Characterisation of biocatalysts immobilised in niobium—a new inorganic solid support. (14th February 2012)

• Record Type: Journal Article
• Authors: Aguiar‐Oliveira, E.; Fernandes, P.; Cabral, J. M. S.; Maugeri, F.
• Is Part Of: Canadian journal of chemical engineering. Volume 91:Number 3(2013)
• Page Start: 432
• Page End: 440
• Publication Date: 2012-02-14
• Subjects: Chemical engineering -- Periodicals; Technology -- Periodicals; 660.05
• DOI: 10.1002/cjce.21653
• Languages: English
• ISSNs: 0008-4034

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>A new support for enzyme immobilisation, an alloy of niobium ore and graphite, was tested with: invertase from baker's yeast and inulinase from <italic>Aspergillus niger</italic>. 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</p> </abstract>