcatb.2012.08.010 · Cited by 322 · see citing works
Bohara, R. A., Thorat, N. D., & Pawar, S. H. (2016) · RSC Advances · doi:10.1039/c6ra02129h · Cited by 279 · see citing works
Verma, M. L., Barrow, C. J., & Puri, M. (2012) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-012-4535-9 · Cited by 278 · see citing works
Darwesh, O. M., Matter, I. A., & Eida, M. (2018) · Journal of environmental chemical engineering · doi:10.1016/j.jece.2018.11.049 · Cited by 219 · see citing works
Sigurdardóttir, S. B., Lehmann, J., Ovtar, S., Grivel, J. ‐., Negra, M. D., Kaiser, A., & Pinelo, M. (2018) · Advanced Synthesis & Catalysis · doi:10.1002/adsc.201800307 · Cited by 212 · see citing works
Recent trends in nanomaterials immobilised enzymes for biofuel production
Verma, M. L., Puri, M., & Barrow, C. J. (2014) · Critical Reviews in Biotechnology · doi:10.3109/07388551.2014.928811 · Cited by 207 · see citing works
Chaudhari, D. S., Upadhyay, R. P., Shinde, G. Y., Gawande, M. B., Filip, J., Varma, R. S., & Zbořil, R. (2024) · Green Chemistry · doi:10.1039/d4gc01870b · Cited by 200 · see citing works
The Present and Future of Biologically Inspired Adhesive Interfaces and Materials
Brubaker, C. E., & Messersmith, P. B. (2012) · Langmuir · doi:10.1021/la300044v · Cited by 178 · see citing works
Self-citationImmobilized Biocatalysts: Novel Approaches and Tools for Binding Enzymes to Supports
Torres, P., del Monte‐Martínez, A., Cutiño‐Avila, B., Rodríguez-Colinas, B., Alcalde, M., Ballesteros, A. O., & Plou, F. J. (2011) · Advanced Materials · doi:10.1002/adma.201101821 · Cited by 174 · see citing works
Wu, M., Zhang, D., Zeng, Y., Wu, L., Liu, X., & Liu, J. (2015) · Nanotechnology · doi:10.1088/0957-4484/26/11/115102 · Cited by 166 · see citing works
Luong, D., Sau, S., Kesharwani, P., & Iyer, A. K. (2017) · Biomacromolecules · doi:10.1021/acs.biomac.6b01885 · Cited by 159 · see citing works
A review on the important aspects of lipase immobilization on nanomaterials
Shuai, W., Das, R. K., Naghdi, M., Brar, S. K., & Verma, M. (2016) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.1515 · Cited by 152 · see citing works
Cheng, L., Sun, X., Zhao, X., Wang, L., Yu, J., Pan, G., Li, B., Yang, H., Zhang, Y., & Cui, W. (2016) · Biomaterials · doi:10.1016/j.biomaterials.2016.01.002 · Cited by 149 · see citing works
Robust, self-healing hydrogels synthesised from catechol rich polymers
Yavvari, P. S., & Srivastava, A. (2015) · Journal of Materials Chemistry B · doi:10.1039/c4tb01307g · Cited by 126 · see citing works
Shalev, T., Gopin, A., Bauer, M., Stark, R. W., & Rahimipour, S. (2012) · J. Mater. Chem. · doi:10.1039/c1jm13994k · Cited by 126 · see citing works
N-Terminal Modification of Proteins with o -Aminophenols
Obermeyer, A. C., Jarman, J. B., & Francis, M. B. (2014) · Journal of the American Chemical Society · doi:10.1021/ja500728c · Cited by 124 · see citing works
Kumari, B., & Singh, D. P. (2016) · Ecological Engineering · doi:10.1016/j.ecoleng.2016.08.006 · Cited by 124 · see citing works
Developing Antibacterial Nanocrystalline Cellulose Using Natural Antibacterial Agents
Tavakolian, M., Okshevsky, M., van de Ven, T. G. M., & Tufenkji, N. (2018) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.8b08770 · Cited by 120 · see citing works
POTENTIAL APPLICATIONS OF CHITOSAN NANOPARTICLES AS NOVEL SUPPORT IN ENZYME IMMOBILIZATION
Kouachi (2012) · American journal of biochemistry & biotechnology/American journal of biochemistry and biotechnology · doi:10.3844/ajbbsp.2012.203.219 · Cited by 118 · see citing works
Nanomaterials engineering for drug delivery: a hybridization approach
Mohammadi, M. R., Nojoomi, A., Mozafari, M., Dubņika, A., Inayathullah, M., & Rajadas, J. (2017) · Journal of Materials Chemistry B · doi:10.1039/c6tb03247h · Cited by 113 · see citing works
Touqeer, T., Mumtaz, M. W., Mukhtar, H., Irfan, A., Akram, S., Shabbir, A., Rashid, U., Nehdi, I. A., & Choong, T. S. Y. (2019) · Energies · doi:10.3390/en13010177 · Cited by 105 · see citing works
Aguilar‐Ferrer, D., Szewczyk, J., & Coy, E. L. (2021) · Catalysis Today · doi:10.1016/j.cattod.2021.08.016 · Cited by 105 · see citing works
Yeroslavsky, G., Girshevitz, O., Foster-Frey, J. A., Donovan, D. M., & Rahimipour, S. (2014) · Langmuir · doi:10.1021/la503911m · Cited by 104 · see citing works
Recent advances in immobilized enzymes on nanocarriers
Cao, S., Xu, P., Ma, Y., Yao, X., Yao, Y., Zong, M., Li, X., & Lou, W. (2016) · CHINESE JOURNAL OF CATALYSIS (CHINESE VERSION) · doi:10.1016/s1872-2067(16)62528-7 · Cited by 104 · see citing works
Oberflächenmodifizierung von Wasseraufbereitungsmembranen
Miller, D. J., Dreyer, D. R., Bielawski, C. W., Paul, D. R., & Freeman, B. D. (2016) · Angewandte Chemie · doi:10.1002/ange.201601509 · Cited by 104 · see citing works
Green synthesis of iron nanoparticles: Sources and multifarious biotechnological applications
Kumar, V., Kaushik, N. K., Tiwari, S. K., Singh, D., & Singh, B. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.127017 · Cited by 102 · see citing works
Liu, J., Ma, R.-T., & Shi, Y. (2019) · Analytica Chimica Acta · doi:10.1016/j.aca.2019.11.073 · Cited by 98 · see citing works
Biomedical and Clinical Importance of Mussel-Inspired Polymers and Materials
Kaushik, N. K., Kaushik, N., Pardeshi, S., Sharma, J., Lee, S., & Choi, E. H. (2015) · Marine Drugs · doi:10.3390/md13116792 · Cited by 98 · see citing works
Polydopamine-Assisted Surface Modification for Bone Biosubstitutes
Huang, S., Liang, N., Hu, Y., Zhou, X., & Abidi, N. (2016) · BioMed Research International · doi:10.1155/2016/2389895 · Cited by 97 · see citing works
“as proteins, peptides, and DNA, can anchor on the surface of biosubstitutes via the PDA coating layer [50, 57–60].”
BackgroundChen, C., Sun, W., Lv, H., Li, H., Wang, Y., & Wang, P. (2018) · Chemical Engineering Journal · doi:10.1016/j.cej.2018.06.008 · Cited by 97 · see citing works
Izrael-Živković, L., Živković, L. S., Babić, B., Kokunešoski, M., Jokic, B. M., & Karadžić, I. (2014) · Biochemical Engineering Journal · doi:10.1016/j.bej.2014.09.012 · Cited by 94 · see citing works
Asadpour‐Zeynali, K., & Mollarasouli, F. (2016) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2016.10.071 · Cited by 94 · see citing works
Oroujeni, M., Kaboudin, B., Xia, W., Jönsson, P. E., & Ossipov, D. A. (2017) · Progress in Organic Coatings · doi:10.1016/j.porgcoat.2017.10.007 · Cited by 93 · see citing works
Precise Control of Polydopamine Film Formation by Electropolymerization
Stöckle, B., Ng, D. Y. W., Meier, C. A., Paust, T., Bischoff, F., Diemant, T., Behm, R. J., Gottschalk, K., Ziener, U., & Weil, T. (2014) · Macromolecular Symposia · doi:10.1002/masy.201400130 · Cited by 90 · see citing works
Polydopamine—An Organocatalyst Rather than an Innocent Polymer
Mrówczyński, R., Bunge, A., & Liebscher, J. (2014) · Chemistry - A European Journal · doi:10.1002/chem.201402532 · Cited by 84 · see citing works
Cruz-Izquierdo, Á., Picó, E. A., López, C., Serra, J. L., & Llama, M. J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0115202 · Cited by 83 · see citing works
McCullum, C., Tchounwou, P. B., Ding, L., Liao, X., & Liu, Y. (2014) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf501659m · Cited by 83 · see citing works
Das, R., Talat, M., Srivastava, O. N., & Kayastha, A. M. (2017) · Food Chemistry · doi:10.1016/j.foodchem.2017.10.092 · Cited by 82 · see citing works
Ran, F., Zou, Y., Xu, Y., Liu, X., & Zhang, H. (2019) · Chemical Engineering Journal · doi:10.1016/j.cej.2019.121947 · Cited by 82 · see citing works
Dirigent proteins: molecular characteristics and potential biotechnological applications
Pickel, B., & Schaller, A. (2013) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-013-5167-4 · Cited by 80 · see citing works
Sonochemically produced polydopamine nanocapsules with selective antimicrobial activity
Yeroslavsky, G., Richman, M., Dawidowicz, L.-O., & Rahimipour, S. (2013) · Chemical Communications · doi:10.1039/c3cc37762h · Cited by 80 · see citing works
Progress in Enzymatic Biodiesel Production and Commercialization
Lv, L., Dai, L., Du, W., & Liu, D. (2021) · Processes · doi:10.3390/pr9020355 · Cited by 77 · see citing works
Polydopamine-based nanoreactors: synthesis and applications in bioscience and energy materials
Mei, S., Xu, X., Priestley, R. D., & Lu, Y. Q. (2020) · Chemical Science · doi:10.1039/d0sc04486e · Cited by 76 · see citing works
Carvalho, T., Pereira, A. D. S., Bonomo, R. C. F., Franco, M., Finotelli, P. V., & Amaral, P. F. F. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.05.174 · Cited by 75 · see citing works
Kanyong, P., Rawlinson, S., & Davis, J. (2016) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2016.04.099 · Cited by 74 · see citing works
Yeroslavsky, G., Lavi, R., Alishaev, A., & Rahimipour, S. (2016) · Langmuir · doi:10.1021/acs.langmuir.6b00576 · Cited by 74 · see citing works
Aghabeigi, F., Nikkhah, H., Zilouei, H., & Bazarganipour, M. (2023) · Process Biochemistry · doi:10.1016/j.procbio.2023.01.012 · Cited by 72 · see citing works
Wan, Q., Tian, J., Liu, M., Zeng, G., Huang, Q., Wang, K., Zhang, Q., Deng, F., Zhang, X., & Wei, Y. (2015) · Applied Surface Science · doi:10.1016/j.apsusc.2015.04.012 · Cited by 71 · see citing works
Nafiujjaman, M., Nurunnabi, M., Kang, S.-H., Reeck, G. R., Khan, H. A., & Lee, Y.-K. (2015) · Journal of Materials Chemistry B · doi:10.1039/c5tb00479a · Cited by 70 · see citing works
Andrade, M. F. C., Parussulo, A. L. A., Netto, C. G. C. M., Andrade, L. H., & Toma, H. E. (2016) · Biofuel Research Journal · doi:10.18331/brj2016.3.2.5 · Cited by 70 · see citing works
Biomimetic Nanomaterials: Diversity, Technology, and Biomedical Applications
Газинурович, Г. К., Grouzdev, D. S., Koziaeva, V. V., Sitkov, N. O., Gao, H., Zimina, T. M., & Shevtsov, M. A. (2022) · Nanomaterials · doi:10.3390/nano12142485 · Cited by 64 · see citing works
Forooshani, P. K., Polega, E., Thomson, K., Bhuiyan, M. S. A., Pinnaratip, R., Trought, M., Kendrick, C., Gao, Y., Perrine, K. A., Pan, L., et al. (2019) · Frontiers in Chemistry · doi:10.3389/fchem.2019.00631 · Cited by 63 · see citing works
New versatile polydopamine coated functionalized magnetic nanoparticles
Mrówczyński, R., Turcu, R., Leostean, C., Scheidt, H. A., & Liebscher, J. (2013) · Materials Chemistry and Physics · doi:10.1016/j.matchemphys.2012.11.059 · Cited by 62 · see citing works
Natural and bio-inspired underwater adhesives: Current progress and new perspectives
Cui, M., Ren, S., Wei, S., Sun, C., & Zhong, C. (2017) · APL Materials · doi:10.1063/1.4985756 · Cited by 62 · see citing works
Tan, Y., Ma, S., Liu, C., Yu, W., & Han, F. (2015) · Microbiological Research · doi:10.1016/j.micres.2015.06.001 · Cited by 62 · see citing works
Singh, V., Rakshit, K., Rathee, S., Angmo, S., Kaushal, S., Garg, P., Chung, J. H., Sandhir, R., Sangwan, R. S., & Singhal, N. K. (2016) · Bioresource Technology · doi:10.1016/j.biortech.2016.05.002 · Cited by 61 · see citing works
Shi, J., Wang, X., Jiang, Z., Liang, Y., Zhu, Y., & Zhang, C. (2012) · Bioresource Technology · doi:10.1016/j.biortech.2012.04.099 · Cited by 60 · see citing works
Tang, W., Chen, C., Sun, W., Wang, P., & Wei, D. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.01.161 · Cited by 60 · see citing works
Polydopamine – its Prolific Use as Catalyst and Support Material
Molnár, Á. (2019) · ChemCatChem · doi:10.1002/cctc.201902125 · Cited by 60 · see citing works
Shi, J., Wang, X., Zhang, W., Jiang, Z., Liang, Y., Zhu, Y., & Zhang, C. (2013) · Advanced Functional Materials · doi:10.1002/adfm.201202068 · Cited by 59 · see citing works
Kumar, S., Jana, A. K., Dhamija, I., Singla, Y., & Maiti, M. (2013) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2013.06.019 · Cited by 58 · see citing works
Robust nanocarriers to engineer nanobiocatalysts for bioprocessing applications
Bilal, M., Qamar, S. A., Ashraf, S. M., Rodríguez‐Couto, S., & Iqbal, H. M. N. (2021) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2021.102438 · Cited by 58 · see citing works
Recent applications and future prospects of magnetic biocatalysts
Melo, R. L. F., Sales, M. B., Bizerra, V. D. C., de Sousa, P. G., Cavalcante, A. L. G., Freire, T. M., Neto, F. S., Bilal, M., Jesionowski, T., Soares, J. M., et al. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.126709 · Cited by 54 · see citing works
Esmaeilnejad-Ahranjani, P., Kazemeini, M., Singh, G., & Arpanaei, A. (2015) · RSC Advances · doi:10.1039/c5ra02471d · Cited by 54 · see citing works
Synthesis of glycinamides using protease immobilized magnetic nanoparticles
Sahu, A., Badhe, P., Adivarekar, R. V., Ladole, M. R., & Pandit, A. B. (2016) · Biotechnology Reports · doi:10.1016/j.btre.2016.07.002 · Cited by 54 · see citing works
Li, R., Fu, G., Liu, C., McClements, D. J., Wan, Y., Wang, S., & Liu, T. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.03.077 · Cited by 54 · see citing works
Nanoparticle-Mediated Remote Control of Enzymatic Activity
Knecht, L. D., Ali, N., Wei, Y., Hilt, J. Z., & Daunert, S. (2012) · ACS Nano · doi:10.1021/nn303308v · Cited by 54 · see citing works
Ali, Z., Tian, L., Zhang, B., Ali, N., Khan, M., & Zhang, Q. (2017) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2017.04.008 · Cited by 53 · see citing works
Gao, Z., Yi, Y., Zhao, J. Y., Xia, Y., Jiang, M., Cao, F., Zhou, H., Wei, P., Jia, H., & Yong, X. (2018) · Bioresources and Bioprocessing · doi:10.1186/s40643-018-0215-7 · Cited by 53 · see citing works
Zou, B., Song, C., Xu, X., Xia, J., Huo, S., & Cui, F. (2014) · Applied Surface Science · doi:10.1016/j.apsusc.2014.04.210 · Cited by 52 · see citing works
Gao, X., Ni, K., Zhao, C., Ren, Y., & Wei, D. (2014) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2014.07.443 · Cited by 52 · see citing works
Self-citationShikha, S., Thakur, K. G., & Bhattacharyya, M. S. (2017) · RSC Advances · doi:10.1039/c7ra06075k · Cited by 52 · see citing works
The Food Matrix and the Gastrointestinal Fluids Alter the Features of Silver Nanoparticles
Laloux, L., Kastrati, D., Cambier, S., Gutleb, A. C., & Schneider, Y. (2020) · Small · doi:10.1002/smll.201907687 · Cited by 52 · see citing works
Mehde, A. A., Mehdi, W. A., Severgün, O., Çakar, S., & Özacar, M. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.09.141 · Cited by 51 · see citing works
Ziegler-Borowska, M., Chełminiak-Dudkiewicz, D., Siódmiak, T., Sikora, A., Węgrzynowska-Drzymalska, K., Skopińska-Wiśniewska, J., Kaczmarek, H., & Marszałł, M. P. (2017) · Catalysts · doi:10.3390/catal7010026 · Cited by 50 · see citing works
Subramani, L., Annamalai, K., Parthasarathy, M., Ramalingam, K., Balasubramanian, D., & Lalvani, J. I. J. (2018) · Journal of Testing and Evaluation · doi:10.1520/jte20170246 · Cited by 50 · see citing works
Perspectives on Nanomaterials and Nanotechnology for Sustainable Bioenergy Generation
Markandan, K., & Chai, W. S. (2022) · Materials · doi:10.3390/ma15217769 · Cited by 49 · see citing works
Mulinari, J., Ambrosi, A., Feng, Y., He, Z., Huang, X., Li, Q., Luccio, M. D., Hotza, D., & de Oliveira, J. V. (2023) · Chemical Engineering Journal · doi:10.1016/j.cej.2023.141516 · Cited by 49 · see citing works
Sun, W., Yang, J., Zhu, J., Zhou, Y., Li, J., Zhu, X., Shen, M., Zhang, G., & Shi, X. (2016) · Biomaterials Science · doi:10.1039/c6bm00370b · Cited by 48 · see citing works
Immobilization of Lipase on Silver Nanoparticles via Adhesive Polydopamine for Biodiesel Production
Dumri, K., & Anh, D. H. (2014) · Enzyme Research · doi:10.1155/2014/389739 · Cited by 47 · see citing works
Upadhyay, L. S. B., & Verma, N. (2014) · Bioprocess and Biosystems Engineering · doi:10.1007/s00449-014-1191-8 · Cited by 47 · see citing works
Gebreyohannes, A. Y., Bilad, M. R., Verbiest, T., Courtin, C. M., Dornez, E., Giorno, L., Curcio, E., & Vankelecom, I. F. J. (2015) · Journal of Membrane Science · doi:10.1016/j.memsci.2015.03.069 · Cited by 46 · see citing works
Electron Paramagnetic Resonance Imaging and Spectroscopy of Polydopamine Radicals
Mrówczyński, R., Coy, E. L., Scheibe, B., Czechowski, T., Augustyniak‐Jabłokow, M. A., Jurga, S., & Tadyszak, K. (2015) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5b01524 · Cited by 45 · see citing works
Zhang, W., Tang, Y., Liu, J., Ma, Y., Jiang, L., Huang, W., Huo, F., & Tian, D. (2014) · Journal of Materials Chemistry B · doi:10.1039/c4tb01439a · Cited by 44 · see citing works
Agro-Industrial Residues and Microbial Enzymes
Madeira, J. V., Contesini, F. J., Calzado, F., Rubio, M. V., Zubieta, M. P., Lopes, D. B., & de Melo, R. R. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-803725-6.00018-2 · Cited by 44 · see citing works
Bento, H. B. S., Castro, H. F., Oliveira, P. C., & Freitas, L. (2016) · Journal of Magnetism and Magnetic Materials · doi:10.1016/j.jmmm.2016.11.061 · Cited by 44 · see citing works
Asmat, S., Husain, Q., Shoeb, M., & Mobin, M. (2020) · Materials Science and Engineering C · doi:10.1016/j.msec.2020.110883 · Cited by 43 · see citing works
Yüce‐Dursun, B., Çiğil, A. B., Dongez, D., Kahraman, M. V., Ogan, A., & Demir, S. (2016) · Journal of Molecular Catalysis B Enzymatic · doi:10.1016/j.molcatb.2016.02.007 · Cited by 42 · see citing works
Parnell, C. M., Chhetri, B. P., Brandt, A., Watanabe, F., Nima, Z. A., Mudalige, T., Biris, A. S., & Ghosh, A. (2016) · Scientific Reports · doi:10.1038/srep31415 · Cited by 42 · see citing works
Agrawal, D. C., Yadav, A., Kesarwani, R., Srivastava, O. N., & Kayastha, A. M. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.12.033 · Cited by 42 · see citing works
- Authors
- Ren, Y., Rivera, J. G., He, L., Kulkarni, H., Lee, D.-K., & Messersmith, P. B.
- Affiliations
- East China University of Science and Technology (CN)
- Northwestern University (US)
- Corresponding author
- Ren, Yuhong
- Messersmith, Phillip B
- Venue
- BMC Biotechnology
- Published
- 2011-06-08
- Volume
- 11
- Issue
- 1
- Pages
- 63-63
- ISSN
- 1472-6750 (ISSN-L)
- PMC
- PMC3212977
- OpenAlex
- W2165613512
- Cited by
- 284
- References
- 23
- Citations by year
- 2026: 4 · 2025: 8 · 2024: 21 · 2023: 13 · 2022: 14 · 2021: 12 · 2020: 16 · 2019: 19 · 2018: 25 · 2017: 22 · 2016: 38 · 2015: 25 · 2014: 29 · 2013: 20 · 2012: 16
- FWCI
- 8.71
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- BMC Biotechnology (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- eScholarship (California Digital Library) (submittedVersion, cc-by)
- Funders
- National Institutes of Health
- National Institute of Dental and Craniofacial Research (R37DE014193)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Advanced Biosensing Techniques and Applications
- Keywords
- lipase immobilization, magnetic iron oxide nanoparticles, polydopamine coating, biomimetic coatings, enzyme loading capacity, enzyme stability, magnetic separation, enzyme reusability
- MeSH terms
- Dopamine, Enzymes, Immobilized, Ferric Compounds, Hydrogen-Ion Concentration, Lipase, Polymers, Temperature, Biomimetic Materials, Magnetite Nanoparticles
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
