| Autor: |
Kisukuri CM; Laboratório de Química Fina e Biocatálise and ‡GrAND - Grupo para o Avanço no Design de Nanomateriais, Instituto de Química, Universidade de São Paulo , Av. Prof. Lineu Prestes 748, SP 05508-900 São Paulo, Brazil., Macedo A, Oliveira CC, Camargo PH, Andrade LH |
| Jazyk: |
angličtina |
| Zdroj: |
Langmuir : the ACS journal of surfaces and colloids [Langmuir] 2013 Dec 23; Vol. 29 (51), pp. 15974-80. Date of Electronic Publication: 2013 Dec 13. |
| DOI: |
10.1021/la404081n |
| Abstrakt: |
We employed thiol-funcionalized AgAu nanoshells (AgAu NSs) as supports for the covalent attachment of lipases (BCL, Burkholderia cepacia lipase; PPL, pancreatic porcine lipase). Specifically, we were interested in investigating the effect of the nature/size of the spacer in AgAu NSs-functionalized organic thiols over the covalent attachment of lipases. The catalytic performance of AgAu-lipase systems was measured in the kinetic resolution of (R,S)-1-(phenyl)ethanol via a transesterification reaction. In comparison to free BCL, the lipase attached to AgAu NSs using a small spacer such as cysteamine or mercaptoacetic acid, with the largest spacer mercaptoundecanoic acid, had the fastest conversion rate. The recycling potential for BCL was investigated. After three reaction cycles, the enzyme activity was kept at around 90% of the initial value. The results described herein show that the size of the spacer plays an important role in optimizing lipase activities in metallic nanoshells as solid supports. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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