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For: Rios N, Arana-peña S, Mendez-sanchez C, Ortiz C, Gonçalves L, Fernandez-lafuente R. Reuse of Lipase from Pseudomonas fluorescens via Its Step-by-Step Coimmobilization on Glyoxyl-Octyl Agarose Beads with Least Stable Lipases. Catalysts 2019;9:487. [DOI: 10.3390/catal9050487] [Cited by in Crossref: 27] [Cited by in F6Publishing: 27] [Article Influence: 9.0] [Reference Citation Analysis]
Number Citing Articles
1 Monteiro RR, de Oliveira ALB, de Menezes FL, de Souza MCM, Fechine PB, dos Santos JC. Improvement of enzymatic activity and stability of lipase A from Candida antartica onto halloysite nanotubes with Taguchi method for optimized immobilization. Applied Clay Science 2022;228:106634. [DOI: 10.1016/j.clay.2022.106634] [Cited by in Crossref: 3] [Cited by in F6Publishing: 5] [Article Influence: 3.0] [Reference Citation Analysis]
2 Choudhary P, Bhowmik A, Verma S, Srivastava S, Chakdar H, Saxena AK. Multi-substrate sequential optimization, characterization and immobilization of lipase produced by Pseudomonas plecoglossicida S7. Environ Sci Pollut Res Int 2022. [PMID: 35974269 DOI: 10.1007/s11356-022-22098-6] [Reference Citation Analysis]
3 dos Santos KP, Rios NS, Labus K, Gonçalves LRB. Co-immobilization of lipase and laccase on agarose-based supports via layer-by-layer strategy: effect of diffusional limitations. Biochemical Engineering Journal 2022. [DOI: 10.1016/j.bej.2022.108533] [Reference Citation Analysis]
4 Carballares D, Rocha-Martin J, Fernandez-Lafuente R. Chemical amination of immobilized enzymes for enzyme coimmobilization: Reuse of the most stable immobilized and modified enzyme. Int J Biol Macromol 2022;208:688-97. [PMID: 35358572 DOI: 10.1016/j.ijbiomac.2022.03.151] [Cited by in Crossref: 7] [Cited by in F6Publishing: 7] [Article Influence: 7.0] [Reference Citation Analysis]
5 Carballares D, Rocha-martin J, Fernandez-lafuente R. Preparation of a Six-Enzyme Multilayer Combi-Biocatalyst: Reuse of the Most Stable Enzymes after Inactivation of the Least Stable One. ACS Sustainable Chem Eng 2022;10:3920-34. [DOI: 10.1021/acssuschemeng.1c08180] [Cited by in Crossref: 8] [Cited by in F6Publishing: 8] [Article Influence: 8.0] [Reference Citation Analysis]
6 Arana-Peña S, Carballares D, Morellon-Sterling R, Rocha-Martin J, Fernandez-Lafuente R. The combination of covalent and ionic exchange immobilizations enables the coimmobilization on vinyl sulfone activated supports and the reuse of the most stable immobilized enzyme. Int J Biol Macromol 2022;199:51-60. [PMID: 34973984 DOI: 10.1016/j.ijbiomac.2021.12.148] [Cited by in Crossref: 11] [Cited by in F6Publishing: 12] [Article Influence: 11.0] [Reference Citation Analysis]
7 Carballares D, Rocha-Martin J, Fernandez-Lafuente R. Coimmobilization of lipases exhibiting three very different stability ranges. Reuse of the active enzymes and selective discarding of the inactivated ones. Int J Biol Macromol 2022:S0141-8130(22)00330-0. [PMID: 35218810 DOI: 10.1016/j.ijbiomac.2022.02.084] [Cited by in Crossref: 8] [Cited by in F6Publishing: 8] [Article Influence: 8.0] [Reference Citation Analysis]
8 Camelin E, Romero O, Piumetti M, Ottone C, Illanes A, Fino D. Mechanisms of interaction among enzymes and supports. Nanomaterials for Biocatalysis 2022. [DOI: 10.1016/b978-0-12-824436-4.00022-8] [Reference Citation Analysis]
9 Arana-peña S, Carballares D, Morellon-sterlling R, Berenguer-murcia Á, Alcántara AR, Rodrigues RC, Fernandez-lafuente R. Enzyme co-immobilization: Always the biocatalyst designers' choice…or not? Biotechnology Advances 2021;51:107584. [DOI: 10.1016/j.biotechadv.2020.107584] [Cited by in Crossref: 72] [Cited by in F6Publishing: 78] [Article Influence: 72.0] [Reference Citation Analysis]
10 Morellon-sterling R, Carballares D, Arana-peña S, Siar E, Braham SA, Fernandez-lafuente R. Advantages of Supports Activated with Divinyl Sulfone in Enzyme Coimmobilization: Possibility of Multipoint Covalent Immobilization of the Most Stable Enzyme and Immobilization via Ion Exchange of the Least Stable Enzyme. ACS Sustainable Chem Eng 2021;9:7508-18. [DOI: 10.1021/acssuschemeng.1c01065] [Cited by in Crossref: 19] [Cited by in F6Publishing: 22] [Article Influence: 19.0] [Reference Citation Analysis]
11 Dubey NC, Tripathi BP. Nature Inspired Multienzyme Immobilization: Strategies and Concepts. ACS Appl Bio Mater 2021;4:1077-114. [PMID: 35014469 DOI: 10.1021/acsabm.0c01293] [Cited by in Crossref: 28] [Cited by in F6Publishing: 33] [Article Influence: 28.0] [Reference Citation Analysis]
12 Arana-peña S, Carballares D, Cortés Corberan V, Fernandez-lafuente R. Multi-Combilipases: Co-Immobilizing Lipases with Very Different Stabilities Combining Immobilization via Interfacial Activation and Ion Exchange. The Reuse of the Most Stable Co-Immobilized Enzymes after Inactivation of the Least Stable Ones. Catalysts 2020;10:1207. [DOI: 10.3390/catal10101207] [Cited by in Crossref: 15] [Cited by in F6Publishing: 16] [Article Influence: 7.5] [Reference Citation Analysis]
13 Alnoch RC, Alves dos Santos L, Marques de Almeida J, Krieger N, Mateo C. Recent Trends in Biomaterials for Immobilization of Lipases for Application in Non-Conventional Media. Catalysts 2020;10:697. [DOI: 10.3390/catal10060697] [Cited by in Crossref: 21] [Cited by in F6Publishing: 22] [Article Influence: 10.5] [Reference Citation Analysis]
14 Arana-peña S, Rios NS, Mendez-sanchez C, Lokha Y, Gonçalves LR, Fernández-lafuente R. Use of polyethylenimine to produce immobilized lipase multilayers biocatalysts with very high volumetric activity using octyl-agarose beads: Avoiding enzyme release during multilayer production. Enzyme and Microbial Technology 2020;137:109535. [DOI: 10.1016/j.enzmictec.2020.109535] [Cited by in Crossref: 15] [Cited by in F6Publishing: 14] [Article Influence: 7.5] [Reference Citation Analysis]
15 Arana-peña S, Carballares D, Berenguer-murcia Á, Alcántara A, Rodrigues R, Fernandez-lafuente R. One Pot Use of Combilipases for Full Modification of Oils and Fats: Multifunctional and Heterogeneous Substrates. Catalysts 2020;10:605. [DOI: 10.3390/catal10060605] [Cited by in Crossref: 40] [Cited by in F6Publishing: 42] [Article Influence: 20.0] [Reference Citation Analysis]
16 Ahmad R, Shanahan J, Rizaldo S, Kissel DS, Stone KL. Co-immobilization of an Enzyme System on a Metal-Organic Framework to Produce a More Effective Biocatalyst. Catalysts 2020;10:499. [DOI: 10.3390/catal10050499] [Cited by in Crossref: 14] [Cited by in F6Publishing: 16] [Article Influence: 7.0] [Reference Citation Analysis]
17 Arana-peña S, Rios NS, Mendez-sanchez C, Lokha Y, Carballares D, Gonçalves LR, Fernandez-lafuente R. Coimmobilization of different lipases: Simple layer by layer enzyme spatial ordering. International Journal of Biological Macromolecules 2020;145:856-64. [DOI: 10.1016/j.ijbiomac.2019.10.087] [Cited by in Crossref: 22] [Cited by in F6Publishing: 26] [Article Influence: 11.0] [Reference Citation Analysis]
18 Zhong C, Duić B, Bolivar JM, Nidetzky B. Three‐Enzyme Phosphorylase Cascade Immobilized on Solid Support for Biocatalytic Synthesis of Cello−oligosaccharides. ChemCatChem 2020;12:1350-8. [DOI: 10.1002/cctc.201901964] [Cited by in Crossref: 21] [Cited by in F6Publishing: 21] [Article Influence: 10.5] [Reference Citation Analysis]
19 Kornecki JF, Carballares D, Tardioli PW, Rodrigues RC, Berenguer-murcia Á, Alcántara AR, Fernandez-lafuente R. Enzyme production of d -gluconic acid and glucose oxidase: successful tales of cascade reactions. Catal Sci Technol 2020;10:5740-71. [DOI: 10.1039/d0cy00819b] [Cited by in Crossref: 36] [Cited by in F6Publishing: 39] [Article Influence: 18.0] [Reference Citation Analysis]
20 Rios NS, Mendez-sanchez C, Arana-peña S, Rueda N, Ortiz C, Gonçalves LR, Fernandez-lafuente R. Immobilization of lipase from Pseudomonas fluorescens on glyoxyl-octyl-agarose beads: Improved stability and reusability. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2019;1867:741-7. [DOI: 10.1016/j.bbapap.2019.06.005] [Cited by in Crossref: 31] [Cited by in F6Publishing: 32] [Article Influence: 10.3] [Reference Citation Analysis]
21 Tacias-pascacio, Ortiz, Rueda, Berenguer-murcia, Acosta, Aranaz, Civera, Fernandez-lafuente, Alcántara. Dextran Aldehyde in Biocatalysis: More Than a Mere Immobilization System. Catalysts 2019;9:622. [DOI: 10.3390/catal9070622] [Cited by in Crossref: 25] [Cited by in F6Publishing: 25] [Article Influence: 8.3] [Reference Citation Analysis]
22 Dal Magro L, Kornecki JF, Klein MP, Rodrigues RC, Fernandez‐lafuente R. Stability/activity features of the main enzyme components of rohapect 10L. Biotechnol Prog 2019;35. [DOI: 10.1002/btpr.2877] [Cited by in Crossref: 7] [Cited by in F6Publishing: 8] [Article Influence: 2.3] [Reference Citation Analysis]