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Carbon nanotubes as supports for inulinase immobilization.
Garlet, Tais B; Weber, Caroline T; Klaic, Rodrigo; Foletto, Edson L; Jahn, Sergio L; Mazutti, Marcio A; Kuhn, Raquel C.
Afiliação
  • Garlet TB; Department of Chemical Engineering, Federal University of Santa Maria, 97105-900 Santa Maria, Brazil.
  • Weber CT; Department of Chemical Engineering, Federal University of Santa Maria, 97105-900 Santa Maria, Brazil.
  • Klaic R; Department of Chemical Engineering, Federal University of Santa Maria, 97105-900 Santa Maria, Brazil.
  • Foletto EL; Department of Chemical Engineering, Federal University of Santa Maria, 97105-900 Santa Maria, Brazil.
  • Jahn SL; Department of Chemical Engineering, Federal University of Santa Maria, 97105-900 Santa Maria, Brazil.
  • Mazutti MA; Department of Chemical Engineering, Federal University of Santa Maria, 97105-900 Santa Maria, Brazil. marciomazutti@gmail.com.
  • Kuhn RC; Department of Chemical Engineering, Federal University of Santa Maria, 97105-900 Santa Maria, Brazil.
Molecules ; 19(9): 14615-24, 2014 Sep 15.
Article em En | MEDLINE | ID: mdl-25225722
The commercial inulinase obtained from Aspergillus niger was non-covalently immobilized on multiwalled carbon nanotubes (MWNT-COOH). The immobilization conditions for the carbon nanotubes were defined by the central composite rotational design (CCRD). The effects of enzyme concentration (0.8%-1.7% v/v) and adsorbent:adsorbate ratio (1:460-1:175) on the enzyme immobilization were studied. The adsorbent:adsorbate ratio variable has positive effect and the enzyme concentration has a negative effect on the inulinase immobilization (U/g) response at the 90% significance level. These results show that the lower the enzyme concentration and the higher the adsorbent:adsorbate ratio, better is the immobilization. According to the results, it is possible to observe that the carbon nanotubes present an effective inulinase adsorption. Fast adsorption in about six minutes and a loading capacity of 51,047 U/g support using a 1.3% (v/v) inulinase concentration and a 1:460 adsorbent:adsorbate ratio was observed. The effects of temperature on the immobilized enzyme activity were evaluated, showing better activity at 50 °C. The immobilized enzyme maintained 100% of its activity during five weeks at room temperature. The immobilization strategy with MWNT-COOH was defined by the experimental design, showing that inulinase immobilization is a promising biotechnological application of carbon nanotubes.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Aspergillus niger / Nanotubos de Carbono / Enzimas Imobilizadas / Glicosídeo Hidrolases Idioma: En Revista: Molecules Assunto da revista: BIOLOGIA Ano de publicação: 2014 Tipo de documento: Article País de afiliação: Brasil País de publicação: Suíça

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Aspergillus niger / Nanotubos de Carbono / Enzimas Imobilizadas / Glicosídeo Hidrolases Idioma: En Revista: Molecules Assunto da revista: BIOLOGIA Ano de publicação: 2014 Tipo de documento: Article País de afiliação: Brasil País de publicação: Suíça