| Texto completo | |
| Autor(es): |
Marques Netto, Caterina G. C.
[1]
;
Andrade, Leandro H.
[1]
;
Freitas, Rafael S.
[1]
;
Toma, Henrique E.
[1]
Número total de Autores: 4
|
| Afiliação do(s) autor(es): | [1] Univ Sao Paulo, Inst Quim, BR-05508000 Sao Paulo, SP - Brazil
Número total de Afiliações: 1
|
| Tipo de documento: | Artigo Científico |
| Fonte: | Journal of Nanoscience and Nanotechnology; v. 15, n. 12, p. 9482-9487, DEC 2015. |
| Citações Web of Science: | 2 |
| Resumo | |
Alcohol dehydrogenase (ADH) from Saccharomyces cerevisiae was covalently attached, via glutaraldehyde, to magnetite nanoparticles (MagNP) previously coated with aminopropyltriethoxysilane (MagNP/APTS), or with a silica shell followed by the APTS coating (MagNP@SiO2/APTS). In both cases, a great improvement of enzymatic activity has been observed for the ethanol-acetaldehyde conversion. The MagNP@SiO2/APTS-ADH system exhibited the best stability with respect to pH and temperature. Its residual activity after 10 successive recovery cycles and 24 h storage, was maintained around 80% in comparison with 20% for the MagNP/APTS system, and a null activity for free ADH. Luminescence measurements for the immobilized enzyme indicated the occurrence of conformational changes on ADH, contributing for its improved catalytic performance. (AU) | |
| Processo FAPESP: | 09/08584-6 - Química e nanotecnologia molecular |
| Beneficiário: | Henrique Eisi Toma |
| Modalidade de apoio: | Auxílio à Pesquisa - Temático |