Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions
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Título: | Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions |
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Autor/es: | Rodrigues, Rafael C. | Virgen-Ortiz, Jose J. | Santos, Jose Cleiton S. dos | Berenguer-Murcia, Ángel | Alcántara, Andrés R. | Barbosa, Oveimar | Ortiz, Claudia | Fernández Lafuente, Roberto |
Grupo/s de investigación o GITE: | Materiales Carbonosos y Medio Ambiente |
Centro, Departamento o Servicio: | Universidad de Alicante. Departamento de Química Inorgánica | Universidad de Alicante. Instituto Universitario de Materiales |
Palabras clave: | Lipase interfacial activation | Lipase immobilization | Intermolecular lipase crosslinking | Heterofunctional supports | Enzyme amination | Acyl-vinylsulfone supports | Enzyme coimmobilization |
Área/s de conocimiento: | Química Inorgánica |
Fecha de publicación: | 2019 |
Editor: | Elsevier |
Cita bibliográfica: | Biotechnology Advances. 2019, 37(5): 746-770. doi:10.1016/j.biotechadv.2019.04.003 |
Resumen: | Lipases are the most widely used enzymes in biocatalysis, and the most utilized method for enzyme immobilization is using hydrophobic supports at low ionic strength. This method allows the one step immobilization, purification, stabilization, and hyperactivation of lipases, and that is the main cause of their popularity. This review focuses on these lipase immobilization supports. First, the advantages of these supports for lipase immobilization will be presented and the likeliest immobilization mechanism (interfacial activation on the support surface) will be revised. Then, its main shortcoming will be discussed: enzyme desorption under certain conditions (such as high temperature, presence of cosolvents or detergent molecules). Methods to overcome this problem include physical or chemical crosslinking of the immobilized enzyme molecules or using heterofunctional supports. Thus, supports containing hydrophobic acyl chain plus epoxy, glutaraldehyde, ionic, vinylsulfone or glyoxyl groups have been designed. This prevents enzyme desorption and improved enzyme stability, but it may have some limitations, that will be discussed and some additional solutions will be proposed (e.g., chemical amination of the enzyme to have a full covalent enzyme-support reaction). These immobilized lipases may be subject to unfolding and refolding strategies to reactivate inactivated enzymes. Finally, these biocatalysts have been used in new strategies for enzyme coimmobilization, where the most stable enzyme could be reutilized after desorption of the least stable one after its inactivation. |
Patrocinador/es: | We gratefully recognize the financial support from MINECO-Spanish Government (project number CTQ2017-86170-R), Colciencias (Colombia, project number FP 44842-076-2016), Colciencias, Ministerio de Educación Nacional, Ministerio de Industria, Comercio y Turismo e ICETEX, Convocatoria Ecosistema Científico – Colombia Científica. Fondo Francisco José de Caldas, Contract RC-FP44842-212-2018, Generalitat Valenciana (PROMETEO/2018/076), FAPERGS (project number 17/2551-0000939-8), FUNCAP (project number BP3-0139-00005.01.00/18) and CONACYT (Mexico, project number CB-2016-01, 286992). |
URI: | http://hdl.handle.net/10045/95453 |
ISSN: | 0734-9750 (Print) | 1873-1899 (Online) |
DOI: | 10.1016/j.biotechadv.2019.04.003 |
Idioma: | eng |
Tipo: | info:eu-repo/semantics/article |
Derechos: | © 2019 Elsevier Inc. |
Revisión científica: | si |
Versión del editor: | https://doi.org/10.1016/j.biotechadv.2019.04.003 |
Aparece en las colecciones: | INV - MCMA - Artículos de Revistas |
Archivos en este ítem:
Archivo | Descripción | Tamaño | Formato | |
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2019_Rodrigues_etal_BiotechAdv_final.pdf | Versión final (acceso restringido) | 4,83 MB | Adobe PDF | Abrir Solicitar una copia |
2019_Rodrigues_etal_BiotechAdv_accepted.pdf | Accepted Manuscript (acceso abierto) | 14,83 MB | Adobe PDF | Abrir Vista previa |
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