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Soluble lipase from Thermomyces lanuginosa (TLL) was dramatically hyper-activated by a cationic surfactant, cetyltrimethylammonium bromide (CTAB). The greatest hyperactivation (above 340-fold) was observed with 0.005% CTAB. In addition to that, very high hyperactivation was also observed with much higher concentrations of surfactant (100-fold in the presence of 0.3% CTAB). Without surfactant or with very low surfactant concentrations, TLL was not adsorbed to the cationic exchangers. However, in the presence of high concentrations of surfactant (0.3%), the lipase was completely and strongly adsorbed on sulfopropyl-sepharose. The adsorbed enzyme remained hyperactivated (80-fold more active than the soluble enzyme) after elimination of the excess of surfactant. Complete desorption of the hyperactivated TLL from the cationic exchanger is only achieved at 2 M NaCl. The same level of hyperactivation was observed for the hydrolysis of a large substrate: fish oil. The release of EPA (eicosapentaenoic acid) was 80-fold more rapid with hyperactivated TLL derivatives than with TLL very mildly immobilized on CNBr activated agarose. Hyperactivated derivatives were very stable at 25 °C and 37 °C. Full activity was preserved after 1 week.

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Digital.CSIC  

Autor(es)

Moreno -  Pérez, Sonia -  Ghattas, Nesrine -  Filice, Marco -  Guisán, José Manuel -  Fernández -  Lorente, Gloria - 

Id.: 70043391

Idioma: eng  - 

Versión: 1.0

Estado: Final

Palabras claveNovel hyperactivated lipase derivatives - 

Tipo de recurso: Artículo  - 

Tipo de Interactividad: Expositivo

Nivel de Interactividad: muy bajo

Audiencia: Estudiante  -  Profesor  -  Autor  - 

Estructura: Atomic

Coste: no

Copyright: sí

: closedAccess

Requerimientos técnicos:  Browser: Any - 

Relación: [References] Sí

Fecha de contribución: 19-dic-2017

Contacto:

Localización:
* doi: 10.1016/j.molcatb.2015.08.015
* issn: 1381-1177
* e-issn: 1873-3158
* Journal of Molecular Catalysis B: Enzymatic 122: 199-203 (2015)
* 10.1016/j.molcatb.2015.08.015

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