Association of Yeast Alcohol Dehydrogenase with Superparamagnetic Nanoparticles: Improving the Enzyme Stability and Performance

Autor(es)

Marques Netto, Caterina G. C. ^[1] ; Andrade, Leandro H. ^[1] ; Freitas, Rafael S. ^[1] ; Toma, Henrique E. ^[1]

Afiliação do(s) autor(es)

^[1] Univ Sao Paulo, Inst Quim, BR-05508000 Sao Paulo, SP - Brazil

• 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