Advertisement

Characterisation of biocatalysts immobilised in niobium—a new inorganic solid support

Authors

  • E. Aguiar-Oliveira,

    Corresponding author
    1. Faculty of Food Engineering (FEA), Department of Food Eng. (DEA), University of Campinas (UNICAMP); Campinas—São Paulo, Brazil
    • Faculty of Food Engineering (FEA), Department of Food Eng. (DEA), University of Campinas (UNICAMP); Campinas—São Paulo, Brazil.
    Search for more papers by this author
  • P. Fernandes,

    1. Centre for Biological and Chemical Engineering (CEBQ), Institute for Biotechnology and Bioengineering (IBB), Technical University of Lisbon (IST), Lisbon, Portugal
    Search for more papers by this author
  • J. M. S. Cabral,

    1. Centre for Biological and Chemical Engineering (CEBQ), Institute for Biotechnology and Bioengineering (IBB), Technical University of Lisbon (IST), Lisbon, Portugal
    Search for more papers by this author
  • F. Maugeri

    1. Faculty of Food Engineering (FEA), Department of Food Eng. (DEA), University of Campinas (UNICAMP); Campinas—São Paulo, Brazil
    Search for more papers by this author

Abstract

A new support for enzyme immobilisation, an alloy of niobium ore and graphite, was tested with: invertase from baker's yeast and inulinase from Aspergillus niger. The efficiency of immobilisation was about 30% for invertase and 72% for inulinase. The maximum activities values were observed for both enzymes at: pH 4.5, 50°C and 500 g/L of sucrose. The hydrolysis of inulin (5% w/v) by the free inulinase and invertase presented specific productivity of reducing sugars lower after immobilisation, about 15 and 1.5 times, respectively; with the hydrolysis of sucrose (50% w/v) the reductions observed were of 14 and 3.5 times, respectively. © 2012 Canadian Society for Chemical Engineering

Ancillary