New trends in industrial biocatalysis
The “manufacture and modification” of molecules in nature are catalyzed by enzymes with exquisite selectivity, unparalleled rate acceleration and under “mild” reaction conditions. Nowadays, enzyme-catalyzed synthesis is an attractive and eco-friendly alternative to the traditional multi-step and con...
- Autores:
-
Fernández, Lucas Jesús
- Tipo de recurso:
- Article of journal
- Fecha de publicación:
- 2021
- Institución:
- Corporación Universidad de la Costa
- Repositorio:
- REDICUC - Repositorio CUC
- Idioma:
- eng
- OAI Identifier:
- oai:repositorio.cuc.edu.co:11323/8787
- Acceso en línea:
- https://hdl.handle.net/11323/8787
https://repositorio.cuc.edu.co/
- Palabra clave:
- industrial
biocatalysis
- Rights
- embargoedAccess
- License
- CC0 1.0 Universal
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dc.title.spa.fl_str_mv |
New trends in industrial biocatalysis |
title |
New trends in industrial biocatalysis |
spellingShingle |
New trends in industrial biocatalysis industrial biocatalysis |
title_short |
New trends in industrial biocatalysis |
title_full |
New trends in industrial biocatalysis |
title_fullStr |
New trends in industrial biocatalysis |
title_full_unstemmed |
New trends in industrial biocatalysis |
title_sort |
New trends in industrial biocatalysis |
dc.creator.fl_str_mv |
Fernández, Lucas Jesús |
dc.contributor.author.spa.fl_str_mv |
Fernández, Lucas Jesús |
dc.subject.spa.fl_str_mv |
industrial biocatalysis |
topic |
industrial biocatalysis |
description |
The “manufacture and modification” of molecules in nature are catalyzed by enzymes with exquisite selectivity, unparalleled rate acceleration and under “mild” reaction conditions. Nowadays, enzyme-catalyzed synthesis is an attractive and eco-friendly alternative to the traditional multi-step and contaminating chemical processes. |
publishDate |
2021 |
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2021-10-08T20:53:14Z |
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2021-10-08T20:53:14Z |
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2021 |
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2022-11-01 |
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Artículo de revista |
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07349750 |
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https://hdl.handle.net/11323/8787 |
dc.identifier.doi.spa.fl_str_mv |
10.1016/j.biotechadv.2021.107782 |
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Corporación Universidad de la Costa |
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eng |
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eng |
dc.relation.references.spa.fl_str_mv |
Arana-Pena, ˜ S., Carballares, D., Morellon-Sterlling, R., Berenguer-Murcia, A., ´ Alc´ antara, A.R., Rodrigues, R.C., Fernandez-Lafuente, R., 2021. Enzyme coimmobilization: always the biocatalyst designers’ choice… or not? Biotechnol. Adv. 107584 https://doi.org/10.1016/j.biotechadv.2020.107584. Aranda, C., Carro, J., Gonzalez-Benjumea, ´ A., Babot, E.D., Olmedo, A., Linde, D., Martínez, A.T., Guti´errez, A., 2021. Advances in enzymatic oxyfunctionalization of aliphatic compounds. Biotechnol. Adv. 107703 https://doi.org/10.1016/j. biotechadv.2021.107703. Del Arco, J., Acosta, J., Fern´ andez-Lucas, J., 2021. New trends in the biocatalytic production of nucleosidic active pharmaceutical ingredients using 2′ -deoxyribosyltransferases. Biotechnol. Adv. 107701 https://doi.org/10.1016/j. biotechadv.2021.107701. Fern´ andez-Lucas, J., Camarasa, M.-J. (Eds.), 2018. Enzymatic and Chemical Synthesis of Nucleic Acid Derivatives. John Wiley & Sons. https://doi.org/10.1002/ 9783527812103. Fryszkowska, A., Devine, P.N., 2020. Biocatalysis in drug discovery and development. Curr. Opin. Chem. Biol. 55, 151–160. https://doi.org/10.1016/j.cbpa.2020.01.012. Gkantzou, E., Chatzikonstantinou, A.V., Fotiadou, R., Giannakopoulou, A., Patila, M., Stamatis, H., 2021. Trends in the development of innovative nanobiocatalysts and their application in biocatalytic transformations. Biotechnol. Adv. 107738. htt ps://www.sciencedirect.com/science/article/abs/pii/S0734975021000446. Hobisch, M., Holtmann, D., de Santos, P.G., Alcalde, M., Hollmann, F., Kara, S., 2021. Recent developments in the use of peroxygenases–exploring their high potential in selective oxyfunctionalisations. Biotechnol. Adv. 107615. https://www.sciencedirec t.com/science/article/pii/S0734975020301178. M´esz´ aros, Z., Nekvasilov´ a, P., Bojarova, ´ P., Kˇren, V., Sl´ amova, ´ K., 2021. Advanced glycosidases as ingenious biosynthetic instruments. Biotechnol. Adv. 107733 https:// doi.org/10.1016/j.biotechadv.2021.107733. Nobile, ´ M.L., Stricker, A.M., Marchesano, L., Iribarren, A.M., Lewkowicz, E.S., 2021. Noxygenation of amino compounds: early stages in its application to the biocatalyzed preparation of bioactive compounds. Biotechnol. Adv. 107726 https://doi.org/ 10.1016/j.biotechadv.2021.107726. Paul, C.E., Eggerichs, D., Westphal, A.H., Tischler, D., van Berkel, W.J., 2021. Flavoprotein monooxygenases: versatile biocatalysts. Biotechnol. Adv. 107712. https:// www.sciencedirect.com/science/article/pii/S0734975021000185. Savino, S., Fraaije, M.W., 2021. The vast repertoire of carbohydrate oxidases: an overview. Biotechnol. Adv. 107634. https://www.sciencedirect.com/science/article/pii/ S0734975020301361. Sheldon, R.A., 2012. Fundamentals of green chemistry: efficiency in reaction design. Chem. Soc. Rev. 41 (4), 1437–1451. https://doi.org/10.1039/c1cs15219j. Wohlgemuth, R., 2021. Biocatalysis–key enabling tools from biocatalytic one-step and multi-step reactions to biocatalytic total synthesis. New Biotechnol. 60, 113–123. https://www.sciencedirect.com/science/article/pii/S1871678420301722. Wu, S., Snajdrova, R., Moore, J.C., Baldenius, K., Bornscheuer, U.T., 2021. Biocatalysis: enzymatic synthesis for industrial applications. Angew. Chem. Int. 60 (1), 88–119. https://doi.org/10.1002/anie.202006648. Xu, P., Liang, S., Zong, M.H., Lou, W.Y., 2021. Ionic liquids for regulating biocatalytic process: achievements and perspectives. Biotechnol. Adv. 107702. https://www.sc iencedirect.com/science/article/abs/pii/S0734975021000082?via%3Dihub. |
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Fernández, Lucas Jesús2021-10-08T20:53:14Z2021-10-08T20:53:14Z20212022-11-0107349750https://hdl.handle.net/11323/878710.1016/j.biotechadv.2021.107782Corporación Universidad de la CostaREDICUC - Repositorio CUChttps://repositorio.cuc.edu.co/The “manufacture and modification” of molecules in nature are catalyzed by enzymes with exquisite selectivity, unparalleled rate acceleration and under “mild” reaction conditions. Nowadays, enzyme-catalyzed synthesis is an attractive and eco-friendly alternative to the traditional multi-step and contaminating chemical processes.Fernández, Lucas Jesúsapplication/pdfengBiotechnology AdvancesCC0 1.0 Universalhttp://creativecommons.org/publicdomain/zero/1.0/info:eu-repo/semantics/embargoedAccesshttp://purl.org/coar/access_right/c_f1cfindustrialbiocatalysisNew trends in industrial biocatalysisArtículo de revistahttp://purl.org/coar/resource_type/c_6501http://purl.org/coar/resource_type/c_2df8fbb1Textinfo:eu-repo/semantics/articlehttp://purl.org/redcol/resource_type/ARTinfo:eu-repo/semantics/acceptedVersionhttps://pubmed.ncbi.nlm.nih.gov/34062245/https://pubmed.ncbi.nlm.nih.gov/34062245/Arana-Pena, ˜ S., Carballares, D., Morellon-Sterlling, R., Berenguer-Murcia, A., ´ Alc´ antara, A.R., Rodrigues, R.C., Fernandez-Lafuente, R., 2021. Enzyme coimmobilization: always the biocatalyst designers’ choice… or not? Biotechnol. Adv. 107584 https://doi.org/10.1016/j.biotechadv.2020.107584.Aranda, C., Carro, J., Gonzalez-Benjumea, ´ A., Babot, E.D., Olmedo, A., Linde, D., Martínez, A.T., Guti´errez, A., 2021. Advances in enzymatic oxyfunctionalization of aliphatic compounds. Biotechnol. Adv. 107703 https://doi.org/10.1016/j. biotechadv.2021.107703.Del Arco, J., Acosta, J., Fern´ andez-Lucas, J., 2021. New trends in the biocatalytic production of nucleosidic active pharmaceutical ingredients using 2′ -deoxyribosyltransferases. Biotechnol. Adv. 107701 https://doi.org/10.1016/j. biotechadv.2021.107701.Fern´ andez-Lucas, J., Camarasa, M.-J. (Eds.), 2018. Enzymatic and Chemical Synthesis of Nucleic Acid Derivatives. John Wiley & Sons. https://doi.org/10.1002/ 9783527812103.Fryszkowska, A., Devine, P.N., 2020. Biocatalysis in drug discovery and development. Curr. Opin. Chem. Biol. 55, 151–160. https://doi.org/10.1016/j.cbpa.2020.01.012.Gkantzou, E., Chatzikonstantinou, A.V., Fotiadou, R., Giannakopoulou, A., Patila, M., Stamatis, H., 2021. Trends in the development of innovative nanobiocatalysts and their application in biocatalytic transformations. Biotechnol. Adv. 107738. htt ps://www.sciencedirect.com/science/article/abs/pii/S0734975021000446.Hobisch, M., Holtmann, D., de Santos, P.G., Alcalde, M., Hollmann, F., Kara, S., 2021. Recent developments in the use of peroxygenases–exploring their high potential in selective oxyfunctionalisations. Biotechnol. Adv. 107615. https://www.sciencedirec t.com/science/article/pii/S0734975020301178.M´esz´ aros, Z., Nekvasilov´ a, P., Bojarova, ´ P., Kˇren, V., Sl´ amova, ´ K., 2021. Advanced glycosidases as ingenious biosynthetic instruments. Biotechnol. Adv. 107733 https:// doi.org/10.1016/j.biotechadv.2021.107733.Nobile, ´ M.L., Stricker, A.M., Marchesano, L., Iribarren, A.M., Lewkowicz, E.S., 2021. Noxygenation of amino compounds: early stages in its application to the biocatalyzed preparation of bioactive compounds. Biotechnol. Adv. 107726 https://doi.org/ 10.1016/j.biotechadv.2021.107726.Paul, C.E., Eggerichs, D., Westphal, A.H., Tischler, D., van Berkel, W.J., 2021. Flavoprotein monooxygenases: versatile biocatalysts. Biotechnol. Adv. 107712. https:// www.sciencedirect.com/science/article/pii/S0734975021000185.Savino, S., Fraaije, M.W., 2021. The vast repertoire of carbohydrate oxidases: an overview. Biotechnol. Adv. 107634. https://www.sciencedirect.com/science/article/pii/ S0734975020301361.Sheldon, R.A., 2012. Fundamentals of green chemistry: efficiency in reaction design. Chem. Soc. Rev. 41 (4), 1437–1451. https://doi.org/10.1039/c1cs15219j.Wohlgemuth, R., 2021. Biocatalysis–key enabling tools from biocatalytic one-step and multi-step reactions to biocatalytic total synthesis. New Biotechnol. 60, 113–123. https://www.sciencedirect.com/science/article/pii/S1871678420301722.Wu, S., Snajdrova, R., Moore, J.C., Baldenius, K., Bornscheuer, U.T., 2021. Biocatalysis: enzymatic synthesis for industrial applications. Angew. Chem. Int. 60 (1), 88–119. https://doi.org/10.1002/anie.202006648.Xu, P., Liang, S., Zong, M.H., Lou, W.Y., 2021. Ionic liquids for regulating biocatalytic process: achievements and perspectives. Biotechnol. 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