Stabilization of Candida antarctica Lipase B (CALB) Immobilized on Octyl Agarose by Treatment with Polyethyleneimine (PEI)

Autor: Sara Peirce, Veymar G. Tacias-Pascacio, Maria Elena Russo, Antonio Marzocchella, José J. Virgen-Ortíz, Roberto Fernandez-Lafuente

Publikováno v: Molecules, Vol 21, Iss 6, p 751 (2016)

Lipase B from Candida antarctica (CALB) was immobilized on octyl agarose (OC) and physically modified with polyethyleneimine (PEI) in order to confer a strong ion exchange character to the enzyme and thus enable the immobilization of other enzymes on

Externí odkaz: https://doaj.org/article/2e5d3b4aeebc4a7797adfc55fc886196

Reuse of anion exchangers as supports for enzyme immobilization: Reinforcement of the enzyme-support multiinteraction after enzyme inactivation

Autor: Vicente Cortes-Corberan, Maria Russo, Antonio Marzocchella, Roberto Fernandez-Lafuente, Sara Peirce, Veymar G. Tacias-Pascacio, Jose J. Virgen-Ortíz

Publikováno v: Process biochemistry (1991) 51 (2016): 1391–1396. doi:10.1016/j.procbio.2016.06.020
info:cnr-pdr/source/autori:Virgen-Ortiz, Jose J.; Peirce, Sara; Tacias-Pascacio, Veymar G.; Cortes-Corberan, Vicente; Marzocchella, Antonio; Russo, Maria Elena; Fernandez-Lafuente, Roberto/titolo:Reuse of anion exchangers as supports for enzyme immobilization: Reinforcement of the enzyme-support multiinteraction after enzyme inactivation/doi:10.1016%2Fj.procbio.2016.06.020/rivista:Process biochemistry (1991)/anno:2016/pagina_da:1391/pagina_a:1396/intervallo_pagine:1391–1396/volume:51

beta-Galactosidase from Aspergillus oryze has been immobilized on agarose beads coated with polyethyleneimine. The fresh enzyme was released from the support using 500 mM NaCl at pH 7. After thermal inactivation or inactivation in the presence of org

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::26da964fa5624b4c71b15ca8822d714d
https://doi.org/10.1016/j.procbio.2016.06.020

Comparison between carbonic anhydrase biocatalysts for CO2 capture by enzymatic reactive absorption

Autor: Maria Elena Russo, Sara Peirce, Sonia Del Prete, Clemente Capasso, Antonio Marzocchella, Piero Salatino

Publikováno v: the 12th European Congress of Chemical Engineering, the 5th European Congress of Applied Biotechnology, Firenze, Italy, 15/09/2019, 19/09/2019
info:cnr-pdr/source/autori:Maria Elena Russo, Sara Peirce, Sonia Del Prete, Clemente Capasso, Antonio Marzocchella, Piero Salatino/congresso_nome:the 12th European Congress of Chemical Engineering, the 5th European Congress of Applied Biotechnology/congresso_luogo:Firenze, Italy/congresso_data:15%2F09%2F2019, 19%2F09%2F2019/anno:2019/pagina_da:/pagina_a:/intervallo_pagine

1. Introduction Post-combustion CO2 capture strategy asks for novel processes avoiding the use of polluting solvents and aimed at CO2 utilization. CO2 absorption processes based on the enhancement of capture rate by the enzyme carbonic anhydrase (CA)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=cnr_________::132f5d5940e0b1bf52f9692a3e3180b1
http://www.cnr.it/prodotto/i/411104

Kinetic characterization of carbonic anhydrase immobilized on magnetic nanoparticles as biocatalyst for CO2 capture

Autor: Antonio Marzocchella, Sara Peirce, Roberto Fernandez-Lafuente, Piero Salatino, Maria Russo, Rosa Perfetto, Clemente Capasso, Mosè Rossi

Publikováno v: Biochemical engineering journal 138 (2018): 1–11. doi:10.1016/j.bej.2018.06.017
info:cnr-pdr/source/autori:Peirce S.*, Russo M.E.**, Perfetto R***, Capasso C***, Rossi M***, Fernandez-Lafuente R****, Salatino P*, Marzocchella A */titolo:Kinetic characterization of carbonic anhydrase immobilized on magnetic nanoparticles as biocatalyst for CO2 capture/doi:10.1016%2Fj.bej.2018.06.017/rivista:Biochemical engineering journal/anno:2018/pagina_da:1/pagina_a:11/intervallo_pagine:1–11/volume:138

Carbon dioxide absorption into carbonate solutions promoted by the enzyme carbonic anhydrase (CA, E.C. 4.2.1.1) has been proposed as potential technology for CO2 capture. The use of solid CA-based biocatalysts allows the enzyme recovery and reuse und

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61b158b6e4bf197077acd012a9f008fc
http://hdl.handle.net/11588/722168

Stabilization of Candida antarctica Lipase B (CALB) immobilized on octyl agarose by treatment with polyethyleneimine (PEI)

Autor: Antonio Marzocchella, Sara Peirce, Roberto Fernandez-Lafuente, Veymar G. Tacias-Pascacio, Jose J. Virgen-Ortíz, Maria Russo

Publikováno v: Molecules (Basel, Online) 21 (2016). doi:10.3390/molecules21060751
info:cnr-pdr/source/autori:Peirce S.; Tacias-Pascacio V.G.; Russo M.E.; Marzocchella A.; Virgen-Ortiz J.J.; Fernandez-Lafuente R./titolo:Stabilization of Candida antarctica Lipase B (CALB) immobilized on octyl agarose by treatment with polyethyleneimine (PEI)/doi:10.3390%2Fmolecules21060751/rivista:Molecules (Basel, Online)/anno:2016/pagina_da:/pagina_a:/intervallo_pagine:/volume:21
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Molecules; Volume 21; Issue 6; Pages: 751
Molecules, Vol 21, Iss 6, p 751 (2016)
Molecules

Lipase B from Candida antarctica (CALB) was immobilized on octyl agarose (OC) and physically modified with polyethyleneimine (PEI) in order to confer a strong ion exchange character to the enzyme and thus enable the immobilization of other enzymes on

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::542ac9163ed272d4f52039f7391ef1c6
http://www.scopus.com/inward/record.url?eid=2-s2.0-84976386594&partnerID=q2rCbXpz