Candida rugosa lipase immobilization on hydrophilic charged gold nanoparticles as promising biocatalysts: Activity and stability investigations

被引：50
作者：
Venditti, Iole [1 ]
Palocci, Cleofe [1 ]
Chronopoulou, Laura [1 ]
Fratoddi, Ilaria [1 ,2 ]
Fontana, Laura [1 ]
Diociaiuti, Marco [3 ]
Russo, Maria Vittoria [1 ,4 ]
机构：
[1] Univ Roma La Sapienza, Dept Chem, I-00185 Rome, Italy
[2] Univ Roma La Sapienza, Ctr Nanotechnol Engn CNIS, I-00185 Rome, Italy
[3] Ist Super Sanita, Technol & Hlth Dept, I-00161 Rome, Italy
[4] Univ Roma La Sapienza, Ctr Protect Environm & Cultural Heritages CIABC, I-00185 Rome, Italy
来源：
COLLOIDS AND SURFACES B-BIOINTERFACES | 2015年 / 131卷
关键词：
Gold nanoparticles; Candida rugosa lipase; Lipase immobilization; Biocatalysis; PH-INDUCED AGGREGATION; SILVER NANOPARTICLES; KINETIC RESOLUTION; TRANSESTERIFICATION; NANOSPHERES; BIODIESEL; DELIVERY; ENZYMES; HYBRIDS;
D O I：
10.1016/j.colsurfb.2015.04.046
中图分类号：
Q6 [生物物理学];
学科分类号：
071011 ;
摘要：
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 bio conjugates 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 degrees C), as often required for the industrial scale up of catalytic systems. (C) 2015 Elsevier B.V. All rights reserved.
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收藏
页码：93 / 101
页数：9
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