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Immobilization of laccase of Pycnoporus sanguineus CS43.
Gonzalez-Coronel, Luis A; Cobas, Marta; Rostro-Alanis, Magdalena de J; Parra-Saldívar, Roberto; Hernandez-Luna, Carlos; Pazos, Marta; Sanromán, M Ángeles.
Afiliación
  • Gonzalez-Coronel LA; Tecnológico de Monterrey, Escuela de Ingeniería y Ciencias, Campus Monterrey, Ave. Eugenio Garza Sada 2501, Monterrey, N.L., 64849, Mexico.
  • Cobas M; Department of Chemical Engineering, University of Vigo, Campus As Lagoas, Marcosende 36310 Vigo, Spain.
  • Rostro-Alanis MJ; Tecnológico de Monterrey, Escuela de Ingeniería y Ciencias, Campus Monterrey, Ave. Eugenio Garza Sada 2501, Monterrey, N.L., 64849, Mexico.
  • Parra-Saldívar R; Tecnológico de Monterrey, Escuela de Ingeniería y Ciencias, Campus Monterrey, Ave. Eugenio Garza Sada 2501, Monterrey, N.L., 64849, Mexico.
  • Hernandez-Luna C; Laboratorio de Enzimología, Facultad de Ciencias Biológicas, Universidad Autónoma de Nuevo León, Ave. Pedro de Alba S/N Ciudad Universitaria, San Nicolás de los Garza, Nuevo León, C.P. 64450, Mexico.
  • Pazos M; Department of Chemical Engineering, University of Vigo, Campus As Lagoas, Marcosende 36310 Vigo, Spain.
  • Sanromán MÁ; Department of Chemical Engineering, University of Vigo, Campus As Lagoas, Marcosende 36310 Vigo, Spain. Electronic address: sanroman@uvigo.es.
N Biotechnol ; 39(Pt A): 141-149, 2017 Oct 25.
Article en En | MEDLINE | ID: mdl-28011289
Laccase from Pycnoporus sanguineus CS43 was successfully immobilized onto Immobead-150 and Eupergit-C by covalent binding and by entrapment in LentiKats. The highest immobilization was onto Immobead-150 (97.1±1.2%) compared to the other supports, LentiKats (89±1.1%) and Eupergit-C (83.2±1.4%). All three immobilized enzyme systems showed increased thermostability and better mechanical properties than free laccase. Moreover, after 5 cycles of reuse of these systems, 90% of initial laccase activity was retained. Immobead-150 and LentiKats systems exhibited the highest efficiencies in removal of m-cresol under the combined actions of biodegradation and adsorption, while laccase entrapped in LentiKats showed a high ability for degradation of m-cresol within 24h. In addition, the typical Michaelis-Menten enzymatic model effectively described the kinetic profile of m-cresol degradation by the enzyme entrapped in LentiKats. Based on the results obtained in the present study, it can be established that the immobilized biocatalysts developed here possess significant potential for wastewater treatment.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Lacasa / Enzimas Inmovilizadas / Pycnoporus Idioma: En Revista: N Biotechnol Asunto de la revista: BIOLOGIA MOLECULAR / ENGENHARIA BIOMEDICA Año: 2017 Tipo del documento: Article País de afiliación: México Pais de publicación: Países Bajos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Lacasa / Enzimas Inmovilizadas / Pycnoporus Idioma: En Revista: N Biotechnol Asunto de la revista: BIOLOGIA MOLECULAR / ENGENHARIA BIOMEDICA Año: 2017 Tipo del documento: Article País de afiliación: México Pais de publicación: Países Bajos