In this work, a simple and versatile methodology to obtain two different bioconjugated systems has been developed by the immobilization of Candida rugosa lipase (CRL) on hydrophilic gold nanoparticles functionalized with 2-diethylaminoethanethiol hydrochloride (DEA) or with sodium 3-mercapto-1-propanesulfonate (3MPS), namely Au-DEA@CRL and Au-3MPS@CRL. Both spectroscopic and morphological properties of metal nanoparticles have been deeply investigated. The enzyme loading and lipolytic activity of AuNPs@CRL bioconjugates have been studied with respect to different surface functionalization and compared with the free enzyme. Some physical and chemical parameters had a strong effect on enzyme activity and stability, that were improved in the case of the Au-DEA@CRL bioconjugate, which showed a remarkable biocatalytic performance (95% of residual lipolytic activity compared with free CRL) and stability in experimental conditions concerning pH (range 5-8) and temperature (range 20-60. °C), as often required for the industrial scale up of catalytic systems.
Venditti, I., Palocci, C., Chronopoulou, L., Fratoddi, I., Fontana, L., Diociaiuti, M., et al. (2015). Candida rugosa lipase immobilization on hydrophilic charged gold nanoparticles as promising biocatalysts: Activity and stability investigations. COLLOIDS AND SURFACES. B, BIOINTERFACES, 131, 93-101 [10.1016/j.colsurfb.2015.04.046].
Candida rugosa lipase immobilization on hydrophilic charged gold nanoparticles as promising biocatalysts: Activity and stability investigations
Venditti I.Investigation
;
2015-01-01
Abstract
In this work, a simple and versatile methodology to obtain two different bioconjugated systems has been developed by the immobilization of Candida rugosa lipase (CRL) on hydrophilic gold nanoparticles functionalized with 2-diethylaminoethanethiol hydrochloride (DEA) or with sodium 3-mercapto-1-propanesulfonate (3MPS), namely Au-DEA@CRL and Au-3MPS@CRL. Both spectroscopic and morphological properties of metal nanoparticles have been deeply investigated. The enzyme loading and lipolytic activity of AuNPs@CRL bioconjugates have been studied with respect to different surface functionalization and compared with the free enzyme. Some physical and chemical parameters had a strong effect on enzyme activity and stability, that were improved in the case of the Au-DEA@CRL bioconjugate, which showed a remarkable biocatalytic performance (95% of residual lipolytic activity compared with free CRL) and stability in experimental conditions concerning pH (range 5-8) and temperature (range 20-60. °C), as often required for the industrial scale up of catalytic systems.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
